Researcher Profile and Settings

Affiliation

• Faculty of Fisheries Sciences　Marine Life Science　Marine Chemical Resource Development

Job Title

• Professor

J-Global ID

• 200901074821838411

Research Interests

• 褐藻類   マコンブ   red algae   dulse   ツルシラモ   ウップルイノリ   岩のり   ウミゾウメン   アカバギンナンソウ   クロハギンナンソウ   クシベニヒバ   カギケノリ   核ゲノム   葉緑体ゲノム   ミトコンドリアゲノム   Phycobili Protein   フィコビリソーム   立体構造解析   キシラン   キシロオリゴ糖   フノラン   多糖類分解酵素   マイコスポリン様アミノ酸   フェリチン   超臨界二酸化炭素   亜臨界水   antioxidative effect   antihypertension   antidiabetic   フコイダン   ヘモシアニン   Trypsin Inhibitor   ヒトデ   ホスホリパーゼA2   3重ラセンコラーゲン   Collagen Peptide   Trypsin   キモトリプシン   ペプシン   Environmental Adaptation   温度安定性   Enzymology   Utilization of Marine Products   Fisheries Chemistry(6302)   

Research Areas

• Life sciences / Marine/Aquatic life sciences

Educational Organization

•  Bachelor's degree program　School of Fisheries Sciences
•  Master's degree program　Graduate School of Fisheries Sciences
•  Doctoral (PhD) degree program　Graduate School of Fisheries Sciences

Academic & Professional Experience

• 2017/04 - Today Hokkaido University Faculty of Fisheries Sciences
• 2007/04 - 2017/03 Hokkaido University Faculty of Fisheries Sciences
• 2005/04 - 2007/03 Hokkaido University Faculty of Fisheries Sciences
• 2002/04 - 2005/03 Hokkaido University
• 1987/12 - 2002/03 Hokkaido University School of Fisheries Sciences

Education

• 1987/04 - 1987/12  Hokkaido University
• 1985/04 - 1987/03  Hokkaido University
• 1981/04 - 1985/03  Hokkaido University  School of Fisheries Sciences
• 1978/04 - 1980/03  国立京都教育大学教育学部附属高等学校

Association Memberships

• 日本応用藻類学会   JAPAN SOCIETY OF NUTRITION AND FOOD SCIENCE   日本農芸化学会   マリンバイオテクノロジー学会   日本水産学会   

Research Activities

Published Papers

• Extraction and antioxidant capacity of mycosporine-like amino acids from red algae in Japan

  R.Yamamoto, S.Toriumi, C.Kawagoe, W.Saburi, H.Kishimura, Y.Kumagai

  Bioscience, Biotechnology, and Biochemistry 2024/04 [Refereed][Not invited]
  
• Understanding Antidiabetic Potential of Oligosaccharides from 2 Red Alga Dulse Devaleraea inkyuleei Xylan by Investigating α- 3 Amylase and α-Glucosidase Inhibition

  Martin Alain Mune Mune, Tadashi Hatanaka, Hideki Kishimura, Yuya Kumagai

  Molecules [IF=4.6] 29 2024/04 [Refereed][Not invited]
  
• Mycosporine-like Amino Acids from Red Alga Dulse (Devaleraea inkyuleei): Monthly Variation and Improvement in Extraction

  R.Yamamoto, K.Takizawa, Y.Miyabe, M.M.M.Alain, H.Kishimura, Y. Kumagai

  Phycology [TC=1] 2023/09 [Refereed][Not invited]
  
• 紅藻ダルスの成分特性について

  岸村栄毅

  Algal Resources 16 (1) 49 - 54 2023/07 [Not refereed][Invited]
  
• 海藻レトルト食品の栄養成分および抗酸化力に及ぼす製造条件の影響

  宮部好克, 落合瞳子, 熊谷祐也, 岸村栄毅

  日本調理科学会誌 [IF=0.206] 2023/06 [Refereed][Not invited]
  
• Exploring Bioactive Compounds in Brown Seaweeds Using Subcritical Water: A Comprehensive Analysis

  Jin-Seok Park, Ji-Min Han, Yu-Na Shin, Ye-Seul Park, Ye-Ryeon Shin, Sin-Won Park, Vikash Chandra Roy, Hee-Jeong Lee, Yuya Kumagai, Hideki Kishimura, Byung-Soo Chun

  Marine Drugs [IF=6.085] [TC=8} 21 (6) 328 - 328 2023/05/26 [Refereed][Not invited]
   

  In this study, we characterized the bioactive properties of three important brown seaweed species, Sargassum thunbergii, Undaria pinnatifida, and Saccharina japonica, by subcritical water extraction (SWE), as these species are well known for their beneficial health effects. Their physiochemical properties, including potential antioxidant, antihypertensive, and α-glucosidase inhibitory activity, and the antibacterial activity of the hydroysates were also analyzed. The highest total phlorotannin, total sugar content, and reducing sugar content in the S. thunbergii hydrolysates were 38.82 ± 0.17 mg PGE/g, 116.66 ± 0.19 mg glucose/g dry sample, and 53.27 ± 1.57 mg glucose/g dry sample, respectively. The highest ABTS+ and DPPH antioxidant activities were obtained in the S. japonica hydrolysates (124.77 ± 2.47 and 46.35 ± 0.01 mg Trolox equivalent/g, respectively) and the highest FRAP activity was obtained in the S. thunbergii hydrolysates (34.47 ± 0.49 mg Trolox equivalent/g seaweed). In addition, the seaweed extracts showed antihypertensive (≤59.77 ± 0.14%) and α-glucosidase inhibitory activity (≤68.05 ± 1.15%), as well as activity against foodborne pathogens. The present findings provide evidence of the biological activity of brown seaweed extracts for potential application in the food, pharmaceutical, and cosmetic sectors.
• Monthly variation of mycosporine-like amino acids from red alga dulse (Devaleraea inkyuleei, formerly Palmaria palmata in Japan)

  R.Yamamoto, A.M.M.Martin, Y.Miyabe, H.Kishimura, Y.Kumagai

  Phycology [TC=1] 3 (1) 127 - 137 2023/02 [Refereed][Not invited]
   

  Mycosporine-like amino acids (MAAs) are natural ultraviolet-absorbing compounds found in microalgae and macroalgae. MAA content changes seasonally and in response to environmental factors. We previously investigated MAAs from the red alga dulse (Devaleraea inkyuleei, formerly Palmaria palmata in Japan) in Usujiri, Hokkaido, Japan, from 2019 to 2020. At that time, some factors affecting MAA content were still unclear. In this study, we investigated MAA variation during the period from January to June 2021, and evaluated new methods of MAA extraction from dulse. We recorded a maximum MAA extraction yield (7.03 µmol/g dry weight) on 25 March 2021. Over the course of our three years of investigations from 2019 to 2021, we found that dulse was most suitable for MAA preparation from the middle of February to late April. In the later work reported in this paper, we improved our extraction method by using a lower-risk organic solvent (ethanol) rather than methanol. In addition, we evaluated MAA extraction using different levels of ethanol concentration (25, 50, and 99%) and different extraction times (2, 6, and 24 h). We found that extraction with 25% ethanol for 24 h increased MAA content by a factor of 3.2, compared with our previous extraction method. In summary, we determined the most suitable sampling period for Usujiri dulse, to extract the highest content of MAAs. We also improved the effectiveness of the extraction process.
• Characterisation of bioactive peptides from red alga Gracilariopsis chorda

  A.M.M.Martin, Y.Miyabe, T.Shimizu, W.Matsui, Y.Kumagai, H.Kishimura

  Marine Drugs [IF=6.085] [TC=5] 21 (1) 49 - 49 2023/01 [Refereed][Not invited]
   

  In this study, we studied the bioactive peptides produced by thermolysin hydrolysis of a water-soluble protein (WSP) from the red alga Gracilariopsis chorda, whose major components are phycobiliproteins and Ribulose-1,5-bisphosphate carboxylase-oxygenase (RuBisCo). The results showed that WSP hydrolysate exhibited significantly higher ACE inhibitory activity (92% inhibition) compared to DPP-IV inhibitory activity and DPPH scavenging activity. The phycobiliproteins and RuBisCo of G. chorda contain a high proportion of hydrophobic (31.0–46.5%) and aromatic (5.1–46.5%) amino acid residues, which was considered suitable for the formation of peptides with strong ACE inhibitory activity. Therefore, we searched for peptides with strong ACE inhibitory activity and identified two novel peptides (IDHY and LVVER). Then, their interaction with human ACE was evaluated by molecular docking, and IDHY was found to be a promising inhibitor. In silico analysis was then performed on the structural factors affecting ACE inhibitory peptide release, using the predicted 3D structures of phycobiliproteins and RuBisCo. The results showed that most of the ACE inhibitory peptides are located in the highly solvent accessible α-helix. Therefore, it was suggested that G. chorda is a good source of bioactive peptides, especially ACE-inhibitory peptides.
• Editorial: Application of biotechnology on the high-value development of marine bioresource

  Z.Jiang, H.Mou, Y.Kumagai, H.Kishimura

  Frontiers in Bioengineering and Biotechnology 10 2022/10 [Not refereed]
  
• Impact of extraction condition on the yield and molecular characteristics of collagen from Asian bullfrog (Rana tigerina) skin

  S.Indriani, S.Benjakul, H.Kishimura, S.Karnjanapratum, S.Nalinanon

  LWT-Food Science and Technology [IF=4.952] [TC=12] Elsevier BV 162 113439 - 113439 0023-6438 2022/06 [Refereed][Not invited]
  
• Physicochemical properties of house and cave edible bird’s nest from Southern Thailand

  K.Chantakun, H.Kishimura, Y.Kumagai, S.Benjakul

  ScienceAsia [IF=0.615] [TC=5] Science Society of Thailand under Royal Patronage and the National Research Council of Thailand 48 (2) 136 - 143 1513-1874 2022/04 [Refereed][Not invited]
  
• Characterization of unknown region in glycoside hydrolase family 17 β-1,3-glucanase from Vibrio vulnificus for a novel glucan binding domain

  Y.Kumagai, H.Kishimura, W.Lang, T.Tagami, M.Okuyama, A.Kimura

  Marine Drugs [IF=5.118] [TC=3] 2022/03/31 [Refereed][Not invited]
  
• Characterization of antioxidant activity of heated mycosporine-like amino acids from red alga dulse Palmaria palmata in Japan

  Y.Nishida, W.Saburi, Y.Miyabe, H.Kishimura, Y.Kumagai

  Marine Drugs [IF=5.118] [TC=6] 2022/03/01 [Refereed][Not invited]
  
• 水産加工食品のω3脂肪酸残存率に及ぼす製造条件の影響

  宮部好克, 落合瞳子, 熊谷祐也, 岸村栄毅

  日本調理科学会誌 [IF=0.206] 一般社団法人 日本調理科学会 2022 [Refereed][Not invited]
  
• Preparation of β(1→3)/β(1→4) xylooligosaccharides from red alga dulse by two xylanases from Streptomyces thermogriseus

  Y.Fujii, M.Kobayashi, Y.Miyabe, H.Kishimura, T.Hatanaka, Y.Kumagai

  Bioresources and Bioprocessing [IF=4.740] [TC=4] Springer Science and Business Media LLC 8 (1) 2021/12 [Refereed][Not invited]
   

  Red alga dulse contains xylan with β(1→3)/β(1→4) linkages. We previously prepared xylooligosaccharides (XOSs) from dulse xylan; however, the product contained many d-xylose residues and fewer XOSs with β(1→3) linkages. To improve the efficiency of XOS production, we prepared two recombinant endoxylanases from Streptomyces thermogriseus (StXyl10 and StXyl11). Comparing the k_cat/K_m values for dulse xylan, this value from StXyl10 was approximately two times higher than that from StXyl11. We then determined the suitable conditions for XOS production. As a result, dulse XOS was prepared by the successive hydrolysis of 10 mg/mL dulse xylan by 0.5 μg/mL StXyl10 for 4 h at 50 °C and then 2.0 μg/mL StXyl11 for 36 h at 60 °C. Xylan was converted into 95.8% XOS, including 59.7% XOS with a β(1→3) linkage and 0.97% d-xylose. Our study provides useful information for the production of XOSs with β(1→3) linkages.
• ACE inhibitory effect of the protein hydrolysates prepared from commercially available nori product by pepsin–trypsin digestion

  Rie Morikawa, Keigo Toji, Yuya Kumagai, Hideki Kishimura

  European Food Research and Technology [IF=2.998] [TC=8] Springer Science and Business Media LLC 1438-2377 2021/10/06 [Not invited]
  
• Study on the mechanism of the blood-glucose-lowering effect of collagen peptides from sturgeon by-products

  Y.Sasaoka, T.Takagi, S.Michiba, Y.Yamamoto, Y.Kumagai, H.Kishimura

  Marine Drugs [IF=5.118] [TC=5] MDPI 19 (10) 584 - 584 2021/10 [Refereed][Not invited]
   

  In a previous study, we found that the collagen peptides prepared from the by-products of Bester sturgeon had an inhibitory effect on elevated blood glucose levels in a glucose tolerance test with ICR mice. In the present study, we examine the mechanism of the effect of sturgeon collagen peptides (SCPs) in detail. When glucose was orally administered to mice along with the SCPs, it was found that the glucose remained in the stomach for a longer time. In the above tests, the amount of glucose excreted in the feces of mice also increased. On the contrary, it was revealed that the SCPs have a dipeptidyl-peptidase-IV (DPP-IV) inhibitory ability in an in vitro test. In subsequent oral and intravenous glucose administration tests, glucagon-like peptide-1 (GLP-1) and insulin levels in the blood of mice were maintained at high levels. These results suggested the following three mechanisms: SCPs slow the rate of transportation of glucose from the stomach into the small intestine, resulting in delayed glucose absorption; SCPs suppress the absorption of glucose in the small intestine and excrete it from the body; SCPs inhibit DPP-IV in the blood and maintain a high GLP-1 level in blood, which in turn stimulates insulin secretion.
• Characterization of ACE Inhibitory Peptides Prepared from Pyropia pseudolinearis Protein

  Y.Kumagai, K.Toji, S.Katsukura, R.Morikawa, T.Uji, H.Yasui, T.Shimizu, H.Kishimura

  Marine Drugs [IF=5.118] [TC=17] MDPI 19 (4) 200 - 200 2021/04/01 [Refereed][Not invited]
   

  More than 7000 red algae species have been classified. Although most of them are underused, they are a protein-rich marine resource. The hydrolysates of red algal proteins are good candidates for the inhibition of the angiotensin-I-converting enzyme (ACE). The ACE is one of the key factors for cardiovascular disease, and the inhibition of ACE activity is related to the prevention of high blood pressure. To better understand the relationship between the hydrolysates of red algal proteins and the inhibition of ACE activity, we attempted to identify novel ACE inhibitory peptides from Pyropia pseudolinearis. We prepared water soluble proteins (WSP) containing phycoerythrin, phycocyanin, allophycocyanin, and ribulose 1,5-bisphosphate carboxylase/oxygenase. In vitro analysis showed that the thermolysin hydrolysate of the WSP had high ACE inhibitory activity compared to that of WSP. We then identified 42 peptides in the hydrolysate by high-performance liquid chromatography and mass spectrometry. Among 42 peptides, 23 peptides were found in chloroplast proteins. We then synthesized the uncharacterized peptides ARY, YLR, and LRM and measured the ACE inhibitory activity. LRM showed a low IC50 value (0.15 μmol) compared to ARY and YLR (1.3 and 5.8 μmol). In silico analysis revealed that the LRM sequence was conserved in cpcA from Bangiales and Florideophyceae, indicating that the novel ACE inhibitory peptide LRM was highly conserved in red algae.
• Monthly variation and ultraviolet stability of mycosporine-like amino acids from red alga dulse Palmaria palmata in Japan

  Y.Nishida, Y.Miyabe, H. Kishimura, Y.Kumagai

  Phycology [TC=3] 1 (2) 119 - 128 2021 [Refereed][Not invited]
   

  Mycosporine-like amino acids (MAAs) are the natural ultraviolet (UV)-absorbing compounds from micro- and macro-algae. The MAAs in algae change with the environmental conditions and seasons. We previously determined an efficient extraction method of MAAs from red alga dulse in Usujiri (Hokkaido, Japan) and revealed monthly variation of MAA in 2019. Dulse samples in 2019 for MAA preparation were suitable from late February to April. In this study, to confirm the suitable timings to extract MAAs from Usujiri dulse, we also investigated the monthly (from January to May) variation of MAA content in 2020. There were the most MAAs in the sample on 18 March (6.696 µmol g−1 dry weight) among the samples from January to May 2020. From two years of investigation, we deduce that samples of Usujiri dulse from late February to early April were suitable for MAA preparation. The UV stability of the two major purified MAAs in Usujiri dulse—palythine and porphyra-334—was tested. The two MAAs and 2-hydroxy-4-methoxybenzophenone were stable for up to 12 h under a 312 nm lamp at 200 µW cm−2, but 2-ethylhexyl-4-methoxycinnamate formed a cis/trans-mixture in a short time. The data in this study show the suitable sampling period for Usujiri dulse and the possible application for UV protection from food and cosmetics.
• Enzymological characteristics of pepsinogens and pepsins purified from lizardfish (Saurida micropectoralis) stomach

  S.Kuepethkaew, Y.Zhang, H.Kishimura, Y.Kumagai, BK.Simpson, S.Benjakul, S.Damodarane, S.Klomklao

  Food Chemistry [IF=7.514] [TC=17] ELSEVIER 366 130532 - 130532 0308-8146 2021 [Refereed][Not invited]
  
• Efficient Extraction and Antioxidant Capacity of Mycosporine-Like Amino Acids from Red Alga Dulse Palmaria palmata in Japan

  Y.Nishida, Y.Kumagai, S.Michiba, H.Yasui, H.Kishimura

  Marine Drugs [IF=5.118] [TC=47] MDPI 18 (10) 502 - 502 2020/09/30 [Refereed][Not invited]
   

  Mycosporine-like amino acids (MAAs) are the ultraviolet (UV)-absorbable compounds, which are naturally produced by cyanobacteria and algae. Not only these algae but also marine organisms utilize MAAs to protect their DNA from UV-induced damage. On the other hand, the content of MAAs in algae was changed by the environmental condition and season. In addition to the UV-protected function, the antioxidant capacity of MAAs can apply to the cosmetic sunscreen materials and anti-cancer for human health. In this study, we developed the efficient extraction method of MAAs from red alga dulse in Usujiri (Hokkaido, Japan) and investigated the monthly variation. We also evaluated the antioxidant capacity. We employed the successive extraction method of water and then methanol extraction. Spectrophotometric and HPLC analyses revealed that the yield of MAAs by 6 h water extraction was the highest among the tested conditions, and the content of MAAs in the sample of February was the most (6.930 µmol g−1 dry weight) among the sample from January to May in 2019. Antioxidant capacity of MAAs such as crude MAAs, the purified palythine and porphyra-334 were determined by 2,2’-azinobis(3-ethylbenzothiazoline 6-sulfonic acid) (ABTS) radical scavenging and ferrous reducing power assays in various pH conditions, showing that the highest scavenging activity and reducing power were found at alkaline condition (pH 8.0).
• Debittering of salmon (Salmo salar) frame protein hydrolysate using 2-butanol in combination with β-cyclodextrin: Impact on some physicochemical characteristics and antioxidant activities

  A.Singh, AT.Idowu, S.Benjakul, H.Kishimura, RE.Aluko, Y.Kumagai

  Food Chemistry [IF=7.514] [TC=39] Elsevier 321 126686 - 126686 0308-8146 2020/08 [Refereed][Not invited]
  
• The potential of freshwater fish viscus from silver carp Hypophthalmichthys molitrix for trypsin source

  K.Abe, C.H.Yuan, Y.Kumagai, H.Kishimura

  Waste and Biomass Valorization [IF=2.851] [TC=4] Springer Nature 11 (8) 3971 - 3978 1877-2641 2020/08/01 [Refereed][Not invited]
   

  © 2019, Springer Nature B.V. Abstract: Purpose Silver carp is widely cultured in China (the product reached 3.5 million ton per year), and approximately 20% of the non-edible viscera are discarded. Utilization of the viscera leads to a reduction in waste. Our previous study showed that silver carp produced two types of myosin isoforms, thermostable myosin in summer and unstable one in winter, for the adaptation of the environmental changes. Therefore, in this study, we purified trypsins from silver carp in summer and winter samples to investigate their thermostabilities. Methods: Trypsins from summer and winter samples were purified by a series of chromatographies. The temperature dependence of trypsins was determined at pH 8.0 in the range of 20–80 °C, and the effect of temperature on the thermostability was determined by measuring the remaining activity after the incubation at pH 8.0 for 15 min in the range of 20–75 °C. Results: From the summer sample, two trypsins (SSC-T1 and SSC-T2) were purified 63- and 72-fold with the yields of 24 and 21%, respectively, and a trypsin (WSC-T) was purified 81-fold with a yield of 40% from the winter sample. SSC-T1, SSC-T2 and WSC-T showed the same enzymatic characteristics, especially their optimum temperature (65 °C) and thermostability (stable below 63 °C in 15-min incubation) were similar to mammalian trypsins. Additionally, all were stable at 30 °C for 8 h in the presence of calcium-ion. Conclusion: These data indicated the silver carp viscus has a potential for thermostable trypsin source all the year round. Graphic Abstract: Thermostable characteristics of trypsins from viscera of freshwater fish including silver carp (Hypophthalmichthys molitrix).[Figure not available: see fulltext.].
• Identification of ACE inhibitory peptides from red alga Mazzaella japonica

  Y.Kumagai, Y.Kitade, M.Kobayashi, K.Watanabe, H.Kurita, H.Takeda, H.Yasui, H. Kishimura (*)

  European Food Research and Technology [IF=2.366] [TC=19] Springer Nature 246 2225 - 2231 1438-2377 2020/07 [Refereed][Not invited]
  
• Potentiality of xylooligosaccharides from red alga dulse as prebiotics

  Hideki Kishimura, Yuya Kumagai

  Medical Science Digest 46 (7) 46 - 47 2020/07 [Not refereed][Invited]
  
• Characterization of acid soluble collagen from the skin of snakeskin gourami (Trichogaster pectoralis)

  P.Sukkon, AMM.Ali, S.Nalinanon, H.Kishimura, S.Takeungwongtrakul

  Carpathian Journal of Food Science and Technology [IF=0.169] 75 - 87 2066-6845 2020/06/30 [Refereed][Not invited]
  
• Protein hydrolysates from Pacific white shrimp cephalothorax manufactured with different processes: compositions, characteristics and antioxidative activity [IF:1.874]

  S.Sinthusamran, S.Benjakul, K.Kijroongrojana, T.Prodpran, H.Kishimura

  Waste and Biomass Valorization [IF=2.851] [TC=20] Springer Nature 11 (5) 1657 - 1670 2020/05 [Refereed][Not invited]
  
• Identification of a key enzyme for the hydrolysis of β-(1→3)-xylosyl linkage in red alga dulse xylooligosaccharide from Bifidobacterium adolescentis [IF:3.772]

  M.Kobayashi, Y.Kumagai, Y.Yamamoto, H.Yasui, H.Kishimura

  Marine Drugs [IF=5.118] [TC=12] MDPI AG 18 (174) 1 - 13 2020/03 [Refereed][Not invited]
  
• In silico analysis of ACE inhibitory peptides from chloroplast proteins of red alga Grateloupia asiatica [IF:2.798]

  K.Sumikawa, K.Takei, Y.Kumagai, T.Shimizu, H.Yasui, H.Kishimura

  Marine Biotechnology [IF=3.619] [TC=9] Springer Nature 23 391 - 402 2020/03 [Refereed][Not invited]
  
• Effect of proteases and alcohols used for debittering on characteristics and antioxidative activity of protein hydrolysate from salmon frames

  S.Sinthusamran, A.T.Idowu, S.Benjakul, Thummanoon, P.Ahmet, F.Yesilsu, H.Kishimura

  Journal of Food Science and Technology [IF=1.946] [TC=32] Springer Nature 57 473 - 483 2020/03 [Refereed][Not invited]
  
• 北海道大学発バイオイノベーション -水産副次産物の有効利用-

  岸村栄毅

  FOOD STYLE 21 23 (11) 28 - 29 2019/11 [Not refereed][Invited]
  
• Complete sequence of mitochondrial DNA of Gloiopeltis furcata (Postels & Ruprecht) J. Agardh

  K.Watanabe, T.Kishimoto, Y.Kumagai, T.Shimizu, T.Uji, H.Yasui, H.Kishimura

  Mitochondrial DNA Part B [IF=0.831] [TC=5] Taylor & Francis 4 (2) 2543 - 2544 2019/07 [Refereed][Not invited]
  
• Characteristics of acid and pepsin solubilized collagens from Nile tilapia (Oreochromis niloticus ) scale [IF:0.609]

  P.Kittiphattanabawon, C.Sriket, H.Kishimura, S.Benjakul

  Emirates Journal of Food and Agriculture [IF=1.008] [TC=19] 32 95 - 101 2019/05 [Refereed][Not invited]
  
• Enzymatic production of xylooligosaccharides from red alga dulse (Palmaria sp.) wasted in Japan

  Y.Yamamoto, H.Kishimura, Y.Kinoshita, W.Saburi, Y.Kumagai, H.Yasui, T.Ojima

  Process Biochemistry [IF=2.952] [TC=18] Elsevier BV 82 117 - 122 2019/04 [Refereed][Not invited]
  
• In silico analysis of relationship between proteins from plastid genome of red alga Palmaria sp. (Japan) and angiotensin I converting enzyme inhibitory peptides

  Y.Kumagai, Y.Miyabe, T.Takeda, K.Adachi, H.Yasui, H.Kishimura

  Marine Drugs [IF=4.379] [TC=28] MDPI AG 17 (3) 190 - 190 2019/03 [Refereed][Not invited]
   

  Plastid proteins are one of the main components in red algae. In order to clarify the angiotensin I converting enzyme (ACE) inhibitory peptides from red alga Palmaria sp. (Japan), we determined the plastid genome sequence. The genome possesses 205 protein coding genes, which were classified as genetic systems, ribosomal proteins, photosystems, adenosine triphosphate (ATP) synthesis, metabolism, transport, or unknown. After comparing ACE inhibitory peptides between protein sequences and a database, photosystems (177 ACE inhibitory peptides) were found to be the major source of ACE inhibitory peptides (total of 751). Photosystems consist of phycobilisomes, photosystem I, photosystem II, cytochrome complex, and a redox system. Among them, photosystem I (53) and II (51) were the major source of ACE inhibitory peptides. We found that the amino acid sequence of apcE (14) in phycobilisomes, psaA (18) and psaB (13) in photosystem I, and psbB (11) and psbC (10) in photosystem II covered a majority of bioactive peptide sequences. These results are useful for evaluating the bioactive peptides from red algae.
• A thermostable trypsin from freshwater fish Japanese dace (Tribolodon hakonensis): a comparison of the primary structures among fish trypsins

  G.Kanno, S.Klomklao, Y.Kumagai, H.Kishimura

  Fish Physiology and Biochemistry [IF=1.735] [TC=5] Springer Nature 2019/03 [Refereed][Not invited]
  
• Antioxidant activity of proteins extracted from red alga dulse harvested in Japan

  N.Sato, T.Furuta, T.Takeda, Y.Miyabe, K.Ura, Y.Takagi, H.Yasui, Y.Kumagai, H.Kishimura

  Journal of Food Biochemistry [IF=1.552] [TC=23] WILEY 43 (2) e12709 - e12709 0145-8884 2019/02 [Refereed][Not invited]
  
• Protein hydrolysate from salmon frames: Production, characteristics and antioxidative activity

  AT.Idowu, S.Benjakul, S.Sinthusamran, P.Sookchoo, H.Kishimura

  Journal of Food Biochemistry [IF:1.552] [TC=94] WILEY 43 e12734  2019/02 [Refereed][Not invited]
  
• Complete mitochondrial genome of Pacific red alga dulse Palmaria sp. (Japan) reveals the structural difference in Atlantic Palmaria palmate

  Y.Kumagai, R.Tsubouchi, Y.Miyabe, T.Takeda, K.Adachi, H.Yasui, H.Kishimura

  Mitochondrial DNA Part B [IF=0.831] [TC=13] Taylor & Francis 4 (2) 3177 - 3178 2019 [Refereed][Not invited]
  
• Amino Acid Composition, Volatile Compounds and Bioavailability of Biocalcium Powders from Salmon Frame as Affected by Pretreatment

  AT.Idowu, S.Benjakul, T.Sae-Leaw, P.Sookchoo, H.Kishimura, N.Suzuki, Y.Kitani

  Journal of Aquatic Food Product Technology [IF=1.020] [TC=10] Taylor & Francis 28 (7) 772 - 780 1049-8850 2019 [Refereed][Not invited]
   

  © 2019, © 2019 Taylor & Francis Group, LLC. Biocalcium powders, Bio-cal-H, and Bio-cal-A, obtained from non-alkaline treated and alkaline treated salmon frame were characterized. Glycine was the dominant amino acid (216.45–321.80 mg/g), followed by glutamic acid (102.52–110.38 mg/g), proline (72.96–96.10 mg/g), and hydroxyproline (72.98–83.75 mg/g) in both biocalcium powders. Bio-cal-H possessed a high abundance of volatile compounds such as 2-propanone, acetonitrile, and 2-butanone than Bio-cal-A. Bio-cal-A had a higher solubility in in vitro simulated gastrointestinal tract than Bio-cal-H and CaCO3 (P <.05). However, transportation of calcium across Caco-2 cell monolayer of Bio-cal-H was higher than Bio-cal-A and CaCO3 (P <.05). Overall, biocalcium could serve as a promising source of calcium supplementation.
• Physicochemical and molecular properties of gelatin from skin of golden carp (Probarbus Jullieni) as influenced by acid pretreatment and prior-ultrasonication

  AMM.Ali, H.Kishimura, S.Benjakul

  Food Hydrocolloids [IF=5.839] [TC=70] Elsevier BV 82 164 - 172 0268-005X 2018/09/01 [Refereed][Not invited]
   

  Gelatins from golden carp skin pretreated using different acids (acetic acid and sulfuric acid + acetic acid), with and without prior-ultrasonication, extracted at 55 °C for 3 and 6 h, were characterized. Different extraction efficiency and gelatin properties were obtained with different acid pretreatments. Prior-ultrasonication (20 kHz) with amplitude of 80% increased the yield of gelatins from acetic acid and sulfuric acid + acetic acid pretreated skins by 110.9% and 174.8%, respectively, compared with the corresponding controls (without prior-ultrasonication), when extracted for 6 h. All the gelatin samples had α- and β-chain as the major components. The gelatins extracted from skin with prior-ultrasonication showed slightly higher content of imino acids, compared to those produced by conventional method, regardless of acid pretreatments. Moreover, gelatin extracted by prior-ultrasonication had higher gelling and melting temperature than those produced by conventional method by 9.1–12.0 and 8.2–12.2%, respectively. FTIR spectra revealed that the formers had the higher cross-links stabilized by hydrogen bond than the latter. Based on microstructure study, the formers had higher number of interjunction zones with finer networks. Overall, pretreatment with sulfuric acid/acetic acid in combination with prior-ultrasonication effectively improved the extraction efficiency and gelling properties of gelatin from golden carp skin.
• Collagen peptides derived from the triple helical region of sturgeon collagen improve glucose tolerance in normal mice

  Y.Sasaoka, H.Kishimura, S.Adachi, Y.Takagi

  Journal of Food Biochemistry [IF=1.358] [TC=9] WILEY 42 (2) e12478  1745-4514 2018/04/01 [Refereed][Not invited]
   

  We prepared collagen peptides (SCP) from sturgeon by-products: the skin, fin, and bone. The materials were pretreated and hydrolyzed by papain. Finally, we obtained 85.1 g of dried SCP powder from 864 g (wet weight) of the materials. In oral glucose tolerance test (OGTT) with ICR mice, blood glucose levels of SCP group were significantly lower than those of control group. Then, we fractionated SCP by Sephadex column chromatography and all fractions showed hypoglycemic effect. Further, we separated each peptide in the fractions by reversed-phase HPLC. Most of the peptides in these peaks consisted of Gly-X-Y (X and Y are optional amino acid residues) repetitive sequences which are common to the triple helical region of the collagen molecules. Moreover, many peptides contained Pro and Ala residues, which promises to serve as a DPP-IV inhibitor. Altogether, these results suggest the hypoglycemic effect of SCP may be caused by these structural properties. Practical applications: While sturgeon is famous and highly valuable for its salted egg “caviar” and meat, other parts such as skin, fin, and bone, that is, by-products are not fully utilized in seafood industry. In this study, we focused on whole utilization of a sturgeon and prepared collagen peptides (SCP) from sturgeon by-products. The yield of SCP was approximately 100 g SCP/kg wet by-products. In animal experiments, SCP showed hypoglycemic effect. Moreover, the effect is probably caused by Gly-X-Y repetitive sequences derived from the triple helical region of a collagen molecule. The mechanism might be related to DPP-IV inhibitory activity. SCP was white, odorless, and easily soluble in water and it could be advantages in using SCP as an ingredient for functional foods preventing Type 2 diabetes mellitus. The by-products of sturgeon will be a new fishery resource which could be used as a material for collagen peptides providing the hypoglycemic effect.
• Extraction efficiency and characteristics of acid and pepsin soluble collagens from the skin of golden carp (Probarbus Jullieni) as affected by ultrasonication

  AMM.Ali, H.Kishimura, S.Benjakul

  Process Biochemistry [IF=2.883] [TC=90] Elsevier 66 237 - 244 1359-5113 2018/03/01 [Refereed][Not invited]
   

  Extraction efficiency and physiochemical properties of acid and pepsin soluble collagens from the skin of golden carp (Probarbus jullieni) as influenced by ultrasonication were studied. The ultrasound treatment (20 kHz) with increasing amplitudes from 20 to 80% increased the yield of acid soluble collagen (ASC) (P < 0.05). When the ultrasound at an amplitude of 80% was employed in combination with pepsin (0.1. 0.5 and 1%), the marked increase in pepsin soluble collagen (PSC) was obtained when pepsin level increased (P < 0.05). The yield of ASC and PSC increased as ultrasonication time increased (P < 0.05). ASC and PSC with ultrasound aided process, named as UASC and UPSC, had the yields of 81.53 and 94.88%, while ASC and PSC prepared with typical method showed the yields of 51.90 and 79.27%, respectively. All the collagens, with similar amino acid composition, contained α- and β-chains and were type I. Based on circular dichroism (CD) and fourier transform infrared spectroscopy (FTIR), all the collagens had the triple helical structure. Tmax of PSC and UPSC were higher than those of ASC and UASC. Overall, ultrasound treatment under appropriate condition effectively improved the extraction efficiency of ASC and PSC without affecting their physiochemical properties.
• Structural characteristics of phycobiliproteins from red alga Mazzaella japonica

  Y.Kitade, Y.Miyabe, Y.Yamamoto, H.Takeda, T.Shimizu, H.Yasui, H.Kishimura

  Journal of Food Biochemistry [IF=1.358] [TC=22] WILEY 42 (1) e12436  1745-4514 2018/02/01 [Refereed][Not invited]
   

  We determined the primary structures of phycoerythrin (PE), phycocyanin (PC), and allophycocyanin (APC) from red alga Mazzaella japonica. The phycobiliproteins consist of α- and β-subunits like other red algae. M. japonica phycobiliproteins all conserved Cys residues for chromophore attachment site. The amino acid sequences of M. japonica phycobiliproteins showed considerably high identities with those of other red algae (81–100%). In addition, the sequences (YRD, LDY, LRY, VY, LF, and FY), which were angiotensin I converting enzyme (ACE) inhibitory peptides from other algae were detected in the primary structures of M. japonica phycobiliproteins. Then, we prepared the protein hydrolysates from M. japonica and measured its ACE inhibitory activity. Consequently, M. japonica protein hydrolysates indicated considerably high ACE inhibitory activity. Practical applications: M. japonica is an abundant resource in Japan, which contains a lot of phycobiliproteins. Then, M. japonica protein hydrolysates strongly inhibited the activity of ACE. Therefore, it has the potential to be an ingredient of functional food.
• Characteristics and Properties of Gelatin from Seabass (Lates calcarifer) Swim Bladder : Impact of Extraction Temperatures

  S.Sinthusamran, S.Benjakul, Y.Hemar, H.Kishimura

  Waste and Biomass Valorization [IF=2.15] [TC=17] Springer Nature 9 (2) 315 - 325 1877-265X 2018/02/01 [Refereed][Not invited]
   

  Purpose: This study aimed to investigate the impact of various extracting temperatures on yield and properties of gelatin from swim bladder of seabass (Lates calcarifer), a byproduct from processing. Methods: Gelatin from seabass swim bladderwas extracted at different temperatures (45, 55, 65 and 75 °C). The gelatins obtained using various extraction temperatures were characterized. Results: The yield and recovery of gelatin from swim bladder (44.83–71.95% and 49.08–74.83%, based on dry weight) increased with increasing extraction temperatures. All gelatins contained α-chains as the predominant components, followed by β-chain. Gelatin from seabass swim bladder showed a high imino acid content (195 residues/1000 residues). FTIR and CD spectra revealed the loss of triple helix during heating via breaking down hydrogen bonds between α-chains. Gel strength generally increased as the extraction temperature increased up to 65 °C (P < 0.05). Gelatin extracted at 65 °C for 6 h showed a higher gel strength, compared to bovine gelatin (P < 0.05). Gelling and melting temperatures were 10.4–19.7 and 19.3–28.4 °C, respectively, depending on extraction temperature. Conclusion: Properties of gelatin from swim bladder were affected by extraction temperature. Therefore, seabass swim bladder could serve as an alternative collagenous material for gelatin production, when the appropriate extraction condition was implemented.
• Extraction and characterisation of collagen from the skin of golden carp (Probarbus jullieni), a processing by-product

  AMM.Ali, S.Benjakul, T.Prodpran, H.Kishimura

  Waste and Biomass Valorization [IF=2.15] [TC=58] Springer Nature 9 783 - 791 2018 [Refereed][Not invited]
  
• Characteristics and gelling property of gelatin from scale of spotted golden goatfish (Parupeneus heptacanthus)

  S.Chuaychan, S.Benjakul, H.Kishimura

  Journal of Food Processing and Preservation [IF=1.510] [TC=15] 41 (5) e13139  0145-8892 2017/10 [Refereed][Not invited]
   

  Gelatins from the scales of spotted golden goatfish were extracted under different conditions and characterized. The gelatin yield, when extracted at 45, 60 and 75C (for 6 or 12 h), was 2.3-2.6%, 8.6-9.3% and 9.9-10.1% on dry weight basis, respectively. All the gelatins had - and -chains as the dominant components, and had high imino acid contents (182-192 residues/1,000 residues). Gel strength of the gelatin decreased and the gelatin solution became more turbid with increasing temperature and time of extraction. The gelling and melting temperatures of gelatin were 18.7-20.1 and 26.4-28.0C, respectively, and these decreased with extraction temperature and time. The results suggest that the scales of spotted golden goatfish have potential to serve as the collagenous raw material for gelatin extraction. Practical ApplicationsSpotted golden goatfish (Parupeneus heptacanthus) is used in the manufacturing of frozen fish fillets in Thailand, and the scales with low market value are generated as byproducts. Large amounts of scales could potentially serve as raw material for gelatin production. However, the proper extraction conditions need to be determined experimentally, considering both yield and properties of the resulting gelatin.
• Characteristics and gel properties of gelatin from skin of Asian bullfrog (Rana tigerina)

  S.Karnjanapratum, S.Sinthusamran, T.Sae-leaw, S.Benjakul, H.Kishimura

  Food Biophysics [IF=2.051] [TC=20] 12 (3) 289 - 298 1557-1858 2017/09 [Refereed][Not invited]
   

  Characteristics and gel properties of gelatin from frog skin as influenced by extraction temperatures (45-75 A degrees C) were investigated. Yield of gelatin increased as the extraction temperature increased (P < 0.05). All gelatins contained alpha- and beta-chains as the predominant components and showed a high imino acid content (215 residues/1000 residues). Fourier transform infrared (FTIR) spectra indicated that all gelatin samples had major peaks in amide regions. Gelatin extracted at 55 A degrees C exhibited the highest gel strength (P < 0.05), which was similar to that of commercial bovine gelatin (P > 0.05). Gelling and melting temperatures of frog skin gelatin were 23.47-24.87 and 33.22-34.66 A degrees C, respectively. Gels became more yellowish with increasing extraction temperatures (P < 0.05). All gelatin gels were sponge or coral-like in structure but varied in patterns as visualized by scanning electron microscopy (SEM). Gelatin from frog skin could be used as a replacement for land animal counterpart.
• Structural properties of phycoerythrin from dulse Palmaria palmata

  Y.Miyabe, T.Furuta, T.Takeda, G.Kanno, T.Shimizu, Y.Tanaka, Z.Gai, H.Yasui, H.Kishimura

  Journal of Food Biochemistry [IF=1.552] [TC=25] 41 (1) e12301  0145-8884 2017/02 [Refereed][Not invited]
   

  We found that the red alga dulse (Palmaria palmata) contains a lot of proteins, which is mainly composed of phycoerythrin (PE) and the protein hydrolysates showed high angiotensin I converting enzyme (ACE) inhibitory activities. Therefore, we investigated the structure of dulse PE to discuss its structure-function relationship. We prepared the chloroplast DNA and analyzed the nucleotide sequences encoding PE by cDNA cloning method. It was clarified that dulse PE has alpha- and beta-subunits and they are composed by 164 amino acids (MW: 17,638) and 177 amino acids (MW: 18,407), respectively. The dulse PE contained conserved cysteine residues for chromophore attachment site. On the alignment of amino acid sequences of dulse PE with those of other red algal PE, the sequence identities were very high (81-92%). In addition, we purified and crystallized the dulse PE, and its crystal structure was determined at 2.09 angstrom resolution by molecular replacement method. The revealed 3D structure of dulse PE which forms an (alpha beta)(6) hexamer was similar to other red algal PEs. Conversely, it was clarified that the dulse PE proteins are rich in hydrophobic amino acid residues (51.0%), especially aromatic amino acid and proline residues. The data imply that the high ACE inhibitory activity of dulse protein hydrolysates would be caused by the specific amino acid composition and sequence of dulse PE.
• Characteristics and functional properties of ovary from squid Loligo formosana

  A.Singh, S.Benjakul, H.Kishimura

  Journal of Aquatic Food Product Technology [IF=0.682] [TC=26] 26 (9) 1083 - 1092 1049-8850 2017 [Refereed][Not invited]
   

  The characteristics and functional properties of the ovary from Loligo formosana were studied. Moisture (72.07 +/- 0.24%) was dominant, followed by protein (18.64 +/- 0.51%) and carbohydrate (7.44 +/- 0.2%). Ash (1.39 +/- 0.03%) and lipids (0.46 +/- 0.5%) were found as the minor constituents. Albumin (79.02 +/- 0.79%) was the major protein of the squid ovary, followed by glutelin-1 (8.31 +/- 0.62%) and globulin (6.68 +/- 0.08%). Nevertheless, prolamin and glutelin-2 constituted approximately 1% of the total proteins. Based on the electrophoretic studies, albumin had the largest band intensity. The squid ovary was rich in non-essential amino acids (52.26%) and high in hydrophobic amino acids (48.03%). It was also rich in polyunsaturated fatty acid (PUFA, 43.76 +/- 0.84%), followed by saturated fatty acid (SFA, 39.36 +/- 0.12%) and monounsaturated fatty acid (MUFA, 12.94 +/- 0.55%). Ovary lipids had a high amount of docosa-hexaenoic acid (C22: 6) (28.59%). At pH 3, the squid ovary powder (SOP) had the maximum solubility (96.39%), whereas the lowest solubility (38.33%) was observed at pH 9. The foaming capacity and stability of SOP were increased with increasing concentration up to 8% (p < 0.05). The globulin fraction showed the higher foaming capacity, as compared to albumin and glutelin-1 fractions. The squid ovary had good nutritional value and possessed excellent foaming properties. Therefore, the squid ovary could serve as a novel food additive or ingredient.
• Molecular characteristics of acid and pepsin soluble collagens from the scales of golden carp (Probarbus jullieni)

  AMM. Ali, S.Benjakul, H.Kishimura

  Emirates Journal of Food and Agriculture [IF=0.609] [TC=36] 29 (6) 450 - 457 2079-052X 2017 [Refereed][Not invited]
   

  Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) were isolated from the scales of golden carp (Probarbus jullieni). Both ASC and PSC, identified as type I collagen, contained alpha- and beta-chains as the dominant constituents. ASC and PSC had the yields of 0.42 and 1.16 g 100 g(-1) (dry weight basis), respectively. Amino acid composition revealed that glycine constituted 1/3 of total amino acid residues and no cysteine was found. ASC and PSC had imino acid contents of 197 and 202 residues/1000 residues, respectively. Fourier transform infrared spectroscopy (FTIR) and circular dichroism (CD) spectra indicated high integrity of the triple helical structure of both collagens. Based on differential scanning calorimetry (DSC), ASC and PSC had T-max of 37.67 and 37.83 degrees C, respectively. Both collagens exhibited high solubility in acidic pH range (1-3) and the decrease in solubility was found in the presence of NaCl at concentrations above 30 g L-1. The overall results demonstrated that scales of golden carp could serve as another source of collagen.
• Characteristics of Collagen from Rohu (Labeo rohita) Skin

  W.Savedboworn, P.Kittiphattanabawon, S.Benjakul, S.Sinthusamran, H.Kishimura

  Journal of Aquatic Food Product Technology [IF=0.682] [TC=16] 26 (3) 248 - 257 1049-8850 2017 [Refereed][Not invited]
   

  Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) were isolated from rohu skin with the yield of 64.2 and 6.8% (dry weight basis), respectively. Both collagens had glycine as the major amino acid with imino acid content of 196-202 residues/1,000 residues and were characterized as type I collagen with molecular composition of (1)(2)2-heterotrimer. Fourier transform infrared spectra of both collagens were similar, with no shift in wavenumber of all amide bands. The T-max value of ASC and PSC was 36.40 and 35.48 degrees C, respectively. The zero surface net charge of ASC and PSC was found at pH 5.9 and 5.3, respectively.
• Characteristics and functional properties of gelatin from seabassskin as influenced by defatting

  T.Sae-leaw, S.Benjakul, NM.O'Brien, H.Kishimura

  International Journal of Food Science and Technology [IF=2.383] [TC=25] 51 (5) 1204 - 1211 0950-5423 2016/05 [Refereed][Not invited]
   

  Gelatins from nondefatted and defatted seabass skins were characterised and evaluated for their functional properties in comparison with commercial fish skin gelatin. All gelatins contained (1)- and (2)-chains as the predominant components and showed a high imino acid content (199-201 residues/1000 residues). All gelatins had a relative solubility greater than 90% in the wide pH ranges (1-10). Foaming properties of all gelatins increased with increasing concentrations (1-3%, w/v). Gelatin from defatted skin had higher foam expansion and stability than that extracted from nondefatted skin. Emulsion containing gelatin from defatted skin had smaller oil droplet size (d(32), d(43)), compared with that having gelatin from nondefatted skin (P<0.05). After 10days of storage at room temperature (28-30 degrees C), emulsion stabilised by gelatin from defatted skin showed the higher stability as indicated by the lower increases in d(32) and d(43), and lower flocculation factor and coalescence index. Coincidentally, emulsion stabilised by gelatin from defatted skin had higher zeta potential than that containing gelatin from nondefatted skin. Thus, defatting of seabass skin directly affected characteristics and functional properties of resulting gelatin.
• Purification and characterization of trypsin inhibitor from yellowfin tuna (Thunnus albacores) roe

  S.Klomklao, S.Benjakul, H.Kishimura, K.Osako, BK.Simpson

  Journal of Food Biochemistry [IF=1.552] [TC=8] 40 (2) 140 - 147 0145-8884 2016/04 [Refereed][Not invited]
   

  Trypsin inhibitor was purified to homogeneity from the roe of yellowfin tuna (Thunnus albacores) by heat treatment at 60C for 10min, followed by column chromatographies on Sephacryl S-200, Sephadex G-50 and DEAE-cellulose. The trypsin inhibitor was purified 11.29-fold with a yield of 46.02%. Yellowfin tuna trypsin inhibitor migrated as a single band using native polyacrylamide gel electrophoresis. Purified trypsin inhibitor had an apparent molecular weight of 70kDa when analyzed using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and size exclusion chromatography. No inhibitory activity was obtained under reducing condition of -mercaptoethanol. Maximal activity was recorded at pH7.0 and 50C. The purified inhibitor was stable in the temperature range of 20-60C for 10min and in the pH range of 5-8. NaCl concentration up to 3% did not significantly affect the inhibitory activity of purified trypsin inhibitor. However, the activity decreased when trypsin inhibitor was incubated with metal ions (Cu+, Na+, Mg2+ and Ca2+) at ambient temperature for 30min. Practical ApplicationsTrypsin inhibitor from yellowfin tuna (Thunnus albacores) roe, the by-products of tuna processing, can be purified. The yellowfin tuna trypsin inhibitor is a salt-stable peptide and could be useful for food applications, especially surimi.
• Gelatin from clown featherback skin: extraction conditions

  P.Kittiphattanabawon, S.Benjakul, S.Sinthusamran, H.Kishimura

  LWT-Food Science and Technology [IF=2.329] [TC=110] 66 186 - 192 0023-6438 2016/03 [Refereed][Not invited]
   

  Gel properties of gelatin from clown featherback skin as affected by different extraction temperatures (45, 65 and 85 degrees C) and times (6 and 12 h) were determined. The gelatin recovery was found in the range of 73.99-95.85 g/100 g. Gelatin had glycine as major amino acid, followed by alanine and proline. Gel strength generally decreased as extraction temperature and time increased. With increasing temperature and time, band intensity of alpha-, beta- and gamma-chains decreased. Gelling temperature (15.53-24.71 degrees C) and gelling time (11.62-49.27 min) varied, depending on extraction condition. All gelatin could set at 25 degrees C, except those extracted at 65 degrees C for 12 or at 85 degrees C for 6 and 12 h. Gelatin extracted at 45 degrees C for 6 and 12 h showed higher gel strength, compared bovine gelatin (P < 0.05). Therefore, properties of gelatin from clown featherback skin could be influenced by extraction condition. (C) 2015 Elsevier Ltd. All rights reserved.
• Enzymatic hydrolysis of starry triggerfish (Abalistes stellaris) muscle using liver proteinase from albacore tuna (Thunnus alalunga)

  P.Sripokar, M.Chaijan, S.Benjakul, H.Kishimura, S Klomklao

  Journal of Food Science and Technology [IF=1.262] [TC=8] 53 (2) 1047 - 1054 0022-1155 2016/02 [Refereed][Not invited]
   

  Proteinases from liver extract from albacore tuna (Thunnus alalunga) were used to produce protein hydrolysate from starry triggerfish (Abalistes stellaris) muscle. Hydrolysis conditions for preparing protein hydrolysate from starry triggerfish muscle were optimized. Enzyme level, reaction time and fish muscle/buffer ratio significantly affected the hydrolysis (p < 0.05). Optimum conditions for triggerfish muscle hydrolysis were 5.5 % liver extract, 40 min reaction time and fish muscle/buffer ratio of 1:3 (w/v). The freeze-dried protein hydrolysate was characterized with respect to chemical composition, amino acid composition and color. The product contained 91.73 % protein, 2.04 % lipid and 6.48 % ash. The protein hydrolysate exhibited high amount of essential amino acids (45.62 %). It was light yellow in color (L (*) = 82.94, a (*) = 0.84, b (*) = 22.83). The results indicate that the extract from liver of albacore tuna could be used to produce fish protein hydrolysate and protein hydrolysate from starry triggerfish muscle may potentially serve as a good source of desirable peptide and amino acids.
• Angiotensin I converting enzyme inhibitory peptides derived from phycobiliproteins of dulse Palmaria palmata

  T.Furuta, Y.Miyabe, H.Yasui, Y.Kinoshita, H.Kishimura

  Marine Drugs [IF=3.143] [TC=104] 14 (2) 1 - 10 1660-3397 2016/02 [Refereed][Not invited]
   

  We examined the inhibitory activity of angiotensin I converting enzyme (ACE) in protein hydrolysates from dulse, Palmaria palmata. The proteins extracted from dulse were mainly composed of phycoerythrin (PE) followed by phycocyanin (PC) and allophycocyanin (APC). The dulse proteins showed slight ACE inhibitory activity, whereas the inhibitory activity was extremely enhanced by thermolysin hydrolysis. The ACE inhibitory activity of hydrolysates was hardly affected by additional pepsin, trypsin and chymotrypsin treatments. Nine ACE inhibitory peptides (YRD, AGGEY, VYRT, VDHY, IKGHY, LKNPG, LDY, LRY, FEQDWAS) were isolated from the hydrolysates by reversed-phase high-performance liquid chromatography (HPLC), and it was demonstrated that the synthetic peptide LRY (IC50: 0.044 mol) has remarkably high ACE inhibitory activity. Then, we investigated the structural properties of dulse phycobiliproteins to discuss the origin of dulse ACE inhibitory peptides. Each dulse phycobiliprotein possesses -subunit (Mw: 17,477-17,638) and -subunit (Mw: 17,455-18,407). The sequences of YRD, AGGEY, VYRT, VDHY, LKNPG and LDY were detected in the primary structure of PE -subunit, and the LDY also exists in the APC - and -subunits. In addition, the LRY sequence was found in the -subunits of PE, PC and APC. From these results, it was suggested that the dulse ACE inhibitory peptides were derived from phycobiliproteins, especially PE. To make sure the deduction, we carried out additional experiment by using recombinant PE. We expressed the recombinant - and -subunits of PE (rPE and rPE, respectively), and then prepared their peptides by thermolysin hydrolysis. As a result, these peptides showed high ACE inhibitory activities (rPE: 94.4%; rPE: 87.0%). Therefore, we concluded that the original proteins of dulse ACE inhibitory peptides were phycobiliproteins.
• Characteristics of gelatin extracted from the swim bladder of yellowfin tuna (Thunnus albacores) as affected by alkaline pretreatments

  O.Kaewdang, S.Benjakul, T.Prodpran, T.Kaewmanee, H.Kishimura

  Journal of Aquatic Food Product Technology [IF=0.478] [TC=8] 25 (8) 1190 - 1201 1049-8850 2016 [Refereed][Not invited]
   

  Gelatins extracted from the swim bladder of yellowfin tuna (Thunnus albacores) using various alkaline pretreatments were characterized. Alkaline mixtures (Na2CO3:NaOH) at different ratios (9:1, 8:2, 7:3, and 6:4) with a concentration of 4% (w/v) were used. The corresponding gelatins termed G1, G2, G3, and G4 had yields of 9.78, 14.91, 35.96, and 13.60% (dry weight basis), respectively. All gelatins had -chains as the major components. Fourier transform infrared spectra of obtained gelatins revealed the significant loss of molecular order of the triple-helix. G3 having the highest imino acid content and exhibited the highest gel strength (p < 0.05), compared with others. The microstructure of G3 gel was finer with smaller voids, compared with others. With increasing proportion of NaOH, the L*-value of gelatin gel increased with coincidental decrease in E*-value. Gelling and melting temperatures of swim bladder gelatin were 12.3-15.1 and 21.3-22.3 degrees C, respectively.
• Trypsin inhibitor from yellowfin tuna (Thunnus albacores) roe: Effects on gel properties of surimi from bigeye snapper (Priacanthus macracanthus)

  S.Klomklao, S.Benjakul, H.Kishimura, K.Osako, BK.Simpson

  LWT-Food Science and Technology [IF=2.329] [TC=34] 65 122 - 127 0023-6438 2016/01 [Refereed][Not invited]
   

  Effects of partially purified trypsin inhibitor from the roe of yellowfin tuna (Thunnus albacores) (TIYTR) at different levels (0-3.0 g/100 g) on gelling properties of bigeye snapper (Priacanthus macracanthus) surimi were investigated. TIYTR showed inhibitory activity against proteolysis in kamaboko (40/90 degrees C) and modori (60/90 degrees C) gels in a concentration-dependent manner. Myosin heavy chain (MHC) was more retained in both gels when the level of TIYTR increased up to 3.0 g/100 g. This was associated with the increased breaking force and deformation as well as lowered protein degradation as evidenced by the decrease in trichloroacetic acid-soluble peptide content (p < 0.05). Whiteness of kamaboko and modori gels slightly decreased with increasing TIYTR levels (p < 0.05). However, water-holding capacity of both gels was improved as TIYTR level increased (p < 0.05). Incorporation of TIYTR, beef plasma protein (BPP) and egg white (EW) at a level of 3.0 g/100 g resulted in the increased breaking force and deformation of surimi gels. Nevertheless, TIYTR and BPP showed the higher gel strengthening effect than EW. Therefore, TIYTR could be used as an alternative cheap proteinase inhibitor to improve gel strength of surimi. (C) 2015 Elsevier Ltd. All rights reserved.
• Crystal structure of the 3.8-MDa respiratory supermolecule hemocyanin at 3.0 Å resolution

  Zuoqi Gai, Asuka Matsuno, Koji Kato, Sanae Kato, Md Rafiqul Islam Khan, Takeshi Shimizu, Takeya Yoshioka, Yuki Kato, Hideki Kishimura, Gaku Kanno, Yoshikatsu Miyabe, Tohru Terada, Yoshikazu Tanaka, Min Yao

  Structure [IF=5.618] [TC=33] 23 (12) 2204 - 2212 0969-2126 2015/12 [Refereed][Not invited]
   

  Molluscan hemocyanin, a copper-containing oxygen transporter, is one of the largest known proteins. Although molluscan hemocyanins are currently applied as immunotherapeutic agents, their precise structure has not been determined because of their enormous size. Here, we have determined the first X-ray crystal structure of intact molluscan hemocyanin. The structure unveiled the architecture of the 3.8-MDa supermolecule composed of homologous functional units (FUs), wherein the dimers of FUs hierarchically associated to form the entire cylindrical decamer. Most of the specific inter-FU interactions were localized at narrow regions in the FU dimers, suggesting that rigid FU dimers formed by specific interactions assemble with flexibility. Furthermore, the roles of carbohydrates in assembly and allosteric effect, and conserved sulfur-containing residues in copper incorporation, were revealed. The precise structural information obtained in this study will accelerate our understanding of the molecular basis of hemocyanin and its future applications.
• Characteristics of collagen from the skin of clown featherback (Chitala ornata)

  P.Kittiphattanabawon, S.Benjakul, S.Sinthusamran, H.Kishimura

  International Journal of Food Science and Technology [IF=2.383] [TC=30] 50 (9) 1972 - 1978 0950-5423 2015/09 [Refereed][Not invited]
   

  Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from the skin of clown featherback (Chitala ornata) were isolated and characterised. Yields of ASC and PSC were 27.64 and 44.63% (dry weight basis) with total collagen recovery of 82.08%. Both collagens contained glycine as the major amino acid with relatively high content of proline, hydroxyproline and glutamic acid/glutamine. Nevertheless, they had the low content of cysteine, histidine and tryrosine. The collagen was characterised as type I, comprising (1)(2)2-heterotrimer. Pepsin-aided process did not affect triple-helical structure of PSC as determined by FTIR spectra. Thermal transition temperature of ASC (36.28 degrees C) was slightly higher than that of PSC (35.23 degrees C). However, no differences in isoelectric point (5.54-5.68) between ASC and PSC were observed. Therefore, collagen from the skin of clown featherback could be successfully extracted for further applications.
• Characteristics of acid- and pepsin-soluble collagens from scale of seabass (Lates calcarifer)

  S.Chuaychan, S.Benjakul, H.Kishimura

  LWT-Food Science and Technology [IF=2.329] [TC=110] 63 (1) 71 - 76 0023-6438 2015/09 [Refereed][Not invited]
   

  Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from seabass (Lates calcarifer) scale were characterised. Yields of ASC and PSC were 0.38 and 1.06% (based on dry weight), respectively. Both ASC and PSC were identified to be type I collagen, which consisted of alpha(1) and alpha(2) chains. beta component was also found in both collagens. ASC and PSC contained glycine as the major amino acid and had high imino acid content (193-198 residues/1000 residues). T-max of ASC and PSC from seabass scale were 38.17 degrees C and 39.32 degrees C, respectively. FTIR spectra indicated that triple helical structure of resulting PSC was not disrupted by pepsin digestion. ASC and PSC from seabass scale exhibited high solubility in very acidic pH range (pH 2-4). Therefore, seabass scale could be an alternative source of collagen and the characteristics of collagens were slightly affected by extraction process used. (C) 2015 Elsevier Ltd. All rights reserved.
• Purification and characterization of trypsin from hepatopancreas of Pacific white shrimp

  Theeraphol Senphan, Soottawat Benjakul, Hideki Kishimura

  Journal of Food Biochemistry [IF=1.552] [TC=27] 39 (4) 388 - 397 0145-8884 2015/08 [Refereed][Not invited]
   

  Trypsin from hepatopancreas of Pacific white shrimp (Litopenaeus vannamei) was purified to homogeneity using ammonium sulfate precipitation and a series of chromatographies including diethylaminoethyl sepharose and soybean trypsin inhibitor sepharose 4B columns. Trypsin was purified to 50.4-fold with a yield of 13.7%. Based on native-polyacrylamide gel electrophoresis (PAGE), the purified trypsin showed a single band. Trypsin had a molecular weight of 24kDa as estimated by sodium dodecyl sulphate-PAGE. The optimal pH and temperature for -N-benzoyl-dl-arginine-p-nitroanilide (BAPNA) hydrolysis were 8.0 and 60C, respectively. Trypsin was stable to heat treatment up to 60C and over a pH range of 7.0-11.0. The activity was strongly inhibited by soybean N--tosyl-L-lysine chloromethyl ketone. Purified trypsin had Michaelis-Menten constant (K-m) and catalytic constant (k(cat)) of 1.60mM and 3.33s(-1), respectively, when BAPNA was used as the substrate. Trypsin with high k(cat) indicated its high capacity of hydrolysis and it could serve as a promising protease. Practical ApplicationsPacific white shrimp hepatopancreas generally serves as a major source of proteases, especially trypsin and chymotrypsin, which can be used as an alternative food processing aid. Proteases in the hepatopancreas can be recovered and further used, in which the cost of commercially available proteases can be reduced. Furthermore, the by-product can be better exploited and the extracted proteases can increase the revenues for the shrimp processor.
• Antioxidant activity of gelatin hydrolysate produced from fish skin gelatin using extracellular protease from Bacillus amyloliquefaciensH11

  S.Sai-U, S.Benjakul, P.Sumpavapol, H.Kishimura

  Journal of Food Processing and Preservation [IF=1.510] [TC=22] 39 (4) 394 - 403 0145-8892 2015/08 [Refereed][Not invited]
   

  Antioxidant activities of gelatin hydrolysates (GHs) from unicorn leatherjacket skin prepared using extracellular protease from Bacillus amyloliquefaciensH11 (GH-H11) with different degrees of hydrolysis (DHs) were comparatively studied with those of hydrolysate produced using Alcalase (GH-Al). Antioxidative activities of hydrolysates produced by both proteases increased with increasing DH (P<0.05). With DHs of 20-40%, GH-H11 showed higher 2,2-azinobis(3-ethylbenzothiazoline-6-sulphonic acid) radical-scavenging activity and ferric-reducing antioxidant power than GH-Al (P<0.05), but no differences in chelating activity were found (P>0.05). Both hydrolysates (100 and 1,000ppm) could inhibit lipid peroxidation in lecithin liposome system in a dose-dependent manner. In vitro simulated gastrointestinal digestion study indicated that the antioxidative activity of GH was not affected by pepsin, while further hydrolysis by pancreatin enhanced the antioxidative activity. The dominant antioxidative peptides in GH-H11 and GH-Al had molecular weights of approximately 750 and 3,600Da, respectively. Practical ApplicationsBacillus amyloliquefaciensH11 protease could hydrolyze gelatin more effectively than Alcalase. Gelatin hydrolysate using B.amyloliquefaciensH11 protease had high antioxidant activity than that prepared by Alcalase. Antioxidative peptide could be useful for the food industry owing to process specificity and the economic value of producing bioactive peptide for commercial use.
• Crystallization and preliminary X-ray crystallographic study of a 3.8-MDa respiratory supermolecule hemocyanin

  A.Matsuno, Z.Gai, M.Tanaka, K.Kato, S.Kato, T.Katoh, T.Shimizu, T.Yoshioka, H.Kishimura, Y.Tanaka, M.Yao

  Journal of Structural Biology [IF=3.448] [TC=12] 190 (3) 379 - 382 1047-8477 2015/06 [Refereed][Not invited]
   

  Many molluscs transport oxygen using a very large cylindrical multimeric copper-containing protein named hemocyanin. The molluscan hemocyanin forms a decamer (cephalopods) or multidecamer (gastropods) of approximately 330-450 kDa subunits, resulting in a molecular mass >3.3 MDa. Therefore, molluscan hemocyanin is one of the largest proteins. The reason why these organisms use such a large supermolecule for oxygen transport remains unclear. Atomic-resolution X-ray crystallographic analysis is necessary to unveil the detailed molecular structure of this mysterious large molecule. However, its propensity to dissociate in solution has hampered the crystallization of its intact form. In the present study, we successfully obtained the first crystals of an intact decameric molluscan hemocyanin. The diffraction dataset at 3.0-angstrom resolution was collected by merging the datasets of two isomorphic crystals. Electron microscopy analysis of the dissolved crystals revealed cylindrical particles. Furthermore, self-rotation function analysis clearly showed the presence of a fivefold symmetry with several twofold symmetries perpendicular to the fivefold axis. The absorption spectrum of the crystals showed an absorption peak around 345 nm. These results indicated that the crystals contain intact hemocyanin decamers in the oxygen-bound form. (C) 2015 Elsevier Inc. All rights reserved.
• Antioxidant and sensory properties of protein hydrolysate derived from Nile tilapia (Oreochromis niloticus) by one- and two-step hydrolysis

  Suthasinee Yarnpakdee, Soottawat Benjakul, Hordur G. Kristinsson, Hideki Kishimura

  JOURNAL OF FOOD SCIENCE AND TECHNOLOGY-MYSORE [TC=109] 52 (6) 3336 - 3349 0022-1155 2015/06 [Refereed][Not invited]
   

  Antioxidant and sensory properties of Nile tilapia protein hydrolysates prepared by one-and two-step hydrolysis using commercial proteases were investigated. Hydrolysates prepared using single protease including Alcalase (HA), Flavourzyme (HF), Protamex (HPr) and papain (HPa) had increases in antioxidant activities as the degree of hydrolysis (DH) increased up to 40 % (P<0.05). Amongst all hydrolysates, HA having 40 % DH showed the highest antioxidant activities. When HA was further hydrolysed by papain, the resulting hydrolysate (HAPa) exhibited the highest antioxidant activities for all assays tested (P<0.05). ABTS radical scavenging activity and metal chelating of HAPa generally remained constant in a wide pH range (1-11) and during heating at 30-100 degrees C. Both activities increased in the simulated gastrointestinal tract model system, especially in intestine condition. HAPa (100-1,000 ppm) could retard lipid oxidation in beta-carotene-linoleate and lecithin-liposome model systems in a dose dependent manner. Peptides in both HA and HAPa with molecular weight of 513 Da and 1,484 Da possessed the strongest ABTS radical scavenging activity and metal chelating activity, respectively. The amino acid profile of both HA and HAPa contained a high amount of hydrophobic amino acids (38.26-38.85 %) and had glutamic acid/glutamine, lysine and aspartic acid/asparagine as the dominant amino acids. However, HAPa showed a higher acceptability than did HA, owing to the lower bitterness. Therefore, the use of Alcalase in combination with papain for hydrolysis of protein isolate rendered the hydrolysate with antioxidant properties and reduced bitterness, which could serve as the functional supplement.
• PURIFICATION AND CHARACTERIZATION OF EXTRACELLULAR GELATINOLYTIC PROTEASE FROM BACILLUS AMYLOLIQUEFACIENS H11

  Samart Sai-Ut, Soottawat Benjakul, Punnanee Sumpavapol, Hideki Kishimura

  JOURNAL OF FOOD BIOCHEMISTRY 39 (1) 119 - 128 0145-8884 2015/02 [Refereed][Not invited]
   

  Extracellular gelatinolytic enzyme from Bacillus amyloliquefaciensH11 was purified by gel filtration chromatography on Sephacryl S-200 and ion exchange chromatography on diethylaminoethyl-cellulose with 35% yield and 14-fold increase in purity. Based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the molecular weight of the purified enzyme was estimated to be 21kDa. The optimum gelatinolytic activities of purified enzyme toward porcine gelatin were 50C and pH8.0. The inhibitor study revealed that the purified enzyme was a metallo-serine protease and activated by Ca2+ and Mg2+ but resistant to Triton X-100 and methanol at a concentration of 10% (v/v). Among all gelatins, that from unicorn leatherjacket fish skin was the most preferred for hydrolysis by the purified enzyme, in comparison with porcine and tilapia counterparts. Thus, the enzyme from B.amyloliquefaciensH11 could be used as a potential protease for production of gelatin hydrolysate. Practical ApplicationsExtracellular protease from Bacillus amyloliquefaciensH11 plays a specific catalytic role in the hydrolysis of gelatin and can be used for production of gelatin hydrolysate with bioactivities. It can also be a potential alternative for commercial protease in conversion of marine processing by-products to generate high value-added products.
• Molecular characteristics and properties of gelatin from skin of seabass with different sizes

  Sittichoke Sinthusamran, Soottawat Benjakul, Hideki Kishimura

  INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES [TC=47] 73 146 - 153 0141-8130 2015/02 [Refereed][Not invited]
   

  Gelatin was extracted from the skin of seabass (Lutes calcarifer) with different average sizes (2, 4 and 6 kg/fish), termed G2, G4 and G6, respectively and their characteristics and functional properties were determined. Yields of G2, G4 and G6 were 38.22, 40.50 and 43.48% (based on dry weight), respectively. G2 contained cc-chains as dominant component, whilst G4 and G6 comprised alpha-, beta- and gamma-chains with a larger content of high MW cross-links. All gelatins had the similar imino acid (hydroxyproline and proline) content. Net charge of G2, G4 and G6 became zero at pH of 6.73, 6.41 and 7.12, respectively. Amongst all gelatin samples, G6 exhibited the highest gel strength (321.5g) (p < 0.05), but had the lowest turbidity (p < 0.05). Gels of G6 sample had the lower L*-value but higher a*-, b*- and Delta E*-value, compared with others. Gelling and melting temperatures of all gelatins were 17.09-19.01 and 26.92-28.85 degrees C, respectively. Furthermore, all gelatins were able to set at room temperature, regardless of size of seabass used. G6 had the shorter setting time at room temperature than others. Therefore, size of seabass, in which skin was used for gelatin extraction, had the impact on yield, composition and properties of resulting gelatin. (C) 2014 Elsevier B.V. All rights reserved.
• CHARACTERISTICS OF GELATIN FROM SWIM BLADDER OF YELLOWFIN TUNA (THUNNUS ALBACORES) AS INFLUENCED BY EXTRACTING TEMPERATURES

  O. Kaewdang, S. Benjakul, T. Prodpran, T. Kaewmanee, H. Kishimura

  ITALIAN JOURNAL OF FOOD SCIENCE [TC=159] 27 (3) 366 - 374 1120-1770 2015 [Refereed][Not invited]
   

  Gelatin was extracted from the swim bladder of yellowfin tuna (Thunnus albacores) at different temperatures (60, 70 and 80 degrees C) with the extraction yields of 35.6%, 41.1% and 47.3% (dry weight basis), respectively. The a-chains of gelatin decreased with increasing extraction temperatures. Similar amino acid compositions were noticeable among all gelatins, in which glycine constituted the major amino acid. Imino acids ranged from 169 to 172 residues/1,000 residues. The gel strength of gelatin extracted at lower temperature was higher than that of gelatins extracted at higher temperatures. Gelling and melting temperatures for swim bladder gelatin were 11.07-5.24 and 20.36-22.33 degrees C, respectively. Higher gelling and melting points were observed for gelatin extracted at lower temperatures. Microstructure of gel of gelatin extracted at 60 degrees C was finer with smaller voids, compared with others. FTIR spectra of obtained gelatins revealed the significant loss of molecular order of the triple-helix. Thus, extraction temperatures showed the direct impact on characteristics of gelatin from swim bladder.
• Characteristics of Pepsin-Solubilised Collagen from the Skin of Splendid Squid (Loligo formosana)

  Phanat Kittiphattanabawon, Sitthipong Nalinanon, Soottawat Benjakul, Hideki Kishimura

  JOURNAL OF CHEMISTRY [TC=45] 2015 1 - 8 2090-9063 2015 [Refereed][Not invited]
   

  Pepsin-solubilised collagen from the skin of splendid squid (SC) was isolated, partially purified by salt precipitation and dialysis prior to characterisation. The yield of SC was 75.3% (dry weight basis). SC with high purity was obtained as shown by the distinct UV absorption peak at 232 nm and high hydroxyproline content. Total sugar content of SC was 4.70% (dry weight basis), which was higher than that of collagen from calf skin (CC) (1.45% dry weight basis) (P < 0.05). Based on SDS-PAGE and elution profile, SC might contain the mixed types of collagen (type SQ-I and type SQ-II), in which alpha- and beta-chains were the major components. SC was rich in glycine and had high content of imino acids (189 residues/1000 residues). The degradation induced by chymotrypsin and lysyl endopeptidase was more pronounced in CC, compared with SC. The maximum transition temperature (T-max) of SC was 34.1 degrees C, which was about 7 degrees C lower than that of CC. Fourier transform infrared spectra revealed that the triple-helical structure of SC was predominant with the copresence of carbohydrate moieties. Therefore, the skin of splendid squid, a byproduct from squid processing, can be an alternative source for collagen production.
• Characteristics of collagens from the swim bladders of yellowfin tuna (Thunnus albacares)

  Onouma Kaewdang, Soottawat Benjakul, Thammarat Kaewmanee, Hideki Kishimura

  FOOD CHEMISTRY 155 264 - 270 0308-8146 2014/07 [Refereed][Not invited]
   

  Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) were extracted from the swim bladders of yellowfin tuna (Thunnus albacares) with yields of 1.07% and 12.10%, respectively. Based on electrophoretic patterns, both ASC and PSC consisted of two alpha-chains (alpha 1 and alpha 2) and were characterised to be type I collagen. ASC had higher beta-chains than PSC. Imino acid contents of ASC and PSC were 128 and 169 residues/1000 residues, respectively. Fourier transform infrared (FTIR) spectra of both ASC and PSC were similar and revealed the presence of a triple helix. Both ASC and PSC had the highest solubility at acidic pHs. From zeta potential analysis, a net charge of zero was found at pH 6.05 and 5.93 for ASC and PSC, respectively. T-max of ASC and PSC were 32.97 and 33.92 degrees C, respectively. The swim bladders of yellowfin tuna could therefore serve as an alternative source of collagen for future applications. (C) 2014 Elsevier Ltd. All rights reserved.
• Characteristics and gel properties of gelatin from skin of seabass (Lutes calcarifer) as influenced by extraction conditions

  Sittichoke Sinthusamran, Soottawat Benjakul, Hideki Kishimura

  FOOD CHEMISTRY [TC=189] 152 276 - 284 0308-8146 2014/06 [Refereed][Not invited]
   

  Characterisics and gel properties of gelatin from seabass skin, as influenced by extraction conditions, were studied. Yields of gelatin extracted at 45 and 55 degrees C for various times were 51.6-57.3% and 62.0-66.4% (dry weight basis), respectively. All gelatins contained beta-chain and alpha-chains as the predominant components and showed a high imino acid content (198-202 residues/1000 residues). Generally, the gel strength of gelatins decreased as the extraction temperature and time increased. Gelatin extracted at 45 degrees C for 3 h exhibited the highest gel strength (369 g). Gelling and melting temperatures for seabass skin gelatin were 19.5-20.0 and 26.3-27.0 degrees C, respectively. All gelatins could be set at 25 degrees C within 30 min, however gelatins extracted at 45 degrees C had a shorter setting time than those extracted at 55 degrees C (P < 0.05). Gelatin from seabass skin showed a higher gel strength than bovine gelatin and could be used as a potential replacement for land animal gelatins. (C) 2013 Elsevier Ltd. All rights reserved.
• Anionic Trypsin from the Pyloric Ceca of Pacific Saury (Cololabis saira): Purification and Biochemical Characteristics

  Sappasith Klomklao, Hideki Kishimura, Soottawat Benjakul

  JOURNAL OF AQUATIC FOOD PRODUCT TECHNOLOGY 23 (2) 186 - 200 1049-8850 2014/03 [Refereed][Not invited]
   

  Anionic trypsin from Pacific saury (Cololabis saira) pyloric ceca was purified to homogeneity by ammonium sulfate precipitation, ion-exchange chromatography, and gel filtration chromatography. It was purified to 53.7-fold with a yield of 6.1%. The apparent molecular weight of the enzyme was about 24 kDa, as determined by size exclusion chromatography and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). On native-PAGE, trypsin showed a single band. The purified anionic trypsin displayed optimal activity at pH 8.5 and 55 degrees C. The enzyme was stable at neutral and alkaline pH and in the temperature range of 20-50 degrees C. The stability was affected by the calcium ion. The activity of purified anionic trypsin was completely inhibited by soybean trypsin inhibitor and N-p-tosyl-L-lysine chloromethyl ketone (TLCK) and partially inhibited by ethylenediaminetetraacetic acid (EDTA). NaCl (0-30%) decreased the activity in a concentration-dependent manner. The kinetic trypsin constants K-m and K-cat were 0.19 mM and 210 s(-1), respectively, while the catalytic efficiency (K-cat/K-m) was 1105.26 s(-1) mM(-1). The N-terminal amino acid sequences of anionic trypsin, IVGGYECQAH, were found and were homologous to those of trypsin from other fish species.
• Characteristics and antioxidative activity of carotenoprotein from shells of Pacific white shrimp extracted using hepatopancreas proteases

  Theeraphol Senphan, Soottawat Benjakul, Hideki Kishimura

  FOOD BIOSCIENCE [TC=56] 5 54 - 63 2212-4292 2014/03 [Refereed][Not invited]
   

  Carotenoprotein from shells of Pacific white shrimp (Litopenaeus uannamei) was extracted with the aid of proteases from hepatopancreas of the same species at various levels (5-30 units/g shrimp shell) for different times (0-180 min). Recovery of carotenoprotein increased with increasing protease levels and hydrolysis times, but mainly reached the plateau at 120 min of hydrolysis. Carotenoprotein contained astaxanthin and astaxanthindiester as major carotenoids. Carotenoids extracted from carotenoprotein showed increasing ABTS, DPPH radical scavenging activities, FRAP and metal chelating activity when the concentrations increased up to 5 mg/ml (p <0.05). Carotenoprotein consisted of 73.58% protein, 21.87% lipids and 2.63% ash contents. It was rich in essential amino acids and Asp/ Asn and Clu/Cln were found as dominant amino acids. Therefore, carotenoprotein from shell of Pacific white shrimp could be successfully extracted using shrimp hepatopancreas proteases and could serve as the value-added nutritive food ingredients or as the animal feed. (C) 2013 Elsevier Ltd. All rights reserved.
• Molecular and immunological characterization of -component (Onc k 5), a major IgE-binding protein in chum salmon roe

  Yutaka Shimizu, Hideki Kishimura, Gaku Kanno, Atsushi Nakamura, Reiko Adachi, Hiroshi Akiyama, Kazuhiko Watanabe, Akihiko Hara, Motohiro Ebisawa, Hiroki Saeki

  INTERNATIONAL IMMUNOLOGY 26 (3) 139 - 147 0953-8178 2014/03 [Refereed][Not invited]
   

  Molecular characterization of a major allergen from salmon roe.Salmon roe has a high allergic potency and often causes anaphylaxis in Japan. The major allergic protein of salmon roe is -component, which is a 35kDa vitellogenin fragment consisting of two subunits. To elucidate structural information and immunological characteristics, -component and the subunit components were purified from chum salmon (Onchorhincus keta) roe and vitellogenin-encoding mRNA was used to prepare -component subunit-encoding cDNA. This was PCR-amplified, cloned and sequenced and the deduced amino acid sequence compared with partial sequences of -component obtained by peptide mapping. The recombinant -component subunit was produced by bacterial expression in Escherichia coli and its IgE-binding ability was measured by ELISA using the sera of a patient allergic to salmon roe. This was then compared with that of the native -component with and without carboxymethylation. Following successful cloning of the cDNA encoding the -component subunit, 170 amino acid residues were deduced and matched with the amino acid sequences of 121 and 88 residues in the 16kDa and 18kDa subunits, respectively. The sequences of both -component subunits were almost identical, and the predicted secondary structure of the -component showed a high content of -pleated sheets and no -helices. There was no difference in IgE-binding ability between the native and recombinant -component subunits at the same protein concentration, regardless of carboxymethylation. In conclusion, -component is a homodimer protein composed of two isoform subunits having the same level of IgE-binding ability and, therefore, allergenic identity.
• Optimization of gelatinolytic enzyme production by B. amyloliquefaciens sp. H11 through Plackett–Burman design and response surface methodology

  Samart Sai-Ut, Soottawat Benjakul, Punnanee Sumpavapol, Hideki Kishimura

  International Aquatic Research 6 (1) 1 - 10 2008-6970 2014 [Refereed][Not invited]
   

  Bacillus amyloliquefaciens H11 has been proven as a potential producer of extracellular protease with capacity of hydrolyzing gelatin. Therefore, the cultivation conditions for the enhanced production of gelatinolytic enzyme from a newly isolated B. amyloliquefaciens H11 was investigated using Plackett–Burman design and response surface methodology. Three significant variables (agitation speed, cultivation time and fish gelatin concentration) were selected for optimization. Increases in speed of agitation and fish gelatin concentration markedly increased the production of gelatinolytic enzyme. Gelatin concentration and cultivation time showed significant interaction and both variables played the important role in enzyme production. The maximal gelatinolytic enzyme production in the basal medium was 2,801 U/mL under the following optimal condition: agitation speed of 234 rpm, 8.36 g/L of fish gelatin and 31 h of cultivation. The predicted model fitted well with the experimental results (2,734 ± 101 U/mL). Fourteen-fold increase in yield was achieved, compared with the basal condition (212 U/mL). Thus, cultivation of B.amyloliquefaciens H11 under the optimal condition could enhance the production of gelatinolytic enzyme effectively.
• Optimum extraction and recovery of trypsin inhibitor from yellowfin tuna (Thunnus albacores) roe and its biochemical properties

  Sappasith Klomklao, Soottawat Benjakul, Hideki Kishimura

  INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY 49 (1) 168 - 173 0950-5423 2014/01 [Refereed][Not invited]
   

  Effect of lipid removal, extraction medium and extraction time on the isolation and recovery of trypsin inhibitor from yellowfin tuna (Thunnus albacores) roe was investigated. Trypsin inhibitor extracted from defatted tuna roe showed the higher specific inhibitory activity than extracted from origin tuna roe. Optimal extraction medium was attained by shaking the defatted yellowfin tuna roe powder in 10mm Na phosphate buffer (pH 7.0) containing 0.5m NaCl (P<0.05). The extraction time affected the inhibitor recovery significantly (P<0.05). The extraction time of 30min was optimum for recovery of trypsin inhibitor from yellowfin tuna roe. The biochemical properties of trypsin inhibitor from yellowfin tuna roes were also determined. The inhibitor was stable to heat treatment up to 60C and over a broad pH range (5-8). Increasing the concentration of salt (up to 3%, w/v) did not significantly decrease the trypsin inhibitory activity. However, the activity decreased when trypsin inhibitor was incubated with metal ions at ambient temperature for 30min.
• Effect of Drying Methods on Odorous Compounds and Antioxidative Activity of Gelatin Hydrolysate Produced by Protease from B. Amyloliquefaciens H11

  Samart Sai-Ut, Soottawat Benjakul, Punnanee Sumpavapol, Hideki Kishimura

  DRYING TECHNOLOGY 32 (13) 1552 - 1559 0737-3937 2014 [Refereed][Not invited]
   

  Gelatin hydrolysates with antioxidative activity produced by protease from Bacillus amyloliquefaciens H11 with different hydrolysis times were prepared. Alpha-amino group content and antioxidative activities increased with increasing hydrolysis time (p < 0.05). When gelatin hydrolysate prepared with hydrolysis time of 3 h (GH-3H) was subjected to freeze drying and spray drying, the powder obtained from spray drying showed a decrease in antioxidant activity as measured by DPPH and ABTS radical scavenging activities, ferric-reducing antioxidant power, and metal chelating activity. Spray-dried gelatin hydrolysate (GH-3H-SD) showed higher whiteness with lower fishy odor and off-odor associated with fermentation. This was concomitant with the decreases in several odorous compounds in the sample, except for nonanal, which was higher in comparison with the powder obtained by freeze drying. Thus, spray drying could be an effective drying method to improve color and reduce undesirable odor of gelatin hydrolysate.
• Chemical compositions and nutritional value of Asian hard clam (Meretrix lusoria) from the coast of Andaman Sea

  Supatra Karnjanapratum, Soottawat Benjakul, Hideki Kishimura, Yung-Hsiang Tsai

  FOOD CHEMISTRY [TC=88] 141 (4) 4138 - 4145 0308-8146 2013/12 [Refereed][Not invited]
   

  Chemical compositions and nutritive value of the edible portions including foot, mantle and viscera of Asian hard clam (Meretrix lusoria) harvested from the coast of Andaman Sea were determined. Proximate compositions varied with portions tested. Edible portions had moisture (76.23-84.22%) and protein (9.09-12.75%) as the major components. Carbohydrate (0.32-7.89%), fat (1.58-6.58%) and ash (1.23-2.58%) were also found at various levels, dependent upon portions. Myofibrillar proteins were observed as the major fraction in foot (40.54%) and mantle (31.65%), whilst non-protein nitrogen constituents were dominant in the viscera (36.85%). All portions contained a large amount of essential amino acids (167.66-187.63 mg/g sample), in which leucine (30.91-36.96 mg/g sample) and lysine (35.24-36.03 mg/g sample) were predominant. They were rich in polyunsaturated fatty acids (46.84-49.18% of total fatty acid) with high level of DHA (13.33-16.47 % of total fatty acids) and EPA (4.75-7.11% of total fatty acids). Cholesterol of 0.07-0.21% wet weight was detected. All portions were also rich in macro- (Na, K, Ca and Mg) and micro- (Fe, Zn, Cu and Cr) minerals. Therefore, Asian hard clam is an excellent source of several nutrients, which could be beneficial for the health of the consumers. (C) 2013 Elsevier Ltd. All rights reserved.
• Comparative study on chemical compositions and properties of protein isolates from mung bean, black bean and bambara groundnut

  Tanaji G. Kudre, Soottawat Benjakul, Hideki Kishimura

  JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE 93 (10) 2429 - 2436 0022-5142 2013/08 [Refereed][Not invited]
   

  BACKGROUND Different legume seeds may have different protein compositions and properties, thereby affecting applications in food systems. This study aimed to extract and characterize protein isolates from legumes grown in Thailand, including mung bean (MBPI), black bean (BBPI) and bambara groundnut (BGPI). RESULTS All protein isolates had a protein content in the range of 85.2-88.2%. The highest trypsin inhibitory activity was found in BGPI. All protein isolates exhibited satisfactory balanced amino acids with respect to the FAO/WHO pattern. MBPI and BBPI had three predominant proteins with a molecular weight (MW) range of 42-54 kDa, whereas BGPI had two dominant proteins with MW of 52 and 62kDa. Based on differential scanning calorimetric analysis, MBPI and BGPI had two endothermic peaks, whereas three peaks were found for BBPI. All protein isolates exhibited similar FTIR spectra, indicating similarity in functional group and structure. All protein isolates showed a minimum protein solubility at around pH 4-5. CONCLUSION All protein isolates were important sources of proteins with high lysine content. Isolates from different legumes showed slight differences in physiochemical and thermal properties. Those isolates can be used as proteinaceous ingredients in a variety of food products such as salad dressing, meat products and desserts. (c) 2013 Society of Chemical Industry
• Functional properties and antioxidative activity of protein hydrolysates from toothed ponyfish muscle treated with viscera extract from hybrid catfish

  Sappasith Klomklao, Soottawat Benjakul, Hideki Kishimura

  INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY 48 (7) 1483 - 1489 0950-5423 2013/07 [Refereed][Not invited]
   

  Functional properties and antioxidative activity of a protein hydrolysate prepared from toothed ponyfish (Gazza minuta) muscle, using viscera extract from hybrid catfish (Clarias macrocephalusxClarias gariepinus), with a degree of hydrolysis (DH) of 70%, were investigated. The protein hydrolysate had a good solubility. It was soluble over a wide pH range (3-9), in which more than 77% solubility was obtained. The emulsifying activity index of the protein hydrolysate decreased with increasing concentration (P<0.05). Conversely, the foaming abilities increased as the hydrolysate concentrations increased (P<0.05). Protein hydrolysate exhibited the increases in 2,2-diphenyl-1-picrylhydrazyl (DPPH), 2,2-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) radical scavenging activities, ferric reducing power (FRAP) and metal chelating activity as hydrolysate concentration increased (P<0.05). ABTS radical scavenging activity of protein hydrolysate was stable when heated at 100 degrees C for 180min and subjected to a wide pH range (1-11). Therefore, protein hydrolysate from the muscle of toothed ponyfish produced by viscera extract from hybrid catfish can be used as a promising source of functional peptides with antioxidant properties.
• Comparative study on molecular characteristics of acid soluble collagens from skin and swim bladder of seabass (Lates calcarifer)

  Sittichoke Sinthusamran, Soottawat Benjakul, Hideki Kishimura

  FOOD CHEMISTRY [TC=160] 138 (4) 2435 - 2441 0308-8146 2013/06 [Refereed][Not invited]
   

  Acid soluble collagens (ASCs) from skin and swim bladder of seabass (Lates calcarifer) were isolated and comparatively characterised. Higher yield (28.5%) was obtained for ASC from swim bladder, compared with that from skin (15.8%). ASCs from both skin and swim bladder had the similar protein patterns and were identified to be type I. Both alpha- and beta-chains constituted as major components. Fourier transform infrared (FTIR) spectra revealed that both ASCs were triple helix in structure. ASC from both sources contained glycine as the major amino acid with imino acids (proline and hydroxyproline) of 194-195 residues/1000 residues). Peptide maps of both ASCs digested by chymotrypsin and trypsin showed slight differences, suggesting some differences in their primary structure. The thermal transition temperature of swim bladder ASC (35.02 degrees C) was slightly higher than its skin counterpart (33.33 degrees C). Based on zeta potential analysis, ASCs from skin and swim bladder had a net charge of zero at pH 6.46 and 6.64, respectively. Therefore, both the skin and swim bladder of seabass could be used potentially for collagen extraction. (C) 2012 Elsevier Ltd. All rights reserved.
• Chemical and Thermal Properties of Freshwater Prawn (Macrobrachium rosenbergii) Meat

  Chodsana Sriket, Soottawat Benjakul, Wonnop Visessanguan, Hideki Kishimura, Kenji Hara, Asami Yoshida

  JOURNAL OF AQUATIC FOOD PRODUCT TECHNOLOGY 22 (2) 137 - 145 1049-8850 2013/03 [Refereed][Not invited]
   

  Chemical compositions and thermal properties of cultured freshwater prawn meat (FPM) were studied. FPM contained 83.2% protein (dry basis), 62.7% of which was myofibrillar protein. Pepsin-soluble collagen (PSC) and insoluble collagen (ISC) contents were 0.63 and 0.32%, respectively. Both collagens were similar to type V collagen from porcine placenta. Glutamic acid/glutamine, arginine, aspartic acid/asparagine, and lysine were abundant amino acids in FPM. Glycine, proline, hydroxyproline, and aspartic acid/asparagine were predominant in both collagens. FPM exhibited thermal transition temperatures (Tmax) of 48.3 and 64.7 degrees C, whereas Tmax of PSC and ISC were 43.0 and 46.0 degrees C, respectively. Textural changes in FPM during post-mortem storage on ice are plausibly dependent upon its compositional and thermal properties.
• Effects of protein isolates from black bean and mungbean on proteolysis and gel properties of surimi from sardine (Sardinella albella)

  Tanaji Kudre, Soottawat Benjakul, Hideki Kishimura

  LWT-FOOD SCIENCE AND TECHNOLOGY [TC=173] 50 (2) 511 - 518 0023-6438 2013/03 [Refereed][Not invited]
   

  Effects of protein isolates from black bean (BBPI) and mungbean (MBPI) on proteolysis and gelling properties of surimi from sardine (Sardinella albella) were investigated. Both BBPI and MBPI showed inhibitory activity against proteolysis in kamaboko (40/90 degrees C) and modori (65/90 degrees C) gels in a concentration-dependent manner. Myosin heavy chain (MHC) was more retained in both gels when the concentration of both protein isolates increased up to 1 g 100 g(-1). This was associated with the increased breaking force and deformation as well as lowered degradation as evidenced by the decrease in trichloroacetic acid-soluble peptide content (p < 0.05). Whiteness of kamaboko and modori gels slightly decreased with increasing BBPI or MBPI levels (p < 0.05). However, water-holding capacity of both gels increased with increasing levels of both protein isolates. Microstructure of kamaboko and modori gels added with 1 g 100 g(-1) BBPI or MBPI was finer and denser with more ordered structure than that of the control. Generally, BBPI showed slightly higher gel strengthening effects and inhibition against proteolysis of surimi gels than MBPI. Therefore, proteolysis of sardine surimi, associated with endogenous proteases, could be retarded by the addition of BBPI or MBPI, leading to the increased gel strength. (C) 2012 Elsevier Ltd. All rights reserved.
• Use of viscera extract from hybrid catfish (Clarias macrocephalus × Clarias gariepinus) for the production of protein hydrolysate from toothed ponyfish (Gazza minuta) muscle

  Sappasith Klomklao, Hideki Kishimura, Soottawat Benjakul

  Food Chemistry 136 (2) 1006 - 1012 0308-8146 2013/01/15 [Refereed][Not invited]
   

  Proteolytic activity of viscera extract from hybrid catfish (Clarias macrocephalus × Clarias gariepinus) was studied. The optimal pH and temperature were 9.0 and 50 °C, respectively, when toothed ponyfish (Gazza minuta) muscle was used as a substrate. When viscera extract from hybrid catfish was used for the production of protein hydrolysate from toothed ponyfish muscle, extract concentration, reaction time, and fish muscle/buffer ratio affected the hydrolysis and nitrogen recovery (NR) (p < 0.05). Optimum conditions for toothed ponyfish muscle hydrolysis were 3.5% hybrid catfish viscera extract, 15 min reaction time and fish muscle/buffer ratio of 1:3 (w/v). High correlation between the degree of hydrolysis (DH) and NR (R2 = 0.974) was observed. Freeze-dried hydrolysate had a high protein content (89.02%, dry weight basis) and it was brownish yellow in colour (L * = 63.67, a* = 6.33, b* = 22.41). The protein hydrolysate contained a high amount of essential amino acids (48.22%) and had arginine and lysine as the dominant amino acids. © 2012 Elsevier Ltd. All rights reserved.
• Characteristics and functional properties of gelatin from splendid squid (Loligo formosana) skin as affected by extraction temperatures

  Muralidharan Nagarajan, Soottawat Benjakul, Thummanoon Prodpran, Ponusa Songtipya, Hideki Kishimura

  FOOD HYDROCOLLOIDS [TC=294] 29 (2) 389 - 397 0268-005X 2012/12 [Refereed][Not invited]
   

  Gelatin was extracted from the skin of splendid squid (Loligo formosana) at different temperatures (50, 60, 70 and 80 degrees C) with extraction yield of 8.8%, 21.8%, 28.2%, and 45.3% (dry weight basis) for G50, G60, G70 and G80, respectively. Gelatin from the skin of splendid squid had a high protein content (similar to 90%) with low moisture (8.63-11.09%), fat (0.22-0.31%) and ash contents (0.17-0.68%). Gelatin extracted at higher temperature (G80) had a relatively higher free amino group content than gelatin extracted at lower temperatures (G50, G60 and G70) (P < 0.05). All gelatins contained alpha- and beta-chains as the predominant components. Amino acid analysis of gelatin revealed the high proline and hydroxyproline contents for G50 and G60. FTIR spectra of obtained gelatins revealed the significant loss of molecular order of the triple-helix. The gel strength of gelatin extracted at lower temperature (G50) was higher than that of gelatins extracted at higher temperatures including G60, G70 and G80, respectively. The net charge of G50, G60, G70 and G80 became zero at pHs of 6.84, 5.94, 5.49, and 4.86, respectively, as determined by zeta potential titration. Gelatin extracted at higher temperature (G80) had the lower L* value but higher a* and b* values, compared with those extracted at lower temperatures (P < 0.05). Emulsion activity index decreased, whilst emulsion stability index, foam expansion and stability increased as the concentration (1-3%) increased (P < 0.05). Those properties were governed by extraction temperatures of gelatin. Thus gelatin can be successfully extracted from splendid squid skin using the appropriate extraction temperature. (C) 2012 Elsevier Ltd. All rights reserved.
• Transcriptome Analysis of the Duodenum, Pancreas, Liver, and Muscle from Diabetic Goto-Kakizaki Rats Fed a Trypsin Inhibitors Derived from Squid Viscera

  Kohsuke Adachi, Kana Fukumorita, Michihiro Araki, Nobuhiro Zaima, Zhi-Hong Yang, Satoru Chiba, Hideki Kishimura, Hiroki Saeki

  JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 60 (22) 5540 - 5546 0021-8561 2012/06 [Refereed][Not invited]
   

  Trypsin inhibitors (TIs) have various nutritional effects. However, a detailed mechanism for their effects, especially on the gene expression patterns in various tissues, remains unknown. Here, we used transcriptome techniques and gene ontology (GO) analysis to examine the effects of squid TI (sqTI), a biochemically stable peptide, on diabetic Goto-Kakizaki rats after feeding for 10 weeks. We demonstrated that downregulation of SREBP1c in the liver via duodenal/pancreatic hormones suppresses the blood cholesterol level. Consistently, in GO analysis, the term "cholesterol biosynthetic process" was enriched among downregulated genes. No hypoglycemic or insulinotropic effects were observed, in contrast to the results from our previous studies (single stimulation with the same dose of TI), which can be partly ascribed to the inactive responses of the duodenum and pancreas in this condition.
• Immunomodulatory Properties of Highly Viscous Polysaccharide Extract from the Gagome Alga (Kjellmaniella crassifolia)

  Shigeru Katayama, Toshihiro Nishio, Hideki Kishimura, Hiroki Saeki

  PLANT FOODS FOR HUMAN NUTRITION 67 (1) 76 - 81 0921-9668 2012/03 [Refereed][Not invited]
   

  Marine brown algae are rich in sulfated polysaccharides, which have the ability to form gels and viscous solution. Sulfated polysaccharides exhibit many biological activities; however, little is known whether the viscoelastic property in the polysaccharide extract is correlated with biological activities. We examined the immunomodulatory properties of highly viscous polysaccharide extract (HVPE) from Gagome Kjellmaniella crassifolia in a murine model, and the effects were compared with those of a less viscous polysaccharide extract (LVPE). HVPE or LVPE (10, 30, and 100 mg/kg/day) were orally administered to C57BL/6 mice for 14 days. Secretions of cytokine and IgA in Con A-stimulated spleen and Peyer's patch (PP) cells and phagocytic activity of peritoneal macrophages was determined. IFN-gamma, IL-12, IL-6, and IgA secretions showed high levels in spleen cell cultures from mice administered HVPE, whereas these effects were diminished in the LVPE-administered mice. The phagocytic activity of peritoneal macrophages was enhanced by the continuous oral administration of HVPE, and these effects were higher than those of LVPE. Furthermore, an increase in IgA secretion by administration of HVPE was observed in Con A-stimulated PP cells. These results suggest that the polysaccharide extract from K. crassifolia has immunomodulatory activities, which depend on the viscosity.
• In vitro digestion of major allergen in salmon roe and its peptide portion with proteolytic resistance

  Shingo Fujita, Yutaka Shimizu, Hideki Kishimura, Kazuhiko Watanabe, Akihiko Hara, Hiroki Saeki

  FOOD CHEMISTRY 130 (3) 644 - 650 0308-8146 2012/02 [Refereed][Not invited]
   

  A fish yolk protein, beta'-component (beta'-c), is the major allergen in chum salmon roe. The effect of proteolysis on the allergenicity of beta'-c was estimated. Changes in the IgE-binding ability of beta'-c upon pepsin and trypsin digestion were investigated by monitoring the proteolytic cleavage. In the pepsin-trypsin digestion of chum salmon yolk protein, the beta'-c contained therein was degraded in a manner similar to that of other yolk proteins, but digestion fragments with a molecular mass of >10 kDa remained throughout the digestion process. Specifically, the peptide sequence between 31-Y and 119-Q (10 kDa) was stable to pepsin-trypsin digestion and the portion showed high IgE-binding ability. As a result, pepsin-trypsin digestion had little effect on the IgE-binding ability of beta'-c. These results suggest that beta'-c reaches the small intestine in the form of high-molecular-mass components with IgE-binding ability in vivo. (C) 2011 Elsevier Ltd. All rights reserved.
• A TRYPSIN INHIBITOR IN THE VISCERA OF JAPANESE COMMON SQUID (TODARODES PACIFICUS) ELICITS INSULINOTROPIC EFFECTS IN DIABETIC GK RATS

  Hideki Kishimura, Kana Fukumorita, Kohsuke Adachi, Satoru Chiba, Yujiro Nagai, Shigeru Katayama, Shigeru Nakajima, Hiroki Saeki

  JOURNAL OF FOOD BIOCHEMISTRY 36 (1) 93 - 98 0145-8884 2012/02 [Refereed][Not invited]
   

  The potential use of trypsin inhibitors (TI) present in the viscera of Japanese common squid (Todarodes pacificus) was examined for diabetes treatment. In a single-glucose tolerance test, the crude TI (C-TI) fraction significantly stimulated insulin secretion by normal Wistar rats and by diabetic GK rats. The highly purified TI (H-TI) fraction displayed the same effect on the glucose tolerance test with the GK rats. The TI activity of C-TI was not decreased by pepsin or chymotrypsin digestion in vitro, and the C-TI fraction did not have a-glucosidase inhibitory activity. These results indicate that the substance with the stimulating effect on insulin secretion in rats is the squid TI and that the hypoglycemic effect on glucose tolerance in GK rats is related to an improvement of insulin secretion due to the squid TI.
• Characteristics of menhaden oil ethanolysis by immobilized lipase in supercritical carbon dioxide

  Sang-Kyu Shin, Jeong-Eun Sim, Hideki Kishimura, Byung-Soo Chun

  JOURNAL OF INDUSTRIAL AND ENGINEERING CHEMISTRY 18 (1) 546 - 550 1226-086X 2012/01 [Refereed][Not invited]
   

  Ethanolysis of menhaden oil was performed with 1,3-regiospecific lipase to produce diglycerides and monoglycerides containing polyunsaturated fatty acids, and fatty acid ethyl esters. Immobilized lipases like lipozyme TL-IM (Thermomuces lanuginosa immobilized on silica gel) were used for enzymatic ethanolysis. Ethanolysis was carried out in different processes (solvent free, organic solvent and supercritical fluid system) to compare the reaction rate and yield obtained by menhaden oil ethanolysis. Organic solvent (hexane) and supercritical carbon dioxide (SC-CO2) were used as reaction medium. The reaction products were analyzed by gas chromatography (GC), thin layer chromatography (TLC) and high performance liquid chromatography (HPLC). Higher amounts of ethanol as a substrate caused substrate inhibition which dramatically decreased the reaction rate of ethanolysis. To elucidate the effect of pressure, enzymatic ethanolysis was performed in SC-CO2 at pressures ranging from 75 to 121 bar. Enzymatic ethanolysis of menhaden oil in SC-CO2 decreased by substrate inhibition. Reaction rate and optimum amount of ethanol used were depended on SC-CO2 density individually. Kinetic model with substrate inhibition (dead-end inhibition) by excess ethanol was set up to measure the reaction and inhibition rates. (C) 2011 The Korean Society of Industrial and Engineering Chemistry. Published by Elsevier B.V. All rights reserved.
• Characteristics of acid soluble collagen and pepsin soluble collagen from scale of spotted golden goatfish (Parupeneus heptacanthus)

  K.Matmaroh, S.Benjakul, T.Prodpran, AB.Encarnacion, H.Kishimura

  Food Chemistry [IF=3.655] [TC=258] 129 (3) 1179 - 1186 0308-8146 2011/12 [Refereed][Not invited]
   

  Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) were extracted from scale of spotted golden goatfish (Parupeneus heptacanthus) with the yields of 0.46% and 1.20% (based on dry weight basis), respectively. Both ASC and PSC were characterised as type I collagen, containing alpha(1) and alpha(2) chains. beta and gamma components were also found in both collagens. Based on FUR spectra, the limited digestion by pepsin did not disrupt the triple helical structure of collagen. ASC and PSC contained glycine (336-340 residues/1000 residues) as the major amino acid and had imino acids of 186-189 residues/1000 residues. Maximal transition temperatures (T-max) were 41.58 and 41.01 degrees C for ASC and PSC, respectively. From zeta potential analysis, net charge of zero was found at pH 4.96 and 5.39 for ASC and PSC, respectively. Both collagens exhibited high solubility in acidic pH (2-4) and were soluble in the presence of NaCl at concentration up to 20 and 30 g/l for ASC and PSC, respectively. (C) 2011 Elsevier Ltd. All rights reserved.
• 24 kDa Trypsin: a predominant protease purified from the viscera of hybrid catfish (Clarias macrocephalus x Clarias gariepinus)

  S.Klomklao, S.Benjakul, H.Kishimura, M.Chaijan

  Food Chemistry [IF=3.655] [TC=47] 129 (3) 739 - 746 0308-8146 2011/12 [Refereed][Not invited]
   

  Trypsin was purified to homogeneity from the viscera of hybrid catfish (Clarias macrocephalus x Clarias gariepinus) through ammonium sulphate fractionation and a series of chromatographies including Sephacryl S-200, Sephadex G-50 and DEAE-cellulose. It was purified to 47.6-fold with a yield of 12.7%. Based on native-PAGE, the purified trypsin showed a single band. The molecular weight of purified trypsin was estimated as 24 kDa by size exclusion chromatography and SDS-PAGE. The optimum pH and temperature for N-alpha-p-tosyl-L-arginine methyl ester hydrochloride (TAME) hydrolysis were 8.0 and 60 degrees C, respectively. Trypsin was stable to heat treatment up to 50 degrees C, and over a pH range of 6.0-11.0. Trypsin was stabilized by calcium ion. The trypsin activity was strongly inhibited by soybean trypsin inhibitor and N-p-tosyl-L-lysine chloromethyl ketone and partially inhibited by ethylenediaminetetraacetic acid. Activity decreased continuously as NaCl concentration (0-30%) increased. Apparent K-m value of trypsin was 0.3 mM and K-cat value was 92.1 S-1 for TAME. The N-terminal amino acid sequence of 20 residues of trypsin was IVGGYECQAHSQPPTVSLNA, which is highly homologous with trypsins from other species of fish. (C) 2011 Elsevier Ltd. All rights reserved.
• Extraction, purification and properties of trypsin inhibitor from Thai mung bean (Vigna radiata (L.) R. Wilczek)

  S.Klomklao, S.Benjakul, H.Kishimura, M.Chaijan

  Food Chemistry [IF=3.655] [TC=68] 129 (4) 1348 - 1354 0308-8146 2011/12 [Refereed][Not invited]
   

  A trypsin inhibitor from mung bean (Vigna radiata (L) R. Wilczek) seeds grown in Thailand was extracted and characterised. The optimal extraction medium was attained by shaking the defatted mung been seed powder in distilled water (P < 0.05). The extraction time affected the inhibitor recovery significantly (P < 0.05). The extraction time of 2 h was optimum for the recovery of the trypsin inhibitor from mung bean seeds. The trypsin inhibitor from mung bean seeds was purified by heat-treatment at 90 degrees C for 10 min, followed by ammonium sulphate precipitation with 30-65% saturation and gel filtration on Sephadex G-50. It was purified to 13.51-fold with a yield of 30.25%. Molecular weight distribution and inhibitory activity staining showed that the purified trypsin inhibitor had a molecular weight of 14 kDa. However, the purified inhibitor had no activity under reducing condition (beta ME). The purified inhibitor was heat stable up to 50 min at 90 degrees C. The inhibitory activity was retained over a wide pH range. NaCl, at 0-3% concentration, did not influence the inhibitory activity of the purified trypsin inhibitor from mung bean seeds. (C) 2011 Elsevier Ltd. All rights reserved.
• Cold-adapted structural properties of trypsins from walleye pollock (Theragra chalcogramma) and Arctic cod (Boreogadus saida)

  Gaku Kanno, Hideki Kishimura, Jun Yamamoto, Seiichi Ando, Takeshi Shimizu, Soottawat Benjakul, Sappasith Klomklao, Sitthipong Nalinanon, Byung-Soo Chun, Hiroki Saeki

  EUROPEAN FOOD RESEARCH AND TECHNOLOGY 233 (6) 963 - 972 1438-2377 2011/12 [Refereed][Not invited]
   

  Complementary DNA clones encoding trypsins were isolated from pyloric ceca of cold-adapted fish, walleye pollock (Theragra chalcogramma) (WP-T) and Arctic cod (Boreogadus saida) (AC-T). The isolated full-length cDNA clones of WP-T and AC-T were 852 and 860 bp, respectively, and both cDNAs were contained an open reading frame of 726 bp. WP-T and AC-T seemed to be synthesized as preproenzyme that contains a signal peptide, an activation peptide, and a mature trypsin. Although the amino acid sequence identities of WP-T and AC-T to that of bovine trypsin were 64 and 63%, respectively, they completely conserved the structural features for catalytic function of trypsin. On the other hand, WP-T and AC-T possessed the four Met residues (Met135, Met145, Met175 and Met242) in their molecules and the deletion of Tyr151 and substitution of Pro152 for Gly in their autolysis loops when aligned with the sequences of tropical-zone fish and bovine trypsins. In addition, the contents of charged amino acid residues at the N-terminal regions (positions 20-50) of WP-T and AC-T were extremely higher than those of other fish and bovine trypsins. Moreover, one amino acid (Asn72) and two amino acids (Asn72 and Val75) coordinating with Ca(2+) in bovine trypsin were exchanged for another amino acids in WP-T (His) and AC-T (His and Glu), respectively, and the contents of negative charged amino acids at their Ca(2+)-binding regions were lower than those of tropical-zone fish and bovine trypsins. Therefore, it was considered that these structural characteristics of WP-T and AC-T are closely related to their lower thermostability.
• Transcriptome Analysis of the Duodenum in Wistar Rats Fed a Trypsin Inhibitor Derived from Squid Viscera

  Kohsuke Adachi, Kana Fukumorita, Michihiro Araki, Nobuhiro Zaima, Satoru Chiba, Hideki Kishimura, Hiroki Saeki

  JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 59 (16) 9001 - 9010 0021-8561 2011/08 [Refereed][Not invited]
   

  To investigate the effects of oral administration of a trypsin inhibitor (TI), normal Wistar rats were fed a TI derived from squid (Todarodes pacificus) for 10 weeks and gene expression profiles in the duodenum, pancreas, liver, and muscle were then analyzed using DNA microarrays. Although no significant changes could be observed in growth, food intake, tissue weight, or blood tests among the tissues tested, the duodenum showed the most remarkable changes in the global gene expression profile. Significant up-regulation of mRNAs encoding gastrin, gastrokine, cholecystokinin and somatostatin in the duodenum was validated by qPCR analysis. In gene ontology (GO) analysis of the up-regulated differentially expressed genes (DEGs), GO terms related to keratinization and innate mucosal defense were enriched (p < 0.001) in the category of biological processes in addition to assumable terms such as regulation of secretion and response to nutrients, vesicle-mediated transport, and so forth. In the same analysis, calcium ion binding was listed at the deepest hierarchy in the category of molecular function. These results indicate that the duodenum responds to TI treatment by a wider range of physiological processes than previously assumed such as keratinocyte differentiation and innate mucosal defense, in which calcium plays a crucial role.
• Structural properties of trypsin from cold-adapted fish, arabesque greenling (Pleurogrammus azonus)

  Gaku Kanno, Hideki Kishimura, Seiichi Ando, Sappasith Klomklao, Sitthipong Nalinanon, Soottawat Benjakul, Byung-Soo Chun, Hiroki Saeki

  EUROPEAN FOOD RESEARCH AND TECHNOLOGY 232 (3) 381 - 388 1438-2377 2011/03 [Refereed][Not invited]
   

  A cDNA clone encoding trypsin (AG-T) was isolated from the pyloric ceca of cold-adapted fish, arabesque greenling (Pleurogrammus azonus). The cDNA was composed of 892 bp with an open reading frame of 729 bp at nucleotide positions 25-753. Similar to all the known trypsin, the AG-T seemed to be synthesized as preproenzyme that contains a hydrophobic signal peptide, an activation pentapeptide and a mature trypsin of 222 amino acid residues. The AG-T also completely conserved the major structural features common to trypsin such as the catalytic triad (His57, Asp102, and Ser195), the obligatory Asp189 and twelve Cys residues. On the other hand, the AG-T possessed the deletion of Tyr151 and substitution of Pro152 for Gly in the autolysis loop when aligned with the sequence of tropical-zone fish and bovine trypsins. In addition, Val75 concerned in a combination with calcium ion was exchanged for Ala in the AG-T, and the content of positively charged amino acid residues at the calcium-binding site of the AG-T was three times higher than those of tropical-zone fish trypsins. Moreover, the ratio between charged and hydrophobic amino acid residues in the N-terminal region of the AG-T was also higher than those of temperate-zone fish and tropical-zone fish trypsins. Such structural properties of the AG-T would contribute to its low thermostability.
• Type I collagen from the skin of ornate threadfin bream (Nemipterus hexodon): characteristics and effect of pepsin hydrolysis

  S.Nalinanon, S.Benjakul, H.Kishimura, K.Osako

  Food Chemistry [IF=3.655] [TC=102] 125 (2) 500 - 507 0308-8146 2011/03 [Refereed][Not invited]
   

  Type I collagen from the skin of ornate threadfin bream (Nemipterus hexodon) was purified and characterised. Purified type I collagen contained [alpha 1(I)](2)alpha 2(I) as the dominant component with the co-presence of alpha 1(I)alpha 2(I)alpha 3(I). It was rich in glycine and alanine with high content of imino acids (188 residues/1000 residues). The maximum transition temperature (T-m) and the total denaturation enthalpy (Delta H) of purified type I collagen was 33.35 degrees C and 0.819 J/g, respectively. The isoelectric point (pI) of purified type I collagen was estimated to be 6.40. After hydrolysis of purified type I collagen using pepsin, the band intensity ratios of alpha 1/alpha 2-chains were increased (P < 0.05). The cross-linked components were effectively hydrolysed by pepsin 1 and 2 from skipjack tuna stomach and porcine pepsin at 4 degrees C without the cleavage of beta- and alpha-chains At 50 degrees C, they were more susceptible to porcine pepsin hydrolysis, followed by pepsin 2 and 1, respectively. (C) 2010 Elsevier Ltd All rights reserved.
• Isolation and Characterization of Lecithin from Squid (Todarodes pacificus) Viscera Deoiled by Supercritical Carbon Dioxide Extraction

  Md Salim Uddin, Hideki Kishimura, Byung-Soo Chun

  JOURNAL OF FOOD SCIENCE 76 (2) C350 - C354 0022-1147 2011/03 [Refereed][Not invited]
   

  Marine lecithin was isolated and characterized from squid (Todarodes pacificus) viscera residues deoiled by supercritical carbon dioxide (SC-CO2) extraction. SC-CO2 extraction was carried out to extract the oil from squid viscera at different temperatures (35 to 45 degrees C) and pressures (15 to 25 MPa). The extraction yield was higher at highest temperature and pressure. The major phospholipids of squid viscera lecithin were quantified by high-performance liquid chromatography (HPLC). Phosphatidylcholine (PC; 80.5% +/- 0.7%) and phosphatidylethanolamine (PE; 13.2% +/- 0.2%) were the main phospholipids. Thin layer chromatography (TLC) was performed to purify the individual phospholipids. The fatty acid compositions of lecithin, PC and PE were analyzed by gas chromatography (GC). A significant amount of eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) were present in both phospholipids of PC and PE. Emulsions of lecithin in water were prepared through the use of a homogenizer. The oxidative stability of squid viscera lecithin was high in spite of its high concentration of long-chain polyunsaturated fatty acids. Practical Application Squid viscera are discarded as a waste by fish processing industry. Since lecithin from squid viscera contains higher amounts of polyunsaturated fatty acids, it may have promising effect to use in food, pharmaceutical, and cosmetic industries.
• Functionalities and antioxidant properties of protein hydrolysates from the muscle of ornate threadfin bream treated with pepsin from skipjack tuna (Thomson Leuters, Web of Science, 高被引用文献)

  Sitthipong Nalinanon, Soottawat Benjakul, Hideki Kishimura, Fereidoon Shahidi

  Food Chemistry [IF=3.655] [TC=292] 124 (4) 1354 - 1362 0308-8146 2011/02 [Refereed][Not invited]
   

  Functional properties and antioxidant activities of protein hydrolysates prepared from ornate threadfin bream (Nemipterus hexodon) muscle, using skipjack tuna pepsin, with different degrees of hydrolysis (DH: 10%, 20% and 30%), were evaluated. Emulsifying and foaming properties of hydrolysates were governed by their DH and concentrations used. Hydrolysates with 20% DH had the highest scavenging activities for ABTS and DPPH radicals. However, chelating activity of hydrolysates for ferrous ion increased as DH increased. Size exclusion chromatography of the hydrolysate with 20% DH using Sephadex G-25 revealed that antioxidative peptides with molecular weight of approximately 1.3 kDa exhibited the highest ABTS radical-scavenging activity. In vitro simulated gastrointestinal digestion indicated that ABTS radical-scavenging activity of the antioxidative peptides was not affected by pepsin hydrolysis, whilst further digestion by pancreatin enhanced the activity. Therefore, protein hydrolysate from the muscle of ornate threadfin bream produced by skipjack tuna pepsin can be used as a promising source of functional peptides with antioxidant properties. (C) 2010 Elsevier Ltd. All rights reserved.
• Purified sardine and king crab trypsin display individual differences in PAR-2-, NF-kappa B-, and IL-8 signaling

  Anett K. Larsen, Ole-Morten Seternes, Merethe Larsen, Hideki Kishimura, Galina N. Rudenskaya, Berit Bang

  TOXICOLOGICAL AND ENVIRONMENTAL CHEMISTRY 93 (10) 1991 - 2011 0277-2248 2011 [Refereed][Not invited]
   

  Respiratory symptoms occur in workers processing a great variety of seafood. Studies previously showed that salmon trypsin increases transcriptional activity of NF-kappa B and induces secretion of IL-8 from airway epithelial cells by activating PAR-2. The aim of this study was to explore if purified trypsins from king crab (Paralithodes camtschaticus) and sardine (Sardinops melanostictus) are able to induce similar effects in cell stimulation assays. The knowledge that crustaceans seem to display dissimilar irritant potency compared to fish inspired us to investigate if one could detect differences in intracellular signaling pathways coupled to IL-8 in human airway epithelial cells (A549). Both sardine and king crab trypsin induced secretion of IL-8 from human airway epithelial cells in a concentration-dependent manner and increased transcriptional activity of NF-kappa B. With the use of siRNA data indicate that these effects are both mediated, at least partly, through the activation of PAR-2. Additionally, the king crab and sardine trypsin display individual differences in transformation of the NF-kappa B signal into subsequent IL-8 secretion. The contribution of MEK/ERK, p38, and NF-kappa B to the secretion of IL-8 following stimulation with sardine and king crab trypsins were examined with the use of specific inhibitors. The results demonstrated that MEK/ERK and NF-kappa B are both required for sardine and king crab trypsin-induced secretion of IL-8 but via separate pathways. P38 was also found to contribute to the secretion of IL-8 seemingly by NF-kappa B-dependent processes.
• Application of supercritical carbon dioxide for preparation of fish trypsin [IF:-][CI:0]

  B.-S.Chun, H.Kishimura, S.Nalinanon, S.Klomklao, S.Benjakul

  Journal of Amino Acids 2011 (Article ID 728082) 1 - 7 2011 [Refereed][Not invited]
  
• Isolation and characterisation of collagen extracted from the skin of striped catfish (Pangasius hypophthalmus) (Thomson Leuters, Web of Science, 高被引用文献)

  S.Singh, S.Benjakul, S.Maqsood, H.Kishimura

  Food Chemistry [IF=3.655] [TC=361] 124 (1) 97 - 105 0308-8146 2011/01 [Refereed][Not invited]
   

  Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from the skin of striped catfish (Pangasianodon hypophthalmus) were isolated and characterised. The yields of ASC and PSC were 5.1% and 7.7%, based on the wet weight of skin, respectively, with the accumulated yield of 12.8%. Both ASC and PSC comprising two different alpha-chains (alpha 1 and alpha 2) were characterised as type I and contained imino acid of 206 and 211 imino acid residues/1000 residues, respectively. Peptide maps of ASC and PSC hydrolysed by either lysyl endopeptidase or V8 protease were slightly different and totally differed from those of type 1 calf skin collagen, suggesting some differences in amino acid sequences and collagen structure. Fourier transform infrared (FTIR) spectra of both ASC and PSC were almost similar and pepsin hydrolysis had no marked effect on the triple-helical structure of collagen. Both ASC and PSC had the highest solubility at acidic pH. A loss in solubility was observed at a pH greater than 4 or when NaCl concentration was higher than 2% (w/v). T-max of ASC and PSC were 39.3 and 39.6 degrees C, respectively, and shifted to a lower temperature when rehydrated with 0.05 M acetic acid. Zeta potential studies indicated that ASC and PSC exhibited a net zero charge at pH 4.72 and 5.43, respectively. Thus. ASC and PSC were slightly different in terms of composition and structure, leading to somewhat different properties. (C) 2010 Elsevier Ltd. All rights reserved.
• Collagenolytic serine protease in fresh water prawn (Macrobrachium rosenbergii): Characteristics and its impact on muscle during iced storage

  Chodsana Sriket, Soottawat Benjakul, Wonnop Visessanguan, Hideki Kishimura

  FOOD CHEMISTRY 124 (1) 29 - 35 0308-8146 2011/01 [Refereed][Not invited]
   

  Proteolytic activity of crude protease extract (CPE) from the hepatopancreas of fresh water prawn (Macrobrachium rosenbergii) was studied. Optimal activity of CPE was found at pH 7 and 60 degrees C when casein was used as a substrate. The activity was strongly inhibited by 10 mM N-p-tosyl-L-lysine chloromethylketone (TLCK), suggesting that trypsin-like protease was dominant. CPE also showed the collagenolytic activity toward pepsin soluble collagen extracted from prawn muscle. During extended iced storage of 4 days, proteolytic and trypsin activities were found in the first segment of prawn abdomen. These activities were detected in the second segment after 4 days of storage. Heat soluble collagen content was continuously increased during the storage. Nevertheless, no changes in proteolytic activity and heat soluble collagen content were obtained in the abdomen of prawn with the removal of hepatopancreas. Therefore, the release of trypsin-like collagenase from hepatopancreas was most likely responsible for the softening of prawn meat during iced storage. (C) 2010 Elsevier Ltd. All rights reserved.
• Antioxidative and ACE inhibitory activities of protein hydrolysates from the muscle of brownstripe red snapper prepared using pyloric caeca and commercial proteases

  Sutheera Khantaphant, Soottawat Benjakul, Hideki Kishimura

  PROCESS BIOCHEMISTRY 46 (1) 318 - 327 1359-5113 2011/01 [Refereed][Not invited]
   

  Protein hydrolysates from the muscle of brownstripe red snapper (Lutjanus vitro) prepared using Alcalase or Flavourzyme as the first step with 40% degree of hydrolysis (DH), followed by hydrolysis with pyloric caeca protease (PCP) as the second step for 2 (HAP) and 1 h (HFP), respectively, were prepared and determined for their antioxidative and angiotensin l-converting enzyme (ACE) inhibitory activities. HAP had the higher DPPH and ABTS radical scavenging activity and ferric reducing antioxidant power (FRAP), while HFP showed the higher ferrous chelating activity and ACE inhibitory activity (p<0.05). Both HAP and HFP were able to retard lipid oxidations in lecithin-liposome and beta-carotene-linoleic acid oxidation model systems in dose-dependent manner. HAP and HFP contained 87.36 and 86.55% protein (wet basis). respectively with glutamic acid/glutamine as the major amino acids, followed by aspartic acid/asparagine, lysine, alanine and leucine, respectively. HFP showed a slightly greater efficiency in prevention of lipid oxidation in all systems tested. Antioxidative activities, except DPPH radical scavenging activity, of both HAP and HFP after being subjected to gastrointestinal tract model system (GIMs) increased, suggesting the enhancement of antioxidative activities of both hydrolysates after ingestion. (C), 2010 Elsevier Ltd. All rights reserved.
• Simple preparation of Pacific cod trypsin for enzymatic peptide synthesis [IF:-][CI:0]

  T.Fuchise, M.Kojima, H.Sekizaki, H.Kishimura, S.Klomklao, S.Nalinanon, S.Benjakul, B.-S.Chun

  Journal of Amino Acids 2011 (Article ID 912382) 1 - 8 2011 [Refereed][Not invited]
  
• CATIONIC TRYPSIN: A PREDOMINANT PROTEINASE IN PACIFIC SAURY (COLOLABIS SAIRA) PYLORIC CECA

  S. Klomklao, H. Kishimura, S. Benjakul, B. K. Simpson, W. Visessanguan

  JOURNAL OF FOOD BIOCHEMISTRY 34 (5) 1105 - 1123 0145-8884 2010/10 [Refereed][Not invited]
   

  Cationic trypsin was purified from Pacific saury (Cololabis saira) pyloric ceca by the successive steps of ammonium sulfate precipitation, anion exchange chromatography and gel filtration chromatography. The purification and yield were 90-fold and 8.9%, respectively. The molecular weight was determined to be 24 kDa using Sephacryl S-200 and SDS-PAGE. Cationic trypsin was stable at pH 7-11 for 30 min at 30C, and its maximal activity against L-arginine methyl ester hydrochloride (TAME) was at pH 8.5. Thermostability for cationic trypsin was up to 50C for 15 min and its temperature optimum was 60C. Cationic trypsin was stabilized by calcium ion. Activity decreased as NaCl concentration (0-30%) increased. Inhibitor susceptibility analysis revealed that the enzyme was inhibited effectively by soybean trypsin inhibitor and N-p-tosyl-L-lysine chloromethyl ketone. The K-m and K-cat of the enzyme were 0.17 mM and 200 s-1 , respectively. The N-terminal amino acid sequence of cationic trypsin was partially determined as IVGGYECQPH- and was very homologous to other trypsins. PRACTICAL APPLICATIONS Trypsin is a major member of the serine proteases, which constitute a large family of biologically important enzymes. Trypsins from various sources catalyze the hydrolysis of peptide bonds on the carboxyl sides of arginine and lysine. Hence, it is expected that like other trypsins, Pacific saury trypsin would also be used for processing aids in industry applications. Most trypsins are used for a variety of products in the food industry including baked foods, beer, wine, cereal, meat and fish products, and for production of protein hydrolysates and flavor extract. Trypsins are also used in mammalian cell culture to disaggregate adherent cells for research and the production of recombinant proteins, in diabetes diagnosis and therapy, in detergents and bating of leather.
• Purification and characteristics of trypsin from masu salmon (Oncorhynchus masou) cultured in fresh-water

  Gaku Kanno, Takahito Yamaguchi, Hideki Kishimura, Etsurou Yamaha, Hiroki Saeki

  FISH PHYSIOLOGY AND BIOCHEMISTRY 36 (3) 637 - 645 0920-1742 2010/09 [Refereed][Not invited]
   

  Trypsin from the pyloric ceca of masu salmon (Oncorhynchus masou) cultured in fresh water was purified by a series of chromatographies including Sephacryl S-200, Sephadex G-50 and diethylaminoethyl cellulose to obtain a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and native PAGE. The molecular mass of the purified trypsin was estimated to be approximately 24,000 Da by SDS-PAGE. The enzyme activity was strongly inhibited by phenylmethylsulfonyl fluoride, soybean trypsin inhibitor, and N (alpha) -p-tosyl-l-lysine chloromethyl ketone. Masu salmon trypsin was stabilized by calcium ion. The optimum pH of the masu salmon trypsin was around pH 8.5, and the trypsin was unstable below pH 5.0. The optimum temperature of the masu salmon trypsin was around 60A degrees C, and the trypsin was stable below 50A degrees C, like temperate-zone and tropical-zone fish trypsins. The N-terminal 20 amino acid sequence of the masu salmon trypsin was IVGGYECKAYSQPHQVSLNS, and its charged amino acid content was lower than those of trypsins from frigid-zone fish and similar to those of trypsins from temperate-zone and tropical-zone fish. In the phylogenetic tree, the masu salmon trypsin was classified into the group of the temperate-zone fish trypsin.
• Production of valued materials from squid viscera by subcritical water hydrolysis

  Md. Salim Uddin, Hyang-Min Ahn, Hideki Kishimura, Byung-Soo Chun

  JOURNAL OF ENVIRONMENTAL BIOLOGY 31 (5) 675 - 679 0254-8704 2010/09 [Refereed][Not invited]
   

  Subcritical water hydrolysis was carded out to produce valued materials from squid viscera, the waste product of fish processing industries. The reaction temperatures for hydrolysis of raw and deoiled squid viscera were maintained from 180 to 280 degrees C for 5 min. The ratio of material to water for hydrolysis was 1:50. Most of the proteins from deoiled squid viscera were recovered at high temperature. The protein yield in raw squid viscera hydrolyzate decreased with the rise of temperature. The reducing sugar yield was higher at high temperature in subcritical water hydrolysis of both raw and deoiled squid viscera. The highest yield of amino acids in raw and deoiled squid viscera hydrolyzates were 233.25+/-3.25 and 533.78+/-4.13 mg g(-1) at 180 and 280 degrees C, respectively Most amino acids attained highest yield at the reaction temperature range of 180-220 degrees C and 260-280 degrees C for raw and deoiled samples, respectively The recovery of amino acids from deoiled squid viscera was about 1.5 times higher than that of raw squid viscera.
• ACID- AND HEAT-STABLE TRYPSIN INHIBITORY PEPTIDE FROM THE VISCERA OF JAPANESE COMMON SQUID (TODARODES PACIFICUS)

  Hideki Kishimura, Yujiro Nagai, Kana Fukumorita, Kohsuke Adachi, Satoru Chiba, Sigeru Nakajima, Hiroki Saeki, Sappasith Klomklao, Sitthippong Nalinanon, Soottawat Benjakul, Byung-Soo Chun

  JOURNAL OF FOOD BIOCHEMISTRY 34 (4) 748 - 763 0145-8884 2010/08 [Refereed][Not invited]
   

  Trypsin inhibitor was purified from the viscera except for the hepatopancreas of Japanese common squid (Todarodes pacificus) by gel filtration and anion-exchange chromatography. Final inhibitor preparation was homogeneous as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and its molecular weight was estimated to be approximately 6,000 Da. The N-terminal amino acid sequence of the squid trypsin inhibitor was determined as ANEATXVYKGKTYKKGEGF. The purified inhibitor was heat stable up to 150 min at 80C at pH 8.0. The inhibitory activity was also retained at pH 2.0 and 37C for 180 min. The squid trypsin inhibitor was active against walleye pollock trypsin as well as porcine pancreatic trypsin. The squid trypsin inhibitor showed hypoglycemic effect on blood glucose levels of GK rats, a model of type 2 diabetes.
• EFFECT OF SALTS AND POLYETHYLENE GLYCOLS ON THE PARTITIONING AND RECOVERY OF TRYPSIN FROM HYBRID CATFISH VISCERA IN AQUEOUS TWO-PHASE SYSTEMS

  Sappasith Klomklao, Soottawat Benjakul, Hideki Kishimura, Kazufumi Osako, Munehiko Tanaka

  JOURNAL OF FOOD BIOCHEMISTRY 34 (4) 730 - 747 0145-8884 2010/08 [Refereed][Not invited]
   

  The partitioning behavior of trypsin from hybrid catfish viscera in aqueous two-phase systems (ATPS) was studied. Factors such as polyethylene glycol (PEG) molecular mass and concentration, as well as types and concentration of salts, affected protein separation. Trypsin partitioned mainly in the top PEG-rich phase. ATPS formed by PEG of molecular weight 4,000 (20%, w/w) and NaH2PO4 (20%, w/w) showed the best capability for trypsin purification from hybrid catfish viscera. Under such conditions, the highest specific activity (30.05 units/mg protein) and purification (27.3-fold), were obtained. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis revealed that the enzyme after ATPS separation was near homogeneity and based on the activity staining, the band intensity of enzyme in ATPS fraction increased, indicating the greater specific activity of the viscera extract. The partitioned enzyme displayed optimal activity at pH 9.0 and 50C, respectively. The enzyme was stable up to 40C and within the pH range of 8-12. The enzyme exhibited a progressive decrease in activity with increasing NaCl concentration.
• PROTEINASES IN HYBRID CATFISH VISCERA: CHARACTERIZATION AND EFFECT OF EXTRACTION MEDIA

  Sappasith Klomklao, Soottawat Benjakul, Hideki Kishimura

  JOURNAL OF FOOD BIOCHEMISTRY 34 (4) 711 - 729 0145-8884 2010/08 [Refereed][Not invited]
   

  Proteolytic activity from viscera extract of hybrid catfish (Clarias macrocephalus Clarias gariepinus) was investigated. Optimal pH and temperature for casein hydrolysis were 9.0 and 50C, respectively. The enzyme was stable to heat treatment up to 40C and over a pH range of 7-11 for 30-120 min. The proteolytic activity was effectively inhibited by soybean trypsin inhibitor, benzamidine, phenylmethylsulfonyl fluoride and N-p-tosyl-L-lysine chloromethyl ketone. Activities of the viscera extract continuously decreased as NaCl concentration increased, while activities increased as CaCl2 concentration increased. Based on the proteinase activity of zones separated by electrophoresis, the molecular mass of the major proteinases in hybrid catfish viscera was 23 and 20 kDa. The effect of extraction media on recovery of proteinases was also studied. Extraction of the viscera powder with 50 mM Tris-HCl, pH 7.0 containing 0.5 M NaCl and 0.2% (v/v) Brij 35 rendered a higher recovery of proteinase activity than other extractants tested (P < 0.05). The results suggested that major proteinases in hybrid catfish viscera were heat-activated alkaline proteinases, most likely trypsin-like serine proteinases.
• Collagens from the skin of arabesque greenling (Pleurogrammus azonus) solubilized with the aid of acetic acid and pepsin from albacore tuna (Thunnus alalunga) stomach

  Sitthipong Nalinanon, Soottawat Benjakul, Hideki Kishimura

  JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE 90 (9) 1492 - 1500 0022-5142 2010/07 [Refereed][Not invited]
   

  BACKGROUND: Due to the low extraction efficiency of collagen from fish skin by the typical acid solubilization process, pepsin has been widely used to aid further extraction of collagen from the residue. The aim of this study was to characterize collagen from the skin of arabesque greenling extracted with the aid of albacore tuna pepsin, in comparison with collagen obtained from the acid solubilization process. RESULTS: Acid-solubilized collagen (ASC) from the skin of arabesque greenling was extracted with acetic acid. Pepsin-solubilized collagen (PSC) was further extracted from the skin residue with the aid of pepsin from albacore tuna. The yields of ASC and PSC were 303 and 140 g kg(-1) (dry weight), respectively. Both collagens contained alpha- and beta-chains as their major components and were characterized as type I collagen. Both collagens contained glycine as a major amino acid and had imino acid content of 157-159 residues per 1000 residues. The degradation induced by lysyl endopeptidase and V8-protease was more pronounced in PSC compared with ASC. Maximal transition temperatures of both collagens were in the range of 15.4-15.7 degrees C. Fourier transform infrared spectra revealed some differences in molecular order between ASC and PSC. Nevertheless, the triple-helical structure of PSC was still predominant. Based on zeta-potential, pl of ASC and PSC was estimated to be 6.31 and 6.38, respectively. CONCLUSION: Isolation of collagens from the skin of arabesque greenling could be achieved by acid or albacore tuna pepsin solubilization. However, there was a slight difference in properties between ASC and PSC. (C) 2010 Society of Chemical Industry
• Biochemical properties of pepsinogen and pepsin from the stomach of albacore tuna (Thunnus alalunga)

  Sitthipong Nalinanon, Soottawat Benjakul, Hideki Kishimura

  FOOD CHEMISTRY 121 (1) 49 - 55 0308-8146 2010/07 [Refereed][Not invited]
   

  Pepsinogen (PG) from the stomach of albacore tuna (Thunnus alalunga) was purified to homogeneity by using a series of chromatographies involving Sephacryl S-200HR, Sephadex G-50 and DEAE-cellulose with a 658-fold increase in purity. Based on the native-PAGE and zymography, PG showed a single band with pepsin activity. Molecular weights (MW) of PG and active pepsin were estimated to be 39.9 and 32.7 kDa as determined by SDS-PAGE, respectively. PG was converted to the corresponding pepsin through an intermediate form (MW approximate to 36.8 kDa) and the complete activation was observed after 30-60 min. The N-terminal amino acid sequence of the first 15 amino acids of activation segment of pepsinogen was FHKLPLIKGKTAREE. The optimal pH and temperature for pepsin activity were 2.0 and 50 degrees C, respectively. The activity was stable in the pH range of 2-5. Residual activity more than 85% was found after heating at temperatures up to 50 degrees C for 30 min. Pepsin activity was strongly inhibited by pepstatin A, whilst E-64, ethylenediaminetetraacetic acid (EDTA) and soybean trypsin inhibitor exhibited the negligible effect, SDS and cysteine also showed inhibitory effects, whilst ATP, molybdate, NaCl and CaCl2 had no impact on pepsin activity. (C) 2009 Elsevier Ltd. All rights reserved.
• Purification and biochemical properties of pepsins from the stomach of skipjack tuna (Katsuwonus pelamis)

  Sitthipong Nalinanon, Soottawat Benjakul, Hideki Kishimura

  EUROPEAN FOOD RESEARCH AND TECHNOLOGY 231 (2) 259 - 269 1438-2377 2010/06 [Refereed][Not invited]
   

  Pepsins 1 and 2 from the stomach of skipjack tuna (Katsuwonus pelamis) were purified to homogeneity by using a series of chromatographic purification involving DEAE-cellulose, Sephadex G-50 and Sephadex G-75 with increase in purity of 246-fold and 213-fold, respectively. Molecular weights of pepsins 1 and 2 were estimated by SDS-PAGE to be 33.9 and 33.7 kDa, respectively. The N-terminal amino acid sequences of the first 20 amino acids of both isoenzymes were YQDGTEPMTNDADLSYYGVI. The optimal pH and temperature for pepsin 1 were 2.5 and 50 A degrees C, respectively, while pepsin 2 showed optimal activity at pH 2.0 and 45 A degrees C. The activity of two pepsins was stable in the pH range of 2-5 and at temperatures up to 50 A degrees C. The activity of purified pepsins was strongly inhibited by pepstatin A in a dose-dependent manner. SDS and cysteine showed inhibitory effects toward both pepsins. Activity of pepsin 2 was slightly activated by NaCl, but NaCl had no effect on pepsin 1. Pepsins 1 and 2 had high affinity and hydrolytic activity toward hemoglobin with K (m) of 54 and 71 mu M, respectively. k (cat) of pepsins 1 and 2 were 38.1 and 44.3 s(-1), respectively. Both pepsins effectively hydrolyzed bovine serum albumin, egg white, natural actomyosin from brownstripe red snapper muscle and acid-solubilized collagen from arabesque greenling skin. Nevertheless, the hydrolytic activity was slightly less than that of pepsin from porcine stomach.
• Application of supercritical carbon dioxide for preparation of starfish phospholipase A(2)

  Byung-Soo Chun, Hideki Kishimura, Hiroto Kanzawa, Sappasith Klomklao, Sitthipong Nalinanon, Soottawat Benjakul, Seiichi Ando

  PROCESS BIOCHEMISTRY 45 (5) 689 - 693 1359-5113 2010/05 [Refereed][Not invited]
   

  Pyloric ceca of starfish (Asterina pectinifera) were treated by supercritical carbon dioxide (SCO2) to remove the lipids. Then, phospholipase A(2) (SC-PLA(2)) was extracted from the defatted powder and purified by a series of chromatographies including Sephacryl S-200, DEAE-cellulose, and Sephadex G-50. The purified SC-PLA(2) was nearly homogeneous in SDS-PAGE and native-PAGE. The molecular weight of the SC-PLA(2) was estimated as approximately 20,000. N-terminal amino acid sequence of the SC-PLA(2) was SVYQF. Temperature and pH optimums of the SC-PLA(2) were at around 50 degrees C and pH 9.0, respectively, and the enzyme activity was enhanced by sodium deoxycholate and 1 mM or higher concentration of Ca2+. The SC-PLA(2) was stimulated most by adding Ca2+ followed by Mg2+ and Co2+, while it was strongly inhibited by adding Zn2+ and EDTA. The SC-PLA(2) hydrolyzed phosphatidylcholine more effectively than phosphatidylethanolamine. These characteristics of the SC-PLA(2) were the same as those of the starfish PLA(2) (CM-PLA(2)) purified from the pyloric ceca defatted by chloroform-methanol (2:1, v/v) solution. Therefore, we concluded the SCO2 defatting process is useful as a substitute for organic solvent defatting process. (C) 2010 Elsevier Ltd. All rights reserved.
• Isolation and Characterisation of collagen from the skin of brownbanded bamboo shark (Chiloscyllium punctatum)

  Phanat Kittiphattanabawon, Soottawat Benjakul, Wonnop Visessanguan, Hideki Kishimura, Fereidoon Shahidi

  FOOD CHEMISTRY 119 (4) 1519 - 1526 0308-8146 2010/04 [Refereed][Not invited]
   

  Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from the skin of brownbanded bamboo shark (Chiloscyllium punctatum) were isolated and characterised. The yield of ASC and PSC were 9.38% and 8.86% (wet weight basis), respectively. Based on protein patterns and TOYOPEARL(R) CM-650M column chromatography, both collagens contained alpha- and beta-chains as their major components. These were characterised as type I collagen with the cross-link of alpha 2-chain. As digested by V8-protease and lysyl endopeptidase, peptide maps of both ASC and PSC were similar, but differed from that of type I collagen from calf skin. Fourier transform infrared (FTIR) spectra of both collagens were similar and pepsin hydrolysis had no effect on triple-helical structure of collagen. Transition temperature (T(max)) of ASC and PSC were 34.45 and 34.52 degrees C, respectively, as determined by differential scanning colorimetry (DSC). From zeta potential study, the isoelectric points of ASC and PSC were estimated to be 6.21 and 6.56, respectively. Therefore, the skin of brownbanded bamboo shark could serve as an alternative source of collagen for different applications. (C) 2009 Elsevier Ltd. All rights reserved.
• Atlantic Cod Trypsin-Catalyzed Peptide Synthesis with Inverse Substrates as Acyl Donor Components

  Tomoyoshi Fuchise, Hideki Kishimura, Zhi-hong Yang, Mareshige Kojoma, Eiko Toyota, Haruo Sekizaki

  CHEMICAL & PHARMACEUTICAL BULLETIN 58 (4) 484 - 487 0009-2363 2010/04 [Refereed][Not invited]
   

  Atlantic cod trypsin-catalyzed peptide synthesis has been studied by using p-amidino- and p-guanidinophenyl esters of N-(tert-butyloxycarbonyl)amino acid as acyl donor components. The reaction temperature was optimized at 0 degrees C. The method was shown to be successful as effectively for synthesizing the peptide and useful for preparing dipeptide between D-amino acid with D-amino acid and beta-amino acid with beta-amino acid, respectively. The enzymatic hydrolysis of the resulting products was negligible.
• Transfer rate measurement of lysozyme by liquid-liquid extraction using reverse micelles with dense CO2

  Sun-Mi Jung, Un-Mi Shin, Md. Salim Uddin, Sun-Young Park, Hideki Kishimura, Gordon Wilkinson, Byung-Soo Chun

  KOREAN JOURNAL OF CHEMICAL ENGINEERING 27 (2) 596 - 601 0256-1115 2010/03 [Refereed][Not invited]
   

  Lysozyme was extracted from aqueous solution into i-octane using reverse micelles in the presence of pressurized CO2. A squat vessel with two independent stirrers was used to measure the mass transfer of the lysozyme across a planar interface. Mass transfer coefficient, k(L) of the lysozyme from the aqueous to the organic phase was measured at selected ionic strengths, pH, sodium bis(2-ethylhexyl) sulfosuccinate (AOT) surfactant concentrations, temperatures and pressurized CO2. The mass transfer rate of lysozyme was higher in high temperature (318 K) and pressure (20 MPa). pH of 9 in aqueous phase showed highest mass transfer rate of lysozyme. The application of pressurized CO2 markedly increased the mass transfer rate of lysozyme comparing to conventional non-pressurized system.
• COMPARATIVE STUDY ON THERMAL STABILITY OF TRYPSIN FROM THE PYLORIC CECA OF THREADFIN HAKELING (LAEMONEMA LONGIPES)

  Hideki Kishimura, Sappasith Klomklao, Sitthipong Nalinanon, Soottawat Benjakul, Byung-Soo Chun, Kohsuke Adachi

  JOURNAL OF FOOD BIOCHEMISTRY 34 (1) 50 - 65 0145-8884 2010/02 [Refereed][Not invited]
   

  Trypsin was purified from the pyloric ceca of threadfin hakeling (Laemonema longipes). Final enzyme preparation was nearly homogeneous in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Activity of the enzyme was inhibited by serine protease inhibitors, such as soybean trypsin inhibitor, N(alpha)-tosyl-L-lysine chloromethyl ketone and squid trypsin inhibitor. The molecular weight of the trypsin was estimated to be 24 kDa by SDS-PAGE. The N-terminal amino acid sequence of the trypsin, IVGGKECAKHSQRHQVSLNS, was found, and the sequential identity between the threadfin hakeling trypsin with Frigid Zone fish trypsin was relatively higher (ca. 80%) than Temperate Zone fish trypsin (ca. 74%), Tropical Zone fish trypsin (ca. 75%) and mammalian trypsin (ca. 58%). The trypsin had maximal activities at around pH 8.0 and 50C for hydrolysis of N(alpha)-p-tosyl-L-arginine methyl ester hydrochloride. The trypsin was unstable at below pH 5.0 and at above 30C. It was stabilized by calcium ion. Similar to other trypsin from the Frigid Zone fish, threadfin hakeling trypsin was thermo unstable than the trypsin from the Temperate Zone fish and Tropical Zone fish. The relationship between habitat temperature of fish and thermo stability of the fish trypsin indicated strong positive correlation.
• Extraction and characterisation of pepsin-solubilised collagens from the skin of bigeye snapper (Priacanthus tayenus and Priacanthus macracanthus)

  Soottawat Benjakul, Yaowapa Thiansilakul, Wonnop Visessanguan, Sittiruk Roytrakul, Hideki Kishimura, Thummanoon Prodpran, Jirut Meesane

  JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE 90 (1) 132 - 138 0022-5142 2010/01 [Refereed][Not invited]
   

  BACKGROUND: Fish collagen has been paid increasing attention as an alternative to the mammalian counterpart owing to the abundance of fish skin as a processing by-product. Generally, the low yield of collagen extracted using the typical acid solubilisation process has led to the use of mammalian pepsin as an aid for increasing the yield. Alternatively, fish pepsin, especially from tuna stomach, can be used for the extraction of pepsin-solubilisedcollagen (PSC). Therefore the objective of this study was to extract and characterise PSC from the skin of bigeye snapper, a fish widely used for surimi production in Thailand. RESULTS: PSCs from the skin of two species of bigeye snapper, Priacanthus tayenus and Priacanthus macracanthus, were extracted with the aid of tongol tuna (Thunnus tonggol) pepsin and porcine pepsin. PSCs from the skin of both species extracted using porcine pepsin had a higher content of beta-chain but a lower content of alpha-chains compared with those extracted using tuna pepsin. All PSCs contained glycine as the major amino acid and had an imino acid (proline and hydroxyproline) content of 189-193 residues per 1000 residues. Transition temperatures of PSCs were in the range 30.6-31.3 degrees C. Fourier transform infrared spectra revealed some differences in molecular order between PSCs extracted using porcine pepsin and tuna pepsin. Nevertheless, the triple-helical structure of PSCs was not affected by pepsin digestion. Zeta potential analysis indicated that PSCs from P. tayens and P. macracanthus possessed zero net charge at pH 7.15-7.46 and 5.97-6.44 respectively. CONCLUSION: Tongol tuna pepsin could be used as a replacement for mammalian pepsin in PSC extraction. However, a slight difference in PSC properties was found. (c) 2009 Society of Chemical Industry
• A heat-stable trypsin inhibitor in adzuki bean (Vigna angularis): effect of extraction media, purification and biochemical characteristics

  Sappasith Klomklao, Soottawat Benjakul, Hideki Kishimura, Kazufumi Osako, Munehiko Tanaka

  INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY 45 (1) 163 - 169 0950-5423 2010/01 [Refereed][Not invited]
   

  P>Trypsin inhibitor from adzuki bean (Vigna angularis) seed was isolated and characterised. Extraction of seed with NaCl at the concentration of 0.15 m showed a higher recovery of trypsin inhibitor than other solvents tested (P < 0.05). Optimal extraction time for the recovery trypsin inhibitor from adzuki bean seed was 30 min (P < 0.05). Purification of inhibitor was achieved by heat-treatment at 90 degrees C for 10 min, followed by ammonium sulphate precipitation with 30-65% saturation and size exclusion chromatography on Sephacryl S-200, presenting a yield and purification of 53.9% and 10.91-fold, respectively. The apparent molecular weight of trypsin inhibitor was estimated to be 14 kDa based on SDS-PAGE and inhibitor activity of zones separated by electrophoresis. The purified inhibitor was stable over a broad pH range and retained high inhibitory activity toward trypsin after incubation at 90 degrees C for 60 min. NaCl, at 0-3% concentration, did not affect the inhibitory activity of purified trypsin inhibitor, however, the activity was lost when sample was treated with beta-mercaptoethanol prior to electrophoresis.
• Purification and characteristics of trypsins from cold-zone fish, Pacific cod (Gadus macrocephalus) and saffron cod (Eleginus gracilis)

  Tomoyoshi Fuchise, Hideki Kishimura, Haruo Sekizaki, Yoshiyuki Nonami, Gaku Kanno, Sappasith Klomklao, Soottawat Benjakul, Byung-Soo Chun

  Food Chemistry 116 (3) 611 - 616 0308-8146 2009/10 [Refereed][Not invited]
  
• Trypsin from the Pyloric Ceca of Pectoral Rattail (Coryphaenoides pectoralis): Purification and Characterization

  Sappasith Klomklao, Hideki Kishimura, Soottawat Benjakul

  Journal of Agricultural and Food Chemistry 57 (15) 7097 - 7103 0021-8561 2009/08/12 [Refereed][Not invited]
  
• Autolysis and biochemical properties of endogenous proteinases in Japanese sandfish (Arctoscopus japonicus)

  Sappasith Klomklao, Hideki Kishimura, Soottawat Benjakul, Benjamin K. Simpson

  International Journal of Food Science & Technology 44 (7) 1344 - 1350 0950-5423 2009/07 [Refereed][Not invited]
  
• Biochemical properties of two isoforms of trypsin purified from the Intestine of skipjack tuna (Katsuwonus pelamis)

  Sappasith Klomklao, Hideki Kishimura, Yoshiyuki Nonami, Soottawat Benjakul

  Food Chemistry 115 (1) 155 - 162 0308-8146 2009/07 [Refereed][Not invited]
  
• Comparative study of digestive enzymes of squid (Todarodes pacificus) viscera after supercritical carbon dioxide and organic solvent extraction

  Md. Salim Uddin, Hyang-Min Ahn, Hideki Kishimura, Byung-Soo Chun

  Biotechnology and Bioprocess Engineering 14 (3) 338 - 344 1226-8372 2009/06 [Refereed][Not invited]
  
• Homologue of mammalian apolipoprotein A-II in non-mammalian vertebrates

  M. Choudhury, S. Yamada, M. Komatsu, H. Kishimura, S. Ando

  Acta Biochimica et Biophysica Sinica 41 (5) 370 - 378 1672-9145 2009/05/01
• Partitioning of protease from stomach of albacore tuna (Thunnus alalunga) by aqueous two-phase systems

  Sitthipong Nalinanon, Soottawat Benjakul, Wonnop Visessanguan, Hideki Kishimura

  Process Biochemistry 44 (4) 471 - 476 1359-5113 2009/04
• EXTRACTION OF CAROTENOPROTEIN FROM BLACK TIGER SHRIMP SHELLS WITH THE AID OF BLUEFISH TRYPSIN

  S. KLOMKLAO, S. BENJAKUL, W. VISESSANGUAN, H. KISHIMURA, B.K. SIMPSON

  Journal of Food Biochemistry 33 (2) 201 - 217 0145-8884 2009/04
• Effects of manufacturing factors on the viscosity of a polysaccharide solution extracted from Gagome Kjellmaniella crassifolia

  Shigeru Katayama, Toshihiro Nishio, Zensuke Iseya, Hideki Kishimura, Hiroki Saeki

  Fisheries Science 75 (2) 491 - 497 0919-9268 2009/04
• Major Allergen and Its IgE Cross-Reactivity among Salmonid Fish Roe Allergy

  Yutaka Shimizu, Atsushi Nakamura, Hideki Kishimura, Akihiko Hara, Kazuhiko Watanabe, Hiroki Saeki

  Journal of Agricultural and Food Chemistry 57 (6) 2314 - 2319 0021-8561 2009/03/25
• 食資源としての水産物利用と安全活用

  川合祐史, 安 東賢, 今野久仁彦, 崔 暎準, 岸村栄毅

  Proceedings of the 8th Japan-Korea Joint Seminar on Fisheries Sciences 65 - 74 2009 [Not refereed][Not invited]
  
• Improvement of Gelling Properties of Lizardfish Mince as Influenced by Microbial Transglutaminase and Fish Freshness

  S. Benjakul, S. Phatcharat, A. Tammatinna, W. Visessanguan, H. Kishimura

  Journal of Food Science 73 (6) S239 - S246 0022-1147 2008/08 [Refereed][Not invited]
  
• Tuna Pepsin: Characteristics and Its Use for Collagen Extraction from the Skin of Threadfin Bream (Nemipterus spp.)

  S. Nalinanon, S. Benjakul, W. Visessanguan, H. Kishimura

  Journal of Food Science 73 (5) C413 - C419 0022-1147 2008/06
• Improvement of gelatin extraction from bigeye snapper skin using pepsin-aided process in combination with protease inhibitor

  Sitthipong Nalinanon, Soottawat Benjakul, Wonnop Visessanguan, Hideki Kishimura

  Food Hydrocolloids 22 (4) 615 - 622 0268-005X 2008/06 [Refereed][Not invited]
  
• Endogenous proteinases in true sardine (Sardinops melanostictus)

  Sappasith Klomklao, Hideki Kishimura, Soottawat Benjakul

  Food Chemistry 107 (1) 213 - 220 0308-8146 2008/03 [Refereed][Not invited]
  
• COMPOSITION, ANTIOXIDATIVE AND OXIDATIVE STABILITY OF MUNGOONG, A SHRIMP EXTRACT PASTE, FROM THE CEPHALOTHORAX OF WHITE SHRIMP

  WANWISA BINSAN, SOOTTAWAT BENJAKUL, WONNOP VISESSANGUAN, SITTIRUK ROYTRAKUL, NANDHSHA FAITHONG, MUNEHIKO TANAKA, HIDEKI KISHIMURA

  Journal of Food Lipids 15 (1) 97 - 118 1065-7258 2008/02 [Refereed][Not invited]
  
• Antioxidative activity of Mungoong, an extract paste, from the cephalothorax of white shrimp (Litopenaeus vannamei)

  Wanwisa Binsan, Soottawat Benjakul, Wonnop Visessanguan, Sittiruk Roytrakul, Munehiko Tanaka, Hideki Kishimura

  Food Chemistry 106 (1) 185 - 193 0308-8146 2008/01 [Refereed][Not invited]
  
• Characteristics of trypsin from the pyloric ceca of walleye pollock (Theragra chalcogramma)

  Hideki Kishimura, Sappasith Klomklao, Soottawat Benjakul, Byung-Soo Chun

  Food Chemistry 106 (1) 194 - 199 0308-8146 2008/01 [Refereed][Not invited]
  
• Fibrous texturization and amino acid/fatty acid changes with the extrusion cooking of fish meat containing skin and bone

  KITAGAWA MASAHIKO, IIDA TOSHIYUKI, NOBUTA SHIGEHARU, KISHIMURA HIDEKI, SAEKI HIROKI

  NIPPON SUISAN GAKKAISHI Japanese Society of Fisheries Science 74 (1) 55 - 60 0021-5392 2008 [Refereed][Not invited]
  
• Trypsin from the pyloric caeca of bluefish (Pomatomus saltatrix)

  Sappasith Klomklao, Soottawat Benjakul, Wonnop Visessanguan, Hideki Kishimura, Benjamin K. Simpson

  Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 148 (4) 382 - 389 1096-4959 2007/12 [Refereed][Not invited]
  
• Purification and characterization of two pepsins from the stomach of pectoral rattail (Coryphaenoides pectoralis)

  Sappasith Klomklao, Hideki Kishimura, Mamoru Yabe, Soottawat Benjakul

  Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 147 (4) 682 - 689 1096-4959 2007/08 [Refereed][Not invited]
  
• 29 kDa Trypsin from the Pyloric Ceca of Atlantic Bonito (Sarda sarda):  Recovery and Characterization

  Sappasith Klomklao, Soottawat Benjakul, Wonnop Visessanguan, Hideki Kishimura, Benjamin K. Simpson

  Journal of Agricultural and Food Chemistry 55 (11) 4548 - 4553 0021-8561 2007/05/01 [Refereed][Not invited]
  
• The influence of storage conditions of tuna viscera before fermentation on the chemical, physical and microbiological changes in fish sauce during fermentation

  Sirima Dissaraphong, Soottawat Benjakul, Wonnop Visessanguan, Hideki Kishimura

  Bioresource Technology 97 (16) 2032 - 2040 0960-8524 2006/11 [Refereed][Not invited]
  
• Effects of the addition of spleen of skipjack tuna (Katsuwonus pelamis) on the liquefaction and characteristics of fish sauce made from sardine (Sardinella gibbosa)

  Sappasith Klomklao, Soottawat Benjakul, Wonnop Visessanguan, Hideki Kishimura, Benjamin K. Simpson

  Food Chemistry 98 (3) 440 - 452 0308-8146 2006/01 [Refereed][Not invited]
  
• Proteolytic degradation of sardine (Sardinella gibbosa) proteins by trypsin from skipjack tuna (Katsuwonus pelamis) spleen

  S KLOMKLAO, S BENJAKUL, W VISESSANGUAN, H KISHIMURA, B SIMPSON

  Food Chemistry 98 (1) 14 - 22 0308-8146 2006 [Refereed][Not invited]
  
• Apolipoprotein complexity in Japanese eel Anguilla japonica : truncated apolopoprotein A-I and apolipoprotein A-like protein in plasma lipoproteins

  S.Ando, A.Tachibana, S.Yamada, H.Kishimura

  Bioscience Biotechnology and Biochemistry 69 2258 - 2262 2005 [Refereed][Not invited]
  
• Characteristics of two trypsin isozymes from the viscera of Japanese anchovy (Engraulis japonica)

  H.Kishimura, K.Hayashi, Y.Miyashita, Y.Nonami

  Journal of Food Biochemistry 29 459 - 469 2005 [Refereed][Not invited]
  
• Partitioning and recovery of proteinase from tuna spleen by aqueous two-phase systems

  S.Klomklao, S.Benjakul, W.Visessanguan, B.K.Simpson, H.Kishimura

  Process Biochemistry 40 3061 - 3067 2005 [Refereed][Not invited]
  
• Amount of squalene and fatty acid composition of triacylglycerols and phospholipids in flesh and liver lipids of some deep-sea teleost fish, morid cods and whiptails

  K.Hayashi, H.Kishimura

  Journal of Oleo Science 52 339 - 345 2003 [Refereed][Not invited]
  
• Amount and composition of wax esters in various tissue lipids of folked hake Laemonema longipes

  K.Hayashi, K.Hasegawa, H.Kishimura

  Journal of Oleo Science 51 439 - 445 2002 [Refereed][Not invited]
  
• Amount and composition of diacyl glyceryl ethers in various tissue lipids of deep-sea squid Berryteuthis magister

  K.Hayashi, H.Kishimura

  Journal of Oleo Science 51 523 - 529 2002 [Refereed][Not invited]
  
• Structure and function of starfish phospholipase A2

  H.Kishimura, T.Ojima, K.Hayashi, K.Nishita

  Fisheries Science, 68 Supprement II 1263 - 1264 2002 [Not refereed][Invited]
  
• Bacterial expression and characterization of the starfish phospholipase A2

  H.Kishimura, T.Ojima, K.Hayashi, K.Nishita

  Comparative Biochemistry and Physiology 128B 565 - 573 2001 [Refereed][Not invited]
  
• Positional distribution of DHA and EPA in phosphatidylcholine and phosphatidylethanolamine from different tissues of squids

  D.Igarashi, K.Hayashi, H.Kishimura

  Journal of Oleo Science 50 729 - 734 2001 [Refereed][Not invited]
  
• Isolation and characteristics of trypsin inhibitor from the hepatopancreas of a squid (Todarodes pacificus)

  H.Kishimura, H.Saeki, K.Hayashi

  Comparative Biochemistry and Physiology 130B 117 - 123 2001 [Refereed][Not invited]
  
• Amount and composition of wax esters in salted and dried roe from mullet of Australia

  K.Hayashi, H.Kishimura

  Journal of Japan Oil Chemists' Society 49 1401 - 1406 2000 [Refereed][Not invited]
  
• cDNA cloning and sequencing of phospholipase A2 from the pyloric ceca of the starfish Asterina pectinifera

  H.Kishimura, T.Ojima, K.Hayashi, K.Nishita

  Comparative Biochemistry and Physiology 126B 579 - 586 2000 [Refereed][Not invited]
  
• Distribution and composition of diacyl glyceryl ethers in different tissues of the mature and immature spiny dogfish Squalus acanthias

  K.Hayashi, H.Kishimura

  Journal of Japan Oil Chemists' Society 49 325 - 331 2000 [Refereed][Not invited]
  
• Amino acid sequence of phospholipase A2 from the pyloric ceca of starfish Asterina pectinifera

  H.Kishimura, T.Ojima, H.Tanaka, K.Hayashi, K.Nishita

  Fisheries Science 66 104 - 109 2000 [Refereed][Not invited]
  
• Preparation of neoglycoprotein from carp myofibrillar protein and alginate oligosaccharide: improved solubility in low ionic strength medium

  R.Sato, T.Sawabe, H.Kishimura, K.Hayashi, H.Saeki

  Journal of Agricultural and Food Chemistry 48 17 - 21 2000 [Refereed][Not invited]
  
• Isolation and characteristics of phospholipase A2 from the pyloric ceca of the starfish Asterina pectinifera

  H.Kishimura, K.Hayashi

  Comparative Biochemistry and Physiology 124B 483 - 488 1999 [Refereed][Not invited]
  
• Content and composition of diacyl glyceryl ethers in the pyloric ceca and ovaries of the asteroids Solaster paxillatus and Asterias amurensis

  K.Hayashi, H.Kishimura

  Fisheries Science 63 945 - 949 1997 [Refereed][Not invited]
  
• Preparation and purification of DHA-enriched triacylglycerols from fish oils by column chromatography

  K.Hayashi, H.Kishimura

  Fisheries Science 62 842 - 843 1996 [Refereed][Not invited]
  
• Preparation of n-3 PUFA ethyl ester concentrates from fish oil by column chromatography on silicic acid

  K.Hayashi, H.Kishimura

  Nippon Suisan Gakkaishi 59 1429 - 1429 1993 [Refereed][Not invited]
  
• Seasonal changes in the contents of eicosapentaenoic acid-containing triglycerides in hepatopancreas of scallop

  K.Hayashi, H.Kishimura

  Nippon Suisan Gakkaishi 57 1397 - 1401 1991 [Refereed][Not invited]
  
• Free amino acids of starfish

  H.Kishimura, K.Hayashi

  Nippon Suisan Gakkaishi 56 1693 - 1693 1990 [Refereed][Not invited]
  
• Level and composition of diacyl glyceryl ethers in the different tissues and stomach contents of giant squid Moroteuthis robusta

  K.Hayashi, H.Kishimura, Y.Sakurai

  Nippon Suisan Gakkaishi 56 1635 - 1639 1990 [Refereed][Not invited]
  
• ヒトデ類のプロテアーゼ活性

  岸村栄毅, 林 賢治

  日本水産学会誌 55 843 - 846 1989 [Refereed][Not invited]
  
• アカザラガイミオシンおよびそのハイブリッドミオシンのCa感受性とCa結合性

  岸村栄毅, 尾島孝男, 西田清義

  日本水産学会誌 52 1469 - 1472 1986 [Refereed][Not invited]
  
• 魚類のミオシン軽鎖とアカザラガイ・ミオシンとの交叉試験

  岸村栄毅, 尾島孝男, 西田清義

  日本水産学会誌 52 847 - 851 1986 [Refereed][Not invited]
  

Books etc

• Advances in Oligosaccharides and Polysaccharide Modifications in Marine Bioresources

  Editors, Yuya Kumagai, Hideki Kishimura, Benwei Zhu (Editor)
  MDPI 2023/08
• Marine_Bioactive_PeptidesStructure_Function_and_Application

  A.M.M.Martin, Y.Miyabe, T.Shimizu, W.Matsui, Y.Kumagai, H.Kishimura (Contributorpp.63-77)
  MDPI 2023/07 1 163
• Mycosporine-Like Amino Acids from Marine Resource

  Y. Nishida, Y. Kumagai, S. Michiba, H. Yasui, H. Kishimura (Joint workpp. 39-56)
  Marine Drugs, Multidiciplinary Digital Publishing Institute（MDPI） 2021/01
• Implications and Applications: Animals and Microbes (Advances in Food and Nutrition Research)

  H. Kishimura (Joint workMarine Medicinal Foods; Volume 65; Chapter 29)
  ELSEVIER 2012/02

Conference Activities & Talks

• 函館産マコンブの多糖成分の機能性について  [Invited]

  ○熊谷祐也, 岸村栄毅

  海藻活用研究会令和5年度定期シンポジウム  2024/02
• 函館産マコンブ Saccharina japonica 由来多糖類の調製と その収量，組成及び抗酸化作用に関する研究  [Not invited]

  ○小島大樹, 今武洋人, 田畑大伍, 岸村栄毅, 熊谷祐也

  令和5年度 日本水産学会 北海道支部大会  2024/01
• 4種紅藻由来マイコスポリン様アミノ酸に関する研究  [Not invited]

  ○山本竜矢, 熊谷祐也, 岸村栄毅

  令和5年度 日本水産学会 北海道支部大会  2024/01
• 4種紅藻由来マイコスポリン様アミノ酸の 含有量及び組成の月別変動と抗酸化活性  [Not invited]

  ○山本竜矢, 熊谷祐也, 岸村栄毅

  2023年度 日本農芸化学会北海道支部 第２回学術講演会  2023/12
• 函館産マコンブ由来フコイダンの月別変動  [Not invited]

  ○馬場惇平, 熊谷祐也, 岸村栄毅

  2023年度 日本農芸化学会北海道支部 第２回学術講演会  2023/12
• Fucoidan from Kombu Saccharina japonica: Monthly variation and structure analysis

  ○Jumpei Baba, Yuya Kumagai, Hideki Kishimura

  13th Joint International Symposium on Food Science and Technology Among NUS, TUMSAT, HU, and KU  2023/11
• MAAs

  ○中目 凛, 森田理央, 瀧澤巧季, 山本竜矢, 熊谷祐也, 岸村栄毅

  HAKODATEアカデミックリンク2023  2023/11
• 劇場版 KOMBU×FAMILY CODE：Brown  [Not invited]

  ○濱崎海瑠, 馬場惇平, 張昕然, 濱崎海瑠, 田畑太伍, 熊谷祐也, 岸村栄毅

  HAKODATEアカデミックリンク2023  2023/11
• ダルスの光タンパク質で健康に！  [Not invited]

  ○太田龍成, 松井 亘, 熊谷祐也, 岸村栄毅

  HAKODATEアカデミックリンク2023  2023/11
• Characterization of Food Functionalities of a Land Cultivated Red Alga Dulse (Devaleraea inkyuleei, formerly Palmaria palmata in Japan)  [Not invited]

  ⚪︎Yuya Kumagai, Hideki Kishimura

  16th Asian Congress on Biotechnology (ACB) 2023  2023/10
• 函館産マコンブ由来フコイダンの月別変動 及び構造特性について  [Not invited]

  ○馬場惇平, 熊谷裕也, 岸村栄毅

  第6回 北大・部局横断シンポジウム  2023/10
• Studies on DPPIV Inhibitory Effect of Peptide from Red Alga Dulse  [Invited]

  ⚪︎Wataru Matsui, Yuya Kumagai, Hideki Kishimura

  Seminar of International Technology Cooperation with Pukyong National University, Hokkaido University and PL Micromed  2023/08
• Studies of Oyster Ferritin and Kombu Fucoidan

  ⚪︎Pu Yuan, Yuya Kumagai, Hideki Kishimura

  Seminar of International Technology Cooperation with Pukyong National University, Hokkaido University and PL Micromed  2023/08
• Preparation and Characterization of Xylooligosaccharides from Red Alga Dulse (Devaleraea inkyuleei) by Subcritical Water Treatment  [Invited]

  ⚪︎Yukihiko Tatsumi, Yuya Kumagai, Hideki Kishimura

  Seminar of International Technology Cooperation with Pukyong National University, Hokkaido University and PL Micromed  2023/08
• 真昆布からの中間素材の物性・機能性評価  [Invited]

  熊谷祐也, ○岸村栄毅

  海藻活用研究会 令和5年度 総会  2023/06
• 紅藻ウミゾウメンの葉緑体DNAにコードされるタンパク質に由来するDPP-IV阻害ペプチドのin silico解析  [Not invited]

  Martin Alain Mune Mune, 陳 瑞郷, 熊谷祐也, ○岸村栄毅

  第23回マリンバイオテクノロジー学会大会  2023/05
• Polysaccharides from brown algae: relationship between structure and function  [Invited]

  ○Yuya Kumagai, Hiroki Kojima, Jumpei Baba, Hideki Kishimura

  East Asia Fisheries Technologists Association (EAFTA) 2023  2023/05
• 北海道産ダルスに関する研究  [Invited]

  ○岸村栄毅

  国立遺伝学研究所 セミナー  2023/03  国立遺伝学研究所  国立遺伝学研究所
  
• 函館産褐藻由来の多糖成分について  [Invited]

  ○岸村栄毅, 馬場惇平, 熊谷祐也

  海藻活用研究会 令和４年度定期シンポジウム  2023/03  北海道函館市  海藻活用研究会
  
• 海藻ダルスなどの利活用の可能性  [Invited]

  ○岸村栄毅

  日本食品科学工学会 北海道支部 第2回Web公開セミナー「道南食資源の生産・利用・評価等に関する取り組み」  2022/12
• ビフィズス菌の増殖に適した 紅藻ダルス由来キシロオリゴ糖の組成

  ○吉田光里, 熊谷祐也, 岸村栄毅

  日本水産学会 北海道支部大会  2022/11
• 函館産褐藻由来フコイダンの比較  [Not invited]

  ○馬場惇平, 熊谷祐也, 岸村栄毅

  日本水産学会 北海道支部大会  2022/11
• 紅藻ダルス由来のマイコスポリン様アミノ酸の 月別変動および効率的な抽出方法の検討  [Not invited]

  ○山本竜矢, 熊谷祐也, 岸村栄毅

  令和4年度 日本農芸化学会 北海道・東北合同支部会  2022/09
• 紅藻ダルス由来タンパク質のDPP Ⅳ阻害作用 に関する研究  [Not invited]

  ○松井 亘, 熊谷祐也, 岸村栄毅

  令和4年度 日本農芸化学会 北海道・東北合同支部会  2022/09
• 紅藻ダルス由来キシランから 亜臨界水を用いたオリゴ糖の調製に関する研究  [Not invited]

  ○辰巳幸彦, 熊谷祐也, Byung-Soo Chun, 岸村栄毅

  令和4年度 日本農芸化学会 北海道・東北合同支部会  2022/09
• 紅藻ダルスの成分特性について  [Invited]

  ○岸村栄毅

  日本応用藻類学会第20回大会 シンポジウム  2022/09
• 紅藻ツルシラモ由来フィコエリスロビリンの生合成に関わる酵素に関する研究  [Not invited]

  宮部好克, 熊谷祐也, 清水健志, 松井 亘, 佐藤諒介, ○岸村栄毅

  第22回マリンバイオテクノロジー学会大会  2022/05
• 海藻スプラウト：小型海藻の利用適正に関する研究  [Not invited]

  川越力, 木村和世, 岸村栄毅, 熊谷祐也, ○木下康宣, 鳥海滋

  2022年度北海道立工業技術センター研究成果発表会  2022/05
• 海藻生産におけるITニーズ  [Invited]

  岸村栄毅

  バイオ＆ヘルスケア分野でのIT企業に求めるニーズ発表会  2022/04
• 紅藻ツルシラモ由来フィコエリスリン・ガンマ鎖の構造特性  [Not invited]

  熊谷祐也, 宮部好克, 清水健志, 佐藤諒介, ○岸村栄毅

  令和４年度日本水産学会春季大会  2022/03
• 紅藻類のマイコスポリン様アミノ酸の可能性  [Invited]

  ○岸村栄毅, 熊谷祐也, 木下康宣, 安井 肇, 川越 力

  海藻活用研究会定期シンポジウム 〜ウィズコロナの海藻活用〜  2022/02
• 季節変動から紐解くダルス「MAAs」産業利用への試み  [Not invited]

  ○山本竜矢, ○前田侑也, 熊谷祐也, 岸村栄毅

  HAKODATEアカデミックリンク2021  2021/11  函館  キャンパスコンソーシアム函館
  
• 海藻のヌメヌメ成分「フコイダン」の最大Maxパワー力を生かすために  [Not invited]

  ○伊藤大翔, ○松井 亘, 熊谷祐也, 岸村栄毅

  HAKODATEアカデミクリンク2021  2021/11  函館  キャンパスコソーシアム函館
  
• ダルスが腸に届くまで  [Not invited]

  ○辰巳幸彦, 松本晃帆, 吉田光里, 熊谷祐也, 岸村栄毅

  HAKODATEアカデミックリンク2021  2021/11  函館  キャンパスコンソーシアム函館
  
• Vibrio由来glycoside hydrolase family 17 β-1,3-glucanaseの機能解析  [Not invited]

  ○熊谷祐也, 岸村栄毅

  令和3年度 日本水産学会秋季大会  2021/09
• 紅藻ダルス由来β-(1→3)/β-(1→4)キシランの 腸内細菌増殖作用の検討  [Not invited]

  ○吉田光里, 熊谷祐也, 岸村栄毅

  令和3年度 日本水産学会秋季大会  2021/09
• 紅藻ツルシラモ由来フィコエリスリン の構造・機能特性  [Not invited]

  前田俊介, 熊谷侑貴, 宮部好克, 佐藤諒介, 熊谷祐也, ○岸村栄毅

  令和3年度 日本水産学会秋季大会  2021/09
• 紅藻ダルス小形葉体の 栄養特性に関する研究  [Not invited]

  ○木下康宣, 鳥海 滋, 川越 力, 木村和世, 熊谷祐也, 岸村栄毅

  日本応用藻類学会 第19回大会  2021/09
• 紅藻ウミゾウメン葉緑体DNAにコードされるタンパク質由来ACE阻害ペプチドのin silico解析  [Not invited]

  ○陳 瑞卿, 丁 佳琦, 水田浩之, 熊谷祐也, 岸村栄毅

  2021年度 日本農芸化学会北海道支部 第1 回学術講演会  2021/07
• 海洋深層水を活用した海藻スプラウトの 陸上養殖と利用適性に関する研究  [Not invited]

  ○木下康宣, 木村和世, 川越 力, 高野智宏, 熊谷祐也, 岸村栄毅, 宇治利樹, 水田浩之

  2021年度 北海道立坑業技術センター研究成果発表会  2021/06
• 紅藻ダルス由来β-(1→3)/β-(1→4)-キシロオリゴ糖調製法の開発およびエンド型キシラナーゼの基質特異性  [Not invited]

  ○藤井勇樹, 熊谷祐也, 岸村栄毅, 畑中 唯史

  R2年度 日本応用糖質科学会 北海道支部 支部賞授賞式・受賞公演およびシンポジウム  2021/01
• Bifidobacterium adolescentisによるβ-(1→3)-キシロシル-キシロビオース分解機構の解明  [Not invited]

  ○小林真奈美, 熊谷祐也, 岸村栄毅

  R2年度 日本応用糖質科学会 北海道支部 支部賞授賞式・受賞公演およびシンポジウム  2021/01
• 人類を紫外線から守る海藻？！ 函館産紅藻に秘めたるMAAsのポテンシャル  [Not invited]

  ○杉山佳奈海, 西田有輝, 熊谷祐也, 岸村栄毅

  HAKODATEアカデミックリンク2020  2020/11
• 絶対正義オリゴ糖～もっと海藻は輝ける～  [Not invited]

  ○吉田光里, 小林真奈美, 栗田大輝, 熊谷祐也, 岸村栄毅

  HAKODATEアカデミックリンク2020  2020/11
• 天然＆陸上栽培された紅藻成分の相違とは？  [Not invited]

  ○大井一真, 熊谷祐也, 岸村栄毅

  HAKODATEアカデミックリンク2020  2020/11
• 放線菌 Streptomyces thermogriseus エンド型キシラナーゼを用いた紅藻ダルス β(1-3/1-4)キシロオリゴ糖調製法の開発  [Not invited]

  ○藤井 勇樹, 熊谷 祐也, 岸村 栄毅, 畑中 唯史

  2020年度 日本農芸化学会北海道支部／日本栄養・食糧学会北海道支部 合同学術講演会  2020/12
• 岩のり製品由来タンパク質から調製したペプチドの ACE 阻害作用  [Not invited]

  ○森河理絵, 熊谷祐也, 岸村栄毅

  令和 2 年度日本水産学会 北海道支部大会  2020/12
• 紅藻ダルス由来キシランの簡易調製法の開発とその酵素分解物による Bifidobacterium の増殖  [Not invited]

  ○栗田大輝, 熊谷祐也, 安井 肇, 岸村栄毅

  令和 2 年度日本水産学会 北海道支部大会  2020/12
• Efficient extraction and monthly variation of mycosporine-like amino acids from red alga dulse in Japan  [Invited]

  ○Yuki Nishida, Yuya Kumagai, Shunta Michiba, Hajime Yasui, Hideki Kishimura

  Online International Symposium of FSMILE 2020: Current Trends on Food Processing, Safety and Nutrition  2020/11
• Pepsinogens and pepsins from the stomach of lizardfish (Saurida micropectoralis): Purification and some biochemical properties  [Not invited]

  ○S.Kuepethkaew, H.Kishimura, S.Damodaran, S.Klomklao

  The 5th National Conference and The1st International Conference on Informatics, Agriculture, Management, Business administration, Engineering, Sciences and Technology (IAMBEST2020)  2020/05
• 「海藻の秘密兵器！？「マイコスポリン様アミノ酸」  [Invited]

  ○西田有輝・熊谷祐也・岸村栄毅

  アイデアと街を繋ぎ函館の未来を創る 合同研究発表会  2020/02
• A search for β-(1→3)/β-(1→4)-xylotriose degradation enzyme from Bifidobacterium adolescentis  [Invited]

  ○Manami Kobayashi, Yuya Kumagai, Hideki Kishimura

  12th Joint International Symposium on Food Science and Technology among NUS, TUMSAT, HU, KU and ZGU, 1-2 December 2019, National University of Singapore  2019/12
• 海洋深層水を用いた北方系未利用紅藻「ダルス」の周年栽培技術開発  [Invited]

  岸村栄毅

  産総研北海道センターワークショップ in 函館  2019/11
• 最強のマースおにいさんはただひとり！オレだ！  [Not invited]

  ○西田有輝, 熊谷祐也, 岸村栄毅

  HAKODATEアカデミックリンク2019  2019/11
• ナマコのヌメヌメ「フコイダン」  [Not invited]

  ○瀬能拓海, 栗田大輝, 熊谷祐也, 岸村栄毅

  HAKODATEアカデミックリンク2019  2019/11
• ボーっと海苔食べてると答えられない⁉「フィコビリタンパク質って？」  [Not invited]

  森河理絵, 澄川果奈, 熊谷祐也, 岸村栄毅

  HAKODATEアカデミックリンク2019  2019/11
• Bifidobacterium adolescentisのβ-(1→3)/β-(1→4)-キシロトリオース分解機構に関する研究  [Invited]

  小林真奈美, 熊谷祐也, 岸村栄毅

  第5回 北海道大学部局横断シンポジウム  2019/11
• 紅藻ウップルイノリのACE阻害ペプチドの探索  [Invited]

  渡邊慧, 勝倉 智, 岡田千晃, 熊谷祐也, 岸村栄毅

  第5回 北海道大学部局横断シンポジウム  2019/11
• 海藻の栄養・機能性成分（蛋白・多糖類）  [Invited]

  岸村栄毅

  海藻活用シンポジウム  2019/09
• 函館産紅藻ダルス由来マイコスポリン様アミノ酸の 熱安定性および機能性  [Not invited]

  道場俊太, 木下康宜, 安井 肇, 熊谷祐也, 岸村栄毅

  平成31年度日本水産学会春季大会  2019/03
• 紅藻ダルス由来β-(1→3)/β-(1→4)-キシロトリオースの Bifidobacterium属細菌選択増殖作用の検討  [Not invited]

  山本陽平, 小林真奈美, 熊谷祐也, 山崎浩司, 安井 肇, 尾島孝男, 岸村栄毅

  平成31年度日本水産学会春季大会  2019/03
• 紅藻ダルスのタンパク質に含まれる機能性ペプチドの探索  [Invited]

  熊谷祐也, 岸村栄毅

  第4回 北大・部局横断シンポジウム  2019/01
• 函館産ダルス由来マイコスポリン様アミノ酸の 含有量・組成の時期変動及び安定性に関する検討  [Not invited]

  道場俊太, 武田朋之, 木下康宣, 安井 肇, 栗原秀幸, 熊谷祐也, 岸村栄毅

  日本食品科学工学会 北海道支部大会  2018/12
• 実はこんなにすごい！！ スーパーフード "ダルス"  [Invited]

  栗田大輝, 熊谷祐也, 岸村栄毅

  合同研究発表会 シエスタハコダテ編 ademikku〜HAKODATEアカデミックリンク2018連携〜 アイデアと街を繋ぎ箱館の未来を創る  2018/11
• 紅藻の真価 〜北海道より〜  [Not invited]

  岸本堯大, 熊谷祐也, 岸村栄毅

  HAKODATEアカデミックリンク2018  2018/11
• 絶対に捨てられない海藻がここにある  [Not invited]

  小林真奈美, 山本陽平, 熊谷祐也, 岸村栄毅

  HAKODATEアカデミックリンク2018  2018/11
• 紅藻"ダルス"は"第２のガゴメ"となりうるか  [Not invited]

  藤井勇樹, 熊谷祐也, 岸村栄毅

  HAKODATEアカデミックリンク2018  2018/11
• 実はこんなにすごい！！ スーパーフード "ダルス"  [Not invited]

  栗田大輝, 熊谷祐也, 岸村栄毅

  HAKODATEアカデミックリンク2018  2018/11
• 紅い海藻を科学する  [Invited]

  岸村栄毅

  公開講座「函館学2018」  2018/09
• ダルスの成分と機能性  [Invited]

  岸村栄毅

  第4回食科学プラットフォームセミナー  2018/08
• 紅藻ダルスから調製したキシロオリゴ糖のNMRによる構造解析  [Not invited]

  山本陽平, 安井 肇, 岸村栄毅

  平成30年度 日本水産学会春季大会  2018/03
• 紅藻ダルス・キシランからキシロオリゴ糖の調製とその成分分析  [Not invited]

  山本陽平, 安井 肇, 岸村栄毅

  平成30年度 日本水産学会春季大会  2018/03
• 未・低利用水産物から有用生化学成分の探索  [Invited]

  岸村栄毅

  ケミカルバイオロジー研究会  2018/03
• 人工消化物の静脈内投与によるチョウザメ由来コラーゲンペプチドの血糖上昇抑制作用機序の検討  [Not invited]

  笹岡友季穂, 岸村栄毅

  平成30年度 日本農芸化学会大会  2018/03
• Collagen peptides prepared from sturgeon improve glucose tolerance in normal mice  [Invited]

  ○Y.Sasaoka, H.Kishimura

  NUS-TUMSAT-HU Symposium on Food Science & Technology  2017/12
• 健康機能と遺伝子の大冒険だニャン!  [Not invited]

  柿崎真里奈, 川口寧々, 澄川果奈, 渡邊慧, 岸村栄毅

  HAKODATEアカデミックリンク2017  2017/11
• Sturgeon collagen peptides lower blood glucose in rodents  [Not invited]

  ○Y.Sasaoka, H.Kishimura

  8th International Symposium on Sturgeon  2017/09
• チョウザメ由来コラーゲンペプチドは体内で糖代謝促進作用を示す  [Not invited]

  笹岡友季穂, 岸村栄毅

  平成29年度 日本農芸化学会大会  2017/03
• 解読せよ！ダルスからのシグナルメッセージ  [Not invited]

  壺内亮太, 武井健太郎, 岸村栄毅

  HAKODATE アカデミックリンク2016  2016/11
• 腸がキレイでチョーうれしい！－紅藻ダルスの有効利用－  [Not invited]

  山本陽平, 道場俊太, 佐藤直登, 岸村栄毅

  HAKODATE アカデミックリンク2016  2016/11
• チョウザメ由来コラーゲンペプチドは血中へ吸収され糖代謝促進作用を示す  [Not invited]

  笹岡友季穂, 岸村栄毅

  平成28年度日本栄養・食糧学会北海道支部大会  2016/10
• 紅藻ウップルイノリ由来フィコビリタンパク質のACE阻害作用と一次構造特性との関係  [Not invited]

  勝倉 哲, 清水健志, 安井 肇, 岸村栄毅

  平成28年度日本水産学会北海道東北支部大会  2016/10
• 紅藻ダルス由来フィコエリスリン摂取による老化促進モデルマウスSAMP10の脳機能改善作用  [Not invited]

  佐藤直登, 足立亨介, 安井 肇, 岸村栄毅

  平成28年度日本水産学会北海道東北支部大会  2016/10
• 紅藻ダルス由来フィコエリスリンの脳機能改善作用  [Not invited]

  佐藤直登, 足立亨介, 安井 肇, 岸村栄毅

  日本農芸化学会北海道支部 平成28年度第1回講演会（函館）  2016/08
• 紅藻ダルスの将来性  [Invited]

  岸村栄毅

  日本農芸化学会北海道支部 平成28年度第1回講演会（函館）  2016/08
• 紅藻アカバギンナンソウ由来フィコビリタンパク質の構造と機能  [Not invited]

  北出裕実, 宮部好克, 清水健志, 安井 肇, 岸村栄毅

  第18回マリンバイオテクノロジー学会大会  2016/05
• 北方系未利用紅藻ダルス由来フィコエリスリンの 学習記憶能改善作用  [Not invited]

  佐藤直登, 足立亨介, 安井 肇, 岸村栄毅

  第18回マリンバイオテクノロジー学会大会  2016/05
• 北方系紅藻類のタンパク質の構造と健康機能性  [Invited]

  岸村栄毅

  第18回マリンバイオテクノロジー学会大会 シンポジウム「北方系海藻の新規地域資源としての将来性」  2016/05
• スルメイカヘモシアニン分子のサブユニット間相互作用  [Not invited]

  加藤早苗, 吉岡武也, 清水健志, 岸村栄毅, 田中良和

  日本水産学会 春季大会  2016/03
• ボイル塩蔵ダルスのタンパク質及び色調特性  [Not invited]

  佐藤直登, 吉野真緒, 木下康宣, 安井 肇, 岸村栄毅

  日本食品科学工学会 北海道支部大会  2016/02
• 3.8 MDaの超巨大酸素運搬タンパク質ヘモシアニン会合体形成における結合糖鎖の役割  [Not invited]

  加藤早苗, K.Md.R.Islam, 吉岡武也, 清水健志, 岸村栄毅, 田中良和

  第88回 日本生化学会  2015/12
• The first crystal structure of 3.8-MDa supermolecule hemocyanin  [Not invited]

  ○Yoshikazu Tanaka, Asuka Matsuno, Zuoqi Gai, Koji Kato, Sanae Kato, Takeshi Shimizu, Takeya Yoshioka, Hideki Kishimura, Tohru Terada, Min Yao

  The 4th international symposium "Dynamical ordering of bimolecular systems for creation of integrated functions  2015/11
• ダルス由来フィコビリンの生合成経路の解析  [Not invited]

  熊谷侑貴, 宇治利樹, 宮部好克, 清水健志, 足立亨介, 安井肇, 岸村栄毅

  第17回マリンバイオテクノロジー学会大会  2015/05
• スルメイカヘモシアニン超分子構造における 結合糖鎖の関与  [Not invited]

  加藤早苗, 吉岡武也, 清水健志, 岸村栄毅, 田中良和

  平成27年度日本水産学会春季大会  2015/03
• ツルシラモ・アロフィコシアニンの遺伝子構造  [Not invited]

  熊谷侑貴, 宮部好克, 清水健志, 足立伸次, 安井 肇, 岸村栄毅

  平成27年度日本水産学会春季大会  2015/03
• 和の伝統食材"海藻"と健康  [Not invited]

  中村昭伸

  グリーンテクノバンク「医農融合研究シーズセミナー」  2015/02
• スルメイカヘモシアニンの分子構造および構造安定性  [Not invited]

  加藤早苗, 吉岡武也, 信太茂春, 清水健志, 岸村栄毅, 田中良和

  日本水産学会 北海道支部大会  2014/12
• 次世代シーケンサによるツルシラモ葉緑体DNAの分析  [Not invited]

  熊谷侑貴, 宮部好克, 清水健志, 足立伸次, 安井 肇, 岸村栄毅

  日本水産学会 北海道支部大会  2014/12
• 寒帯性海域に分布する未利用紅藻ダルス  [Invited]

  岸村栄毅

  北大リサーチ＆ビジネスパークセミナー  2014/11
• 捨てるなんてもったいない！ーホタテとダルスの健康機能ー  [Not invited]

  勝倉 哲, 熊谷侑貴, 吉野真緒, 岸村栄毅

  HAKODATE アカデミックリンク2014  2014/11
• Functionality of phycobiliproteins obtained from red algae in Hokkaido, Japan  [Not invited]

  Hideki Kishimura

  Bilateral Symposium on Food Science and Technology between Singapore and Japan  2014/10
• 分子量 4 MDaの細胞外酸素運搬体ヘモシアニンの解離－再会合  [Not invited]

  加藤早苗, Md. Rafiqul, Islam Khan, 吉岡武也, 信太茂春, 岸村栄毅, 清水健志, 田中良和

  第87回 日本生化学会  2014/10
• 頭足類ヘモシアニン分子のサブユニット間相互作用  [Not invited]

  加藤早苗, Md. Rafiqul, Islam Khan, 吉岡武也, 信太茂春, 岸村栄毅, 清水健志, 田中良和

  日本動物学会第85回仙台大会  2014/09
• Characteristics of Acid Soluble and Pepsin Soluble-Collagens from Swim Bladder of Yellowfin Tuna (Thunnus albacares)  [Not invited]

  Onouma Kaewdang, Soottawat Benjakul, Thammarat Kaewmanee, Hideki Kishimura

  The 16th FOOD INNOVATION ASIA CONFERENCE 2014 12 -13 June 2014, BITEC Bangna, Bangkok, Thailand  2014/06
• ティラピア鱗由来アテロコラーゲンから調製したゼラチン水溶液のゲル化に伴う動的粘弾性挙動  [Not invited]

  志田奈津実, 槇靖幸, 土橋敏明, 小柳佳子, 岸村栄毅, 都木靖彰, 元村まみ, 市川寿

  第37回日本バイオレオロジー学会年会  2014/06
• Antioxidant function of the major protein in the gonads of sea urchin Strongylocentrotus nudus  [Not invited]

  ○M.Nagaya, H.Wang, S.Yamashina, S.Maeda, H.Kishimura, Y.Itabashi, N.Azuma, K, Y.Takagi

  Hokkaido-Singapore Scientific Seminar on Food Science and Biotechnology 2014  2014/06
• 紅藻ダルスの葉緑体DNA  [Not invited]

  宮部好克, 武田朋之, 足立亨介, 安井肇, 岸村栄毅

  第16回マリンバイオテクノロジー学会大会  2014/05
• スルメイカヘモシアニンの一次構造解析  [Not invited]

  清水健志, 加藤佑基, 蓋 作啓, 田中良和, 宮部好克, 菅野 岳, 岸村栄毅, 吉岡武也, 加藤早苗

  平成26年度日本水産学会春季大会  2014/03
• スルメイカヘモシアニンの構造安定化条件の検討  [Not invited]

  加藤早苗, Md. Rafiqul, Islam Khan, 吉岡武也, 信太茂春, 岸村栄毅, 清水健志, 田中良和

  平成26年度日本水産学会春季大会  2014/03
• スルメイカヘモシアニンの結晶構造解析  [Not invited]

  田中良和, 加藤公児, 蓋 作啓, 田中深雪, 田中 勲, 姚 閔, 加藤佑基, 清水健志, 宮部好克, 菅野 岳, 岸村栄毅, 吉岡武也, 加藤早苗

  平成26年度日本水産学会春季大会  2014/03
• 効率的な脂質吸収を可能にするホタテ由来ペプチドの開発  [Not invited]

  武田浩郁, 岸村栄毅

  北海道の食と省エネを中心とした新技術説明会  2014/01
• プロテオーム解析に基づいた活スルメイカの健全性評価  [Not invited]

  加藤早苗, Md.R.I.Khan, 岸村栄毅, 清水健志, 信太茂春, 田中良和, 吉岡武也

  平成25年度 日本水産学会北海道支部大会  2013/12
• 海産魚類胃由来ペプシンの温度安定性と構造との関係  [Not invited]

  伊藤滉祐, 岸村栄毅, 成松庸二, 佐藤暁之, 都木靖彰, 佐伯宏樹

  平成25年度 日本水産学会北海道支部大会  2013/12
• ヒトデを丸ごと利用する -血糖値上昇抑制剤等の製造-  [Not invited]

  麻生真悟, 岸村栄毅

  北海道地域5大学3高専1公設試による新技術説明会  2013/11
• ACE inhibitory peptides prepared from phycobiliproteins of dulse  [Not invited]

  H.Kishmura

  1st East Asia Fish Technologists Association Conference  2013/11
• Anti-inflammatory activity of salmon meat peptide introduced alginate oligosaccharide is enhanced by the suppression of NF-kB pathway  [Not invited]

  ○M.Nishizawa, H.Kishimura, H.Saeki

  Internatinal Conference and Exhibition on Nutraceuticals and Functional Foods 2013  2013/11
• Major allergen in gray mullet roe and its IgE cross-reactivity to chum salmon roe  [Not invited]

  ○Y.Shimizu, Z.Li, H.Kishimura, A.Hara, K.Watanabe, H.Saeki

  Internatinal Conference and Exhibition on Nutraceuticals and Functional Foods 2013  2013/11
• 海の不思議な世界 〜アメフラシの紫色の煙幕〜  [Not invited]

  武田朋之, 宮部好克, 岸村栄毅

  HAKODATE アカデミックリンク2013  2013/11
• 分子量 4MDa の巨大酸素運搬蛋白質会合体ヘモシアニンの結晶構造解析  [Not invited]

  田中良和, 加藤公児, 蓋 作啓, 田中深雪, 加藤早苗, 清水健志, 岸村栄毅, 菅野 岳, 宮部好克, 岩崎憲治, 田中 勲, 姚 閔

  平成25年度日本結晶学会年会および総会  2013/10
• スルメイカヘモシアニン分子のサブユニットへの解離と再会合  [Not invited]

  加藤早苗, Md. Rafiqul, Islam Khan, 谷口隆信, 岸村栄毅, 清水健志, 加藤佑基, 吉岡武也

  日本動物学会 第84回大会  2013/09
• マダラ幽門垂キモトリプシンAの構造特性  [Not invited]

  中村一尚, 岸村栄毅, 岡田知晃, 豊田栄子, 山本 潤, 佐伯宏樹

  平成25年度日本水産学会秋季大会  2013/09
• 頭足類スルメイカ生体内におけるヘモシアニン分子の解離は酸素運搬障害を引き起こす  [Not invited]

  加藤早苗, Md. Rafiqul, Islam Khan, 谷口隆信, 岸村栄毅, 清水健志, 加藤佑基, 吉岡武也

  第86回 日本生化学会  2013/09
• 海藻タンパク質の研究状況  [Not invited]

  岸村栄毅

  第4回 函館マリンバイオクラスター 研究テーマ 2 グループミーティング  2013/06
• チョウザメ由来アテロコラーゲンのゲル化に伴う粘弾性変化  [Not invited]

  関口琢磨, 槙 靖幸, 近藤信吾, 土橋敏明, 村元まみ, 市川 寿, 小柳佳子, 岸村栄毅, 安部智貴, 足立伸次, 都木靖彰

  日本バイオレオロジー学会  2013/06
• ダルスACE阻害ペプチドの由来タンパク質  [Not invited]

  岸村栄毅, 宮部好克, 古田智絵, 安井 肇, 佐伯宏樹

  第15回 マリンバイオテクノロジー学会大会  2013/06
• マウス腸管ループ法による難消化性タンパク質の吸収動態評価  [Not invited]

  京坂一生, 横内千恵, 清水 裕, 岸村栄毅, 佐伯宏樹

  第67回 日本栄養・食糧学会大会  2013/05
• 等電点電気泳動分画によるアルギン酸オリゴ糖修飾シロザケ筋肉消化物中の抗炎症ペプチドの回収  [Not invited]

  西澤瑞穂, 佐々木梨那, 三枝武蔵, 岸村栄毅, 佐伯宏樹

  第67回 日本栄養・食糧学会大会  2013/05
• 紅藻ダルス由来フィコビリタンパク質の抗炎症作用  [Not invited]

  李 大英, 西澤瑞穂, 三枝武蔵, 今井奈穂子, 岸村栄毅, 佐伯宏樹

  第67回 日本栄養・食糧学会大会  2013/05
• 紅藻ダルスの機能性タンパク質  [Invited]

  岸村栄毅

  第57回 分析化学討論会 若手ポストシンポジウム  2013/05
• 紅藻ツルシラモ由来フィコシアニンの一次構造  [Not invited]

  前田俊介, 岸村栄毅, 武田朋之, 宮部好克, 古田智絵, 足立伸次, 安井 肇, 佐伯宏樹

  平成25年度 日本水産学会春季大会  2013/03
• 紅藻ダルス由来フィコエリスリンβ鎖の大腸菌による発現  [Not invited]

  岸村栄毅, 宮部好克, 古田智絵, 清水健志, 加藤佑基, 安井 肇, 佐伯宏樹

  平成25年度 日本水産学会春季大会  2013/03
• チョウザメのコラーゲン、海藻の色素タンパク質、魚の酵素  [Not invited]

  前田俊介, 伊藤滉祐, 其田もも子, 中村一尚, 武田朋之, 小柳佳子, 宮部好克, 古田智絵, 富田友季穂, 菅野 岳, 岸村栄毅, 佐伯宏樹

  HAKODATEアカデミックリンク2012  2012/11
• マダラ幽門垂キモトリプシンBの一次構造特性  [Not invited]

  中村一尚, 菅野 岳, 岸村栄毅, 山本 潤, 清水健志, 加藤佑基, 佐伯宏樹

  平成24年度 日本水産学会秋季大会  2012/09
• 熱帯性海産魚類トリプシンの一次構造解析  [Not invited]

  菅野 岳, 岸村栄毅, 木原 稔, 清水健志, 加藤佑基, 佐伯宏樹

  平成24年度 日本水産学会秋季大会  2012/09
• 紅藻アナダルス由来フィコエリスリンの一次構造  [Not invited]

  武田朋之, 岸村栄毅, 宮部好克, 安井 肇, 佐伯宏樹

  平成24年度 日本水産学会秋季大会  2012/09
• 紅藻ダルス由来フィコシアニンα鎖の一次構造  [Not invited]

  宮部好克, 岸村栄毅, 清水健志, 加藤佑基, 安井 肇, 佐伯宏樹

  平成24年度 日本水産学会秋季大会  2012/09
• 紅藻ダルス由来アロフィコシアニンα鎖の一次構造  [Not invited]

  岸村栄毅, 宮部好克, 古田智絵, 安井 肇, 佐伯宏樹

  平成24年度 日本水産学会秋季大会  2012/09
• Seasonal changes in thermostability of several muscle proteins and enzymes from silver carp  [Not invited]

  ○Chunhong Yuan, Gaku Kanno, Hideshi Kishimura, Xichang Wang, Shunsheng Chen, Kunihiko Konno, Ikuo Kimura

  The 2012 International Conference of Food Science and Technology  2012/08
• Structure and function of trypsin from starfish Asterina pectinifera  [Not invited]

  Hideki Kishimura

  14th International Echinoderm Conference  2012/08
• 紅藻類ダルス由来フィコビリタンパク質の構造と健康性機能  [Not invited]

  宮部好克, 古田智絵, 岸村栄毅, 安井 肇, 佐伯宏樹

  平成24年度 日本農芸化学会北海道支部夏期シンポジウム  2012/07
• ガゴメ・クラスター形成とダルスの可能性  [Not invited]

  安井 肇, 岸村栄毅

  函館マリンバイオフォーラム2012  2012/07
• The relationship between thermostability and structure of fish trypsin  [Not invited]

  ○Gaku Kanno, Hideki Kishimura, Hiroki Saeki

  The 9th Asia-Pacific Marine Biotechnology Conference  2012/07
• Inhibitory Activity of Angiotensin I Converting Enzyme in Protein Hydrolysate from Dulse (Palmaria palmata)  [Not invited]

  Hideki Kishimura, Tomoe Furuta, Yoshikatsu Miyabe, Hajime Yasui, Hiroki Saeki

  The 9th Asia-Pacific Marine Biotechnology Conference  2012/07
• 加熱処理が魚卵抗原タンパク質の消化性とIgE結合能に及ぼす影響  [Not invited]

  清水 裕, 佐藤恵理, 渡辺一彦, 岸村栄毅, 佐伯宏樹

  平成24年度 日本食品化学学会  2012/06
• ダルスに含まれる色素タンパク質の構造と健康機能  [Not invited]

  岸村栄毅

  第3回 函館マリンバイオクラスター 研究テーマ 2 グループミーティング  2012/06
• チョウザメ・コラーゲン由来血糖値上昇抑制作用ペプチドの調製とその構造特性  [Not invited]

  富田友季穂, 岸村栄毅, 小柳佳子, Byung-Soo Chun, 安藤靖浩, 都木靖彰, 足立伸次, 佐伯宏樹

  第66回 日本栄養・食糧学会大会  2012/05
• 紅藻ダルス由来ペプチドのアンジオテンシンⅠ変換酵素阻害作用  [Not invited]

  古田智絵, 岸村栄毅, 宮部好克, 安井 肇, 佐伯宏樹

  第66回 日本栄養・食糧学会大会  2012/05
• 棲息温度の異なる淡水魚類トリプシンの 温度安定性と一次構造  [Not invited]

  菅野岳, 岸村栄毅, 袁 春紅, 清水健志, 加藤佑基, 佐伯宏樹

  平成24年度 日本水産学会春季大会  2012/03
• チョウザメ皮由来コラーゲンの調製とその性質  [Not invited]

  小柳佳子, 岸村栄毅, 富田友季穂, 都木靖彰, 足立伸次, 今野久仁彦, 佐伯宏樹

  平成24年度 日本水産学会春季大会  2012/03
• 紅藻ダルス由来フィコシアニンβ鎖の一次構造  [Not invited]

  宮部好克, 岸村栄毅, 清水健志, 加藤佑基, 安井 肇, 佐伯宏樹

  平成24年度 日本水産学会春季大会  2012/03
• ヒトデ体壁由来コラーゲン・ペプチドの アンジオテンシンI変換酵素阻害作用  [Not invited]

  岸村栄毅, 水田卓志, 佐伯宏樹

  平成24年度 日本水産学会春季大会  2012/03
• 紅藻ダルス由来フィコエリスリンα鎖の一次構造  [Not invited]

  宮部好克, 岸村栄毅, 菅野 岳, 清水健志, 加藤佑基, 安井 肇, 佐伯宏樹

  平成23年度 日本水産学会北海道支部大会  2011/11
• Hypoglycemic Effect of Collagen Peptide Prepared from Skin, Fin and Air Bladder of Sturgeon  [Not invited]

  ○Yukiho TOMITA, Hideki KISHIMURA, Yasuaki TAKAGI, Shinji ADACHI, Hiroki SAEKI

  2011 Annual Meeting of the International Society for Nutraceuticals and Functional Foods  2011/11
• Collagen Peptides Prepared from Starfish and its Health Benefits  [Not invited]

  Takashi MIZUTA, Yujiro NAGAI, Hideki KISHIMURA, Hirofumi TAKEDA, Shingo ASO, Masahiko KITAGAWA, Toshiyuki IIDA, Hiroki SAEKI

  2011 Annual Meeting of the International Society for Nutraceuticals and Functional Foods  2011/11
• マグロ類トリプシンの温度安定性と構造との関係  [Not invited]

  菅野岳, 岸村栄毅, 木原稔, 清水健志, 加藤佑基, 佐伯宏樹

  平成23年度 日本水産学会秋季大会  2011/09
• タラ類トリプシンの温度安定性と構造との関係  [Not invited]

  菅野岳, 岸村栄毅, 山本潤, 清水健志, 加藤佑基, 安藤清一, 佐伯宏樹

  平成23年度 日本水産学会秋季大会  2011/09
• 紅藻ダルス由来フィコエリスリンβ鎖の一次構造  [Not invited]

  宮部好克, 岸村栄毅, 菅野 岳, 清水健志, 加藤佑基, 安井 肇, 佐伯宏樹

  平成23年度 日本水産学会秋季大会  2011/09
• 紅藻由来フィコエリスリンの抽出と精製  [Not invited]

  宮部好克, 岸村栄毅, 安井 肇, 佐伯宏樹

  平成23年度 日本水産学会秋季大会  2011/09
• Effect of supercritical CO2 treatment on preparation of anchovy trypsin  [Not invited]

  ○Byung-Soo Chun, Hideki Kishimura, Kenichiro Abe, Gaku Kanno, Hiroki Saeki

  平成23年度 日本水産学会秋季大会  2011/09
• 卵黄タンパク質と脂質の相互作用がイクラ・アレルゲンの吸収挙動に及ぼす影響  [Not invited]

  藤田真伍, 横内千恵, 清水 裕, 岸村栄毅, 佐伯宏樹

  第65回 日本栄養・食糧学会大会  2011/05
• チョウザメ由来コラーゲン・ペプチドの血糖値上昇抑制作用  [Not invited]

  富田友季穂, 岸村栄毅, 都木靖彰, 足立伸次, 佐伯宏樹

  第65回 日本栄養・食糧学会大会  2011/05
• Study on the effect of gamma irradiation on sensory quality and amino acids yield of Antarctic krill extracted by supercritical carbon dioxide  [Not invited]

  ○Abdelkader Ali-Nehari, Hideki Kishimura, Ju-Woon Lee, Byung-Soo Chun

  平成23年度 日本水産学会春季大会  2011/03
• Application of supercritical CO2 on preparation of mackerel viscera for trypsin purification  [Not invited]

  ○Byung-Soo Chun, Hisashi Endo, Gaku Kanno, Hideki Kishimura, Hiroki Saeki

  平成23年度 日本水産学会春季大会  2011/03
• Study on the Thermal Stability of the Bio-Materials Obtained from Laminaria by Subcritical Water Hydrolysis  [Not invited]

  ○Jung-Nam Park, Abdelkader Ali-nehari, Jeong-Eun Sim, Hideki Kishimura, Byung-Soo Chun

  平成23年度 日本水産学会春季大会  2011/03
• シロザケ卵アレルゲンのエピトープ解析  [Not invited]

  清水 裕, 岸村栄毅, 渡辺一彦, 原 彰彦, 佐伯宏樹

  平成23年度 日本水産学会春季大会  2011/03
• 淡水魚類トリプシンの温度安定性と一次構造  [Not invited]

  菅野 岳, 岸村栄毅, 清水健志, 佐伯宏樹

  平成23年度 日本水産学会春季大会  2011/03
• Application of supercritical CO2 on preparation of mackerel viscera for trypsin purification  [Not invited]

  CHUN BYUNG-SOO, ENDO HISASHI, KANNO GAKU, KISHIMURA HIDEKI, SAEKI HIROKI

  日本水産学会大会講演要旨集  2011/03
• チョウザメのコラーゲンと海藻の色素！  [Not invited]

  星 恭兵, 富田友季穂, 古田智絵, 宮部好克, 水田卓志, 安倍健一郎, 菅野 岳, 岸村栄毅, 佐伯宏樹

  HAKODATEアカデミックリンク2010  2010/11
• サケ科魚類トリプシンの温度安定性と構造の関係  [Not invited]

  菅野 岳, 岸村栄毅, 清水健志, 安藤清一, 木村志津雄, 山羽悦郎, 佐伯宏樹

  平成22年度 日本水産学会秋季大会  2010/09
• Application of supercritical CO2 on preparation of starfish phospholipase A2  [Not invited]

  Byung-Soo Chun, Hiroto Kanzawa, Hideki Kishimura, Hiroki Saeki

  平成22年度 日本水産学会秋季大会  2010/09
• 数種ヒトデ由来コラーゲンペプチドの血糖値上昇抑制作用  [Not invited]

  水田卓志, 永井裕次郎, 岸村栄毅, 武田浩郁, 麻生真悟, 蛯谷幸司, 阪本正博, 北川雅彦, 菅野 岳, 佐伯宏樹

  第13回 マリンバイオテクノロジー学会大会 マリンバイオテクノロジー学会大会  2010/05
• チョウザメの骨・皮・鰭・鰾からコラーゲン・ペプチドの調製とその機能性  [Not invited]

  岸村栄毅, 水田卓志, 永井裕次郎, 足立伸次, 都木靖彰, 佐伯宏樹

  第13回 マリンバイオテクノロジー学会大会  2010/05
• サクラマス・トリプシンの温度安定性と一次構造  [Not invited]

  菅野 岳, 山口貴史, 岸村栄毅, 安藤清一, 木村志津雄, 山羽悦郎, 関崎春雄, 豊田栄子, 居弥口大介, 佐伯宏樹

  平成22年度 日本水産学会春季大会  2010/03
• ニッポンヒトデ・コラーゲンペプチドの血糖値上昇抑制作用  [Not invited]

  田卓志, 永井裕次郎, 岸村栄毅, 武田浩郁, 麻生真悟, 蛯谷幸司, 阪本正博, 北川雅彦, 佐伯宏樹

  平成22年度 日本水産学会春季大会  2010/03
• マヒトデ体壁からコラーゲンペプチドの調製とその血糖値上昇抑制作用  [Not invited]

  永井裕次郎, 岸村栄毅, 武田浩郁, 麻生真悟, 蛯谷幸司, 北川雅彦, 飯田訓之, 佐伯宏樹

  第43回 日本栄養・食糧学会東北支部大会  2009/11
• ヒトデ・イカゴロ・魚の内臓の利用  [Not invited]

  水田卓志, 永井裕次郎, 菅野 岳, 安倍健一郎, 松森圭佑, 岸村栄毅, 佐伯宏樹

  HAKODATEアカデミックリンク2009  2009/11
• ハクレン内臓由来トリプシンの精製と性質  [Not invited]

  安倍健一郎, 岸村栄毅, 袁 春紅, 菅野 岳, 遠藤 尚, 王 卓林, 今野久仁彦, 佐伯宏樹

  平成21年度 日本水産学会北海道支部大会  2009/11
• スルメイカ内臓由来トリプシンインヒビターの血糖値上昇抑制機構  [Not invited]

  永井裕次郎, 福盛田佳奈, 岸村栄毅, 佐伯宏樹

  平成21年度 日本水産学会北海道支部大会  2009/11
• カタクチイワシ・トリプシンの結晶化 およびX線結晶構造解析  [Not invited]

  菅野岳, 小林淳一, 岸村栄毅, 居弥口大介, 豊田栄子, 関崎春雄, 佐伯宏樹

  平成21年度 日本水産学会秋季大会  2009/09
• マヒトデコラーゲンペプチドの血糖値上昇抑制作用  [Not invited]

  永井裕次郎, 福盛田佳奈, 岸村栄毅, 武田浩郁, 麻生真悟, 蛯谷幸司, 北川雅彦, 飯田訓之, 佐伯宏樹

  平成21年度 日本水産学会秋季大会  2009/09
• カタクチイワシ・トリプシンの結晶化および立体構造解析  [Not invited]

  菅野 岳, 小林淳一, 岸村栄毅, 居弥口大介, 豊田栄子, 関崎春雄, 佐伯宏樹

  第12回 マリンバイオテクノロジー学会大会  2009/05
• プロテアーゼ消化性がシロザケ卵黄タンパク質のアレルゲン性に及ぼす影響  [Not invited]

  藤田真伍, 清水 裕, 渡辺一彦, 原 彰彦, 岸村栄毅, 佐伯宏樹

  平成21年度 日本水産学会春季大会  2009/03
• ガゴメ粘性多糖の物性におよぼす貯蔵条件の影響  [Not invited]

  西尾年弘, 片山 茂, 伊勢谷善助, 柳原雄一郎, 岸村栄毅, 佐伯宏樹

  平成21年度 日本水産学会春季大会  2009/03
• ホッケトリプシンの構造・機能解析  [Not invited]

  菅野 岳, 岸村 栄毅, 安藤清一, 佐伯宏樹

  平成21年度 日本水産学会春季大会  2009/03

Industrial Property Rights

• 特許第6418579号:ホタテ外套膜のタンパク質分解物を有用成分とする脂質吸収促進剤及びこれを含む飲食品    2018/10/19

  岸村栄毅, 武田浩郁, 秋野雅樹, 麻生真悟
• 特許第5199919号:ヒトデコラーゲンペプチドを有効成分とする血糖値上昇抑制剤およびヒトデコラーゲンペプチドの製造方法    2013/02/15

  麻生慎吾, 武田浩郁, 北川雅彦, 宮崎亜希子, 飯田訓之, 蛯谷幸司, 菅原 玲, 岸村栄毅, 佐伯宏樹  

  特願2009-048595
• 特開2012-229165:抗炎症剤および抗炎症剤の製造方法  2012/11/22

  佐伯宏樹, 岸村栄毅
• 特開2008-266208:糖尿病の予防及び/又は治療用組成物  2008/11/06

  岸村栄毅, 佐伯宏樹, 千葉 智  

  2007-111547
• 特開2008-125365:高純度プラスマローゲンの調製法  2008/06/05

  安藤清一, 岸村栄毅  

  特願2006-310364
• 特開2006-304666:トリプシン阻害活性を有する新規ポリペプチド  2006/11/09

  岸村栄毅, 林 賢治  

  2005-130157
• 特開2006-271332:ヒトデ由来新規トリプシンおよびその利用  2006/10/12

  岸村栄毅, 安藤清一, 林 賢治  

  2005-099448
• 特開2006-254876:L-トリプトファンの製造法  2006/09/28

  岸村栄毅, 林 賢治  

  2005-080616
• 特開2002-101882:「イトマキヒトデ由来ホスホリパーゼＡ２の遺伝子のクローン化と大腸菌による量産化」  2002/04/09

  岸村栄毅, 尾島孝男, 林 賢治, 西田清義  

  2000-294208

Awards & Honors

• 2024/03 北海道大学大学院水産科学研究院 佐々茂雄賞
   （指導学生の受賞） 

  受賞者: 山本竜矢
• 2022/11 キャンパス・コンソーシアム函館 ブースセッション『優秀賞』
   色落ちダルスに救済を! 

  受賞者: ○濵﨑海瑠, ○辰巳 幸彦, 岸村栄毅, 熊谷祐也
• 2022/03 北海道大学大学院水産科学研究院 佐々茂雄賞
   （指導学生の受賞） 

  受賞者: 西田有輝
• 2021/12 キャンパス・コンソーシアム函館 ステージセッション『優秀賞 (産学連携「クリエイティブネットワーク」賞) 』
   季節変動から紐解くダルス「MAAs」産業利用への試み 

  受賞者: ○前田侑也, ○山本竜矢, 熊谷祐也, 岸村栄毅
• 2021/12 キャンパス・コンソーシアム函館 ブースセッション『大賞』
   海藻のヌメヌメ成分「フコイダン」の最大Maxパワー力を生かすために 

  受賞者: ○松井亘, ○伊藤大翔, 熊谷祐也, 岸村栄毅
• 2021/03 北海道大学大学院水産科学研究院 佐々茂雄賞
   （指導学生の受賞） 

  受賞者: 小林真奈美
• 2020/11 キャンパス・コンソーシアム函館 ブースセッション『優秀賞』
   ミッション！低利用海藻に眠るお宝「MAAs」を可能な限り手に入れよ！ 

  受賞者: ○杉山佳奈海;西田有輝;熊谷祐也;岸村栄毅
• 2020/11 キャンパス・コンソーシアム函館 ブースセッション『優秀賞』
   ダルスで腸を元気にする！ 

  受賞者: ○吉田光里, 小林真奈美, 栗田大輝, 熊谷祐也, 岸村栄毅
• 2020/11 Food Society of Modern International Lifestyle Education Good Oral Award
   Efficient Extraction and Monthly Variation of Mycosporine-like Amino Acids from Red Alga Dulse in Japan 

  受賞者: ○Yuki Nishida;Yuya Kumagai;Shunta Michiba;Hajime Yasui;Hideki Kishimura
• 2019/11 キャンパス・コンソーシアム函館 ブース部門『大賞』
   海藻の秘密兵器！？「マイコスポリン様アミノ酸」 

  受賞者: ○西田有輝;熊谷祐也;岸村栄毅
• 2018/11 キャンパス・コンソーシアム函館 ブース部門『優秀賞』
   「絶対に捨てられない海藻がここにある」 

  受賞者: ○小林真奈美;山本陽平;熊谷祐也;岸村栄毅
• 2017/12 10th Joint International Symposium on Food Science and Technology among NUS, TUMSAT, HU, KU and UPM, 7-8 December 2017, National University of Singapore 『3rd Place of Oral Presentation Competition』
   "Collagen peptides prepared from sturgeon improve glucose tolerance in normal mice" 

  受賞者: ○Y. Sasaoka;H. Kishimura
• 2017/01 北海道大学 平成28年度 教育総長賞
   奨励賞 

  受賞者: 岸村栄毅
• 2015/11 キャンパス・コンソーシアム函館 ブース部門『優秀賞』
   「海の宝を探し出せ！―ダルスの健康機能―」 

  受賞者: ○佐藤直登;○北出裕実;岸村栄毅
• 2014/12 日本水産学会北海道支部 『最優秀学生講演賞』
   「次世代シーケンサによるツルシラモ葉緑体DNAの分析」 

  受賞者: 熊谷侑貴;宮部好克;清水健志;足立伸次;安井 肇;岸村栄毅
• 2009/11 キャンパス・コンソーシアム函館 ブースセッション『優秀賞』
   「ヒトデ・イカゴロ・魚の内臓の利用」 

  受賞者: 水田卓志;松森圭佑;安倍健一郎;永井裕次郎;菅野岳;岸村栄毅;佐伯宏樹

Research Grants & Projects

• LASBOSカード、Tシャツ企画に対する支援

  株式会社大野冷機：R4年度 バランスドオーシャン事業に対する支援

  Date (from‐to) : 2022/10 -2023/11
• ホタテガイ外套膜ペプチドの定量技術に関する研究

  北海道立総合研究機構：令和4年度（2022年度）共同研究

  Date (from‐to) : 2022/11 -2023/03 

  Author : 岸村栄毅, 熊谷裕也
• 海洋深層水を活用した海藻スプラウトや有用海藻の陸上栽培技術の実用化

  公益財団法人北海道科学技術振興センター：研究成果展開の側面支援

  Date (from‐to) : 2022/10 -2023/03 

  Author : 川越 力, 木下康宣, 岸村栄毅, 熊谷祐也
• 生活習慣病の予防を実践できる食品因子の解明に関する研究

  JSPS：2022年度 外国人招へい研究者（長期）

  Date (from‐to) : 2022/04 -2023/03 

  Author : 岸村栄毅,熊谷祐也
• ホタテガイ外套膜ペプチドの定量技術に関する研究

  北海道立総合研究機構：令和3年度（2021年度）共同研究

  Date (from‐to) : 2021/09 -2022/03 

  Author : 岸村栄毅, 熊谷祐也
• 海洋深層水を活用した海藻スプラウトや有用海藻の陸上栽培技術の実用化

  公益財団法人北海道科学技術振興センター：2021年度 研究開発助成事業

  Date (from‐to) : 2021/08 -2022/03 

  Author : 川越 力, 水田浩之, 宇治利樹, 高野智宏, 木村和世, 平井輝孝, 岸村栄毅, 谷祐也, 木下康宣, 鳥海 滋
• 北方系紅藻の陸上栽培に関する研究事業

  公益財団法人南北海道学術振興財団：助成事業

  Date (from‐to) : 2021/04 -2022/03 

  Author : 熊谷祐也, 岸村栄毅, 川越 力, 木下康宣, 鳥海 滋
• 塩ストレスによる紅藻類の食味改善物質の同定と機構に関する研究

  公益財団法人ソルト・サイエンス研究財団：研究助成（一般公募研究）

  Date (from‐to) : 2021/04 -2022/03 

  Author : 熊谷祐也, 岸村栄毅, 川越 力
• 陸上栽培による 海藻 の次世代タンパク質化および高機能 性 評価システムの構築

  JST：A-STEP 令和2年度追加募集（トライアウトタイプ）

  Date (from‐to) : 2021/03 -2022/03 

  Author : 熊谷祐也, 川越 力, 岸村栄毅, 木下康宣, 鳥海 滋
• ホタテガイペプチドを用いたサケ科魚類養殖魚の質的向上に関する研究

  独立行政法人 北海道立総合研究機構：令和2年度（2020年度）共同研究

  Date (from‐to) : 2020/08 -2021/03 

  Author : 岸村栄毅, 熊谷祐也
• パエニバチルス酵素による紅藻ダルス・キシロオリゴ糖の調製とその腸内菌叢改善作用

  日本学術振興会：令和2年度（2020年度)）科研費 新学術領域研究「先進ゲノム支援」

  Date (from‐to) : 2020/04 -2021/03 

  Author : 岸村栄毅, 熊谷祐也
• 紫外線防御物質に着目したナマコ種苗の育成および飼料改善

  北水協会：令和２年度（2020年度）研究助成事業

  Date (from‐to) : 2020/04 -2021/03 

  Author : 熊谷祐也, 岸村栄毅
• HU-NUS summer course “Seafood supply chains in Singapore and Japan”

  北海道大学：令和元年度（2019年度）海外ラーニング・サテライト事業

  Date (from‐to) : 2019/04 -2021/03 

  Author : 岸村栄毅, ジョンバウアー, 熊谷祐也
• パエニバチルス酵素による紅藻ダルス・キシロオリゴ糖の調製とその腸内菌叢改善作用

  日本学術振興会：平成30年度（2018年度）科研費 基盤研究(C)(一般）

  Date (from‐to) : 2018/04 -2021/03 

  Author : 岸村栄毅, 尾島孝男
• ホタテガイペプチドを用いたサケ科魚類養殖魚の質的向上に関する研究

  地方独立行政法人 北海道立総合研究機構：令和元年度（2019年度）共同研究

  Date (from‐to) : 2019/08 -2020/03 

  Author : 岸村栄毅, 熊谷祐也
• 北方系海藻の通年収穫を目的とした陸上栽培技術の開発

  ノーステック財団：令和元年度（2019年度）【第26回】「研究開発助成事業」 スタートアップ研究補助金

  Date (from‐to) : 2019/08 -2020/03 

  Author : 川越 力, 水田浩之, 宇治利樹, 木下康宣, 岸村栄毅, 熊谷祐也
• 認知症予防の「二つの作用点」に「一つの食材」でアプローチする

  ノーステック財団：令和元年度（2019年度）「札幌ライフサイエンス産業活性化事業」 事業化支援補助金

  Date (from‐to) : 2019/07 -2020/03 

  Author : 岸村栄毅, 熊谷祐也, 川越力, 木下康宣, 細川雅史
• 海洋深層水を用いた北方系未利用紅藻「ダルス」の周年栽培技術開発

  北海道大学 ロバスト農林水産工学国際連携研究教育拠点：令和元年度（2019年度）ロバスト農林水産工学研究プログラム

  Date (from‐to) : 2019/05 -2020/03 

  Author : 岸村栄毅
• Study on photosynthesis mechanism of the Rhodophyta

  Massachusetts Institute of Technology：令和元年度（2019年度）共同研究

  Date (from‐to) : 2020/01 

  Author : Hideki Kishimura, Yuya Kumagai
• ホタテガイペプチドを用いたサケ科魚類増養殖魚の質的向上に関する研究

  地方独立行政法人北海道立総合研究機構：平成30年度（2018年度）共同研究

  Date (from‐to) : 2018/08 -2019/03 

  Author : 武田浩郁, 岸村栄毅
• HU-NUS summer course “Seafood supply chains in Singapore and Japan”

  北海道大学：平成29年度（2017年度）海外ラーニング・サテライト事業

  Date (from‐to) : 2017/04 -2019/03 

  Author : 都木靖彰, ジョンバウアー, 岸村栄毅
• 未利用資源である磯焼けウニの食品としての健康機能解明と蓄養技術開発による商品化

  農林水産省：平成27年度（2015年度）農林水産業・食品産業科学技術研究推進事業【発展融合ステージ】

  Date (from‐to) : 2015/07 -2018/03 

  Author : 浦 和寛
• 北方圏紅藻類の資源開発とその健康機能・素材特性を活かした 次世代型機能性食品の創出

  農林水産省：平成27年度（2015年度）農林水産業・食品産業科学技術研究推進事業【発展融合ステージ】

  Date (from‐to) : 2015/07 -2018/03 

  Author : 木曽良信
• HU-NUS summer course “Seafood supply chains in Singapore and Japan”

  北海道大学：平成27年度（2015年度）海外ラーニング・サテライト事業

  Date (from‐to) : 2015/04 -2017/03 

  Author : 都木靖彰, ジョンバウアー, 岸村栄毅
• 紅藻由来フィコエリスリンの脳機能改善作用とそのメカニズムの解明

  日本学術振興会：平成25年度（2013年度）科研費 基盤研究（B）（一般）

  Date (from‐to) : 2013/04 -2017/03 

  Author : 岸村栄毅, 足立亨介
• 「津軽海峡広域圏」としての発展を視野に入れたブルー・イノベーションによる国際産業創生 拠点の実現

  科学技術振興機構：平成26年度（2014年度）我が国の未来を拓く地域の実現に関する調査研究

  Date (from‐to) : 2014/11 -2015/03 

  Author : 山口佳三
• 紅藻ダルス属のレトルト食品素材としての利用可能性に係るニーズ調査と安全性の検証

  農林水産省食料産業局：平成26年度（2014年度）緑と水の環境技術革命プロジェクト 新需要創造フロンティア育成事業

  Date (from‐to) : 2014/04 -2015/03 

  Author : 木下康宣
• 脂質吸収を促進するホタテガイペプチドによる高齢者向け食品素材の開発

  公益財団法人 東洋食品研究所：平成25年度（2013年度）研究助成

  Date (from‐to) : 2014/04 -2015/03 

  Author : 武田浩郁, 岸村栄毅
• ホタテ外套膜のタンパク質分解物を有効成分とする脂質吸収促進剤及びこれを含む飲食品

  北海道大学：平成25年度（2013年度）実証研究推進助成事業（HOPPERs事業）

  Date (from‐to) : 2013/11 -2014/03 

  Author : 岸村栄毅, 武田浩郁
• 水産物由来ムチンの物性解析と応用検討

  株式会社 高研：平成25年度（2013年度） 共同研究

  Date (from‐to) : 2013/07 -2014/03 

  Author : 岸村栄毅
• アメフラシが食餌紅藻由来の色素タンパク質から紫色の忌避煙幕を作る経路を探る

  公益財団法人 秋山記念生命科学振興財団：2013年度 研究助成 一般

  Date (from‐to) : 2013/04 -2014/03 

  Author : 岸村栄毅
• 函館マリンバイオクラスター

  文部科学省：平成21年度 グローバル拠点育成型知的クラスター創成事業

  Date (from‐to) : 2009/04 -2014/03 

  Author : 高野洋藏
• 地域再生人材創出拠点の形成

  文部科学省：平成21年度 科学技術振興調整費

  Date (from‐to) : 2009/04 -2014/03 

  Author : 佐伯 浩
• 未利用水産生物・水産廃棄物から有用酵素およびペプチドの探索とその利用

  公益財団法人北水協会：平成22年度 試験研究費補助金

  Date (from‐to) : 2010/04 -2013/03 

  Author : 岸村栄毅
• ホタテガイ外套膜由来ペプチドを活用した脂溶性成分の吸収促進機能の検証

  科学技術振興機構：平成23年度 A-STEPフィージビリティスタディステージ 探索タイプ

  Date (from‐to) : 2011/08 -2012/07 

  Author : 武田浩郁
• コンビナート型ヒトデ・トータル利用システムの開発

  農林水産省：平成20年度 新たな農林水産政策を推進する実用技術開発事業

  Date (from‐to) : 2008/04 -2011/03 

  Author : 飯田訓之
• Proteases and protease-activated receptors in skin reaction to seafood

  ノルウェー：Grants-in-Aid for Scientific Research in Norway

  Date (from‐to) : 2009/09 -2010/08 

  Author : Berit, Bang
• 水産物由来の血糖値上昇抑制剤の開発と応用

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  Date (from‐to) : 2009/04 -2010/03 

  Author : 岸村栄毅
• 棘皮動物由来ホスホリパーゼA2の立体構造と基質特異性との関係

  日本学術振興会：平成19年度（2007年度）科研費 基盤研究（C）（一般）

  Date (from‐to) : 2007/04 -2010/03 

  Author : 岸村栄毅
• イカ類内臓抽出物の抗糖尿病作用

  日本水産株式会社：平成19年度 共同研究

  Date (from‐to) : 2007/04 -2008/03 

  Author : 岸村栄毅
• 魚卵アレルギーにおけるアレルゲンの解明と魚種間の免疫学的交差性の調査

  日本学術振興会：平成18年度（2006年度）科研費 基盤研究（C）（一般）

  Date (from‐to) : 2006/04 -2008/03 

  Author : 佐伯宏樹
• イカ類内臓由来のトリプシンインヒビターの探索とその血糖値低下作用に関する研究

  日本水産株式会社：平成18年度 ニッスイ研究ファンド

  Date (from‐to) : 2006/04 -2007/03 

  Author : 岸村栄毅
• 海産無脊椎動物由来ホスホリパーゼA2の基質特異性発現機構の解明

  日本学術振興会：平成15年度（2003年度）科研費 基盤研究（C）（一般）

  Date (from‐to) : 2003/04 -2007/03 

  Author : 岸村栄毅
• 水産無脊椎動物セルラーゼの一次構造と起源に関する研究

  日本学術振興会：平成15年度（2003年度）科研費 基盤研究（B）（一般）

  Date (from‐to) : 2003/04 -2006/03 

  Author : 尾島孝男
• 軟体動物アルギン酸リアーゼの起源と遺伝子構造に関する研究

  日本学術振興会：平成15年度（2003年度）科研費（萌芽研究）

  Date (from‐to) : 2003/04 -2005/03 

  Author : 尾島孝男
• Characteristics and Utilization of Trypsin from The Fish Viscera

  International Collaboration

  Date (from‐to) : 2003

Educational Activities

Teaching Experience

Committee Membership

• 2021/12 - Today   MDPI   Marine Drugs : Guest Editor of the Special Issue "Advances in Oligosaccharides and Polysaccharide Modifications in Marine Bioresources"
• 2020/03 - Today   MDPI   Marine Drugs (ISSN 1660-3397) : Editorial Board
• 2020/07 -2022/03   Marine Drugs (ISSN 1660-3397)   Guest Editor of the Special Issue "Bioactive Peptides from Marine By-Products and Underused Marine Organisms"

Social Contribution

Social Contribution

Social Contribution

• 高校生に対する出前講師

  Date (from-to) : 2022/07/29-2022/07/29

  Role : Lecturer

  Sponser, Organizer, Publisher  : 函館白稜高校

  Event, Program, Title : 函館白稜高校 理科研究部部員に対する出前講師
• 函館の学生ら研究発表「アカデミックリンク」

  Date (from-to) : 2021/12/24

  Role : Coverage cooperation

  Sponser, Organizer, Publisher  : 北海道新聞社

  Event, Program, Title : 北海道新聞 みなみ風
• 高校生に対する出前講師

  Date (from-to) : 2021/07/02-2021/07/02

  Role : Lecturer

  Sponser, Organizer, Publisher  : 函館白稜高校

  Event, Program, Title : 函館白稜高校 函館白稜高校 理科研究部部員に対する出前講師
• Certificate of Reviewing

  Date (from-to) : 2021/01/28

  Role : Organizing member

  Sponser, Organizer, Publisher  : ELSEVIER

  Event, Program, Title : Food Hydrocolloids
• 海藻スプラウト：海藻の陸上養殖プロジェクト

  Date (from-to) : 2020/11/05-2020/11/06

  Role : Others

  Sponser, Organizer, Publisher  : 経済産業省北海道経済産業局、北海道、札幌市、北海道経済連合会、等

  Event, Program, Title : 2020北海道ビジネスEXPO
• 紅藻色素タンパク質フィコエリスリンの生理活性機能

  Date (from-to) : 2020/10

  Role : Contribution

  Sponser, Organizer, Publisher  : 海藻活用研究会

  Event, Program, Title : 海藻活用研究と商品開発
• 北海道大学ーシンガポール国立大学 サマーコース〜日本とシンガポールにおける水産物供給体制の比較〜

  Date (from-to) : 2020/06-2020/06

  Role : Organizing member

  Sponser, Organizer, Publisher  : 北海道大学 教育改革室

  Event, Program, Title : 北海道大学における教育方法のグッド・プラクティス「海外ラーニングサテライト」
• 青年部コンクール審査員

  Date (from-to) : 2019/11/06-2019/11/06

  Role : Organizing member

  Sponser, Organizer, Publisher  : （社）全日本司厨士協会函館支部・日本中国料理協会函館支部

  Event, Program, Title : 第34回 郷土料理研究会
• 海藻の光る成分を調べてみよう！

  Date (from-to) : 2019/08/05

  Role : Lecturer

  Sponser, Organizer, Publisher  : 北海道大学大学院水産科学研究院

  Event, Program, Title : 2019 北海道大学水産学部オープンキャンパス
• Reviewer Certificate

  Date (from-to) : 2019/06/14

  Role : Organizing member

  Sponser, Organizer, Publisher  : Wiley

  Event, Program, Title : Journal of Food Biochemistry
• 就活会議

  Date (from-to) : 2019

  Role : Others

  Sponser, Organizer, Publisher  : 新田ゼラチン

  Event, Program, Title : 本選考通過エントリーシート
• 水圏生命科学 研究をリードする大学

  Date (from-to) : 2019

  Role : Others

  Sponser, Organizer, Publisher  : 河合塾

  Event, Program, Title : みらいぶっく 学問・大学なび
• 取組24＞ラーニング・サテライト

  Date (from-to) : 2018/11

  Role : Organizing member

  Sponser, Organizer, Publisher  : 北海道大学学務部

  Event, Program, Title : 北海道大学の教育改革・学生支援に関する取組
• ダルスの魅力 広めたい

  Date (from-to) : 2018/10/26

  Role : Others

  Sponser, Organizer, Publisher  : 北海道新聞

  Event, Program, Title : みなみ風
• 「ダルス」資源の活用と展望

  Date (from-to) : 2018/09/04

  Role : Lecturer

  Sponser, Organizer, Publisher  : JICA北海道

  Event, Program, Title : 2018年度 水産資源の持続的利用とバリューチェーン開発
• 海藻の成分を調べてみよう

  Date (from-to) : 2018/08/06-2018/08/06

  Role : Lecturer

  Sponser, Organizer, Publisher  : 北海道大学

  Event, Program, Title : 2018 北海道大学水産学部オープンキャンパス
• 北海道大学ーシンガポール国立大学 サマーコース〜日本とシンガポールにおける水産物供給体制の比較〜

  Date (from-to) : 2018/06-2018/06

  Role : Organizing member

  Sponser, Organizer, Publisher  : 北海道大学 教育改革室

  Event, Program, Title : 北海道大学における教育方法のグッド・プラクティス「海外ラーニングサテライト」
• Reviewer Certificate

  Date (from-to) : 2018/04/30

  Role : Organizing member

  Sponser, Organizer, Publisher  : Wiley

  Event, Program, Title : Journal of Food Biochemistry
• 「ダルス」資源の活用と展望

  Date (from-to) : 2017/09/05

  Role : Lecturer

  Sponser, Organizer, Publisher  : JICA北海道

  Event, Program, Title : 2017年度 水産資源の持続的利用とバリューチェーン開発
• 紅藻フィコビリタンパク質のヘルスベネフィット

  Date (from-to) : 2015/03

  Role : Informant

  Sponser, Organizer, Publisher  : 北海道大学 産学連携本部

  Event, Program, Title : 北海道大学研究シーズ集Vol.2
• 学生が研究成果をアピール HAKODATEアカデミックリンック

  Date (from-to) : 2014/11/09

  Role : Others

  Sponser, Organizer, Publisher  : 函館新聞社

  Event, Program, Title : 函館新聞
• 高齢者の脂質欠乏に着目 ホタテガイ由来脂質吸収促進ペプチド開発

  Date (from-to) : 2014/04/16

  Role : Others

  Sponser, Organizer, Publisher  : 食品科学新聞社

  Event, Program, Title : Health Food Journal
• 海洋資源どう生かす

  Date (from-to) : 2012/08/03

  Role : Others

  Sponser, Organizer, Publisher  : 北海道新聞社

  Event, Program, Title : 北海道新聞
• マリンバイオフォーラム 最新の水産研究成果報告 『紅藻ダルス』健康機能など

  Date (from-to) : 2012/07/24

  Role : Others

  Sponser, Organizer, Publisher  : 函館新聞社

  Event, Program, Title : 函館新聞
• ヒトデが犬を救う？

  Date (from-to) : 2011/11/16

  Role : Others

  Sponser, Organizer, Publisher  : NHK

  Event, Program, Title : 『ネットワークニュス北海道』,『おはよう日本』,『海外ニュース』
• ヒトデからマリンコラーゲンを作ってみよう

  Date (from-to) : 2009/08/01

  Role : Lecturer

  Sponser, Organizer, Publisher  : 北海道大学

  Event, Program, Title : 2009 北海道大学水産学部オープンキャンパス
• 水産食品と酵素

  Date (from-to) : 2008/02/16

  Role : Lecturer

  Sponser, Organizer, Publisher  : 道南薫製クラブ

  Event, Program, Title : 道南薫製クラブ
• 水産廃棄物由来の有用成分

  Date (from-to) : 2007/01/15

  Role : Lecturer

  Sponser, Organizer, Publisher  : 函館水産研修会

  Event, Program, Title : 函館水産研修会

Media Coverage

• 低利用資源の紅藻"ダルス"から紫外線防御物質MAAs調製法を確立 ～効率的な調製法を検討、異なる条件で含有量と組成を比較～

  Date : 2023/10/03

  Writer: Myself

  Publisher, broadcasting station: 北海道大学

  Program, newspaper magazine: プレスリリース

  北海道大学ホームページ Internet
• NHK総合「あさイチ」にて岸村栄毅教授のコメントが放送予定です【10月30日(月)】

  Date : 2023/10

  Publisher, broadcasting station: 北海道大学大学院水産科学研究院

  Program, newspaper magazine: 北海道大学大学院水産科学研究院ホームページ

  お知らせ
• こんな効果があったのか!?魅惑の海藻パワー

  Date : 2023/10

  Writer: Myself

  Publisher, broadcasting station: NHK

  Program, newspaper magazine: あさイチ

  こんな効果があったのか!?魅惑の海藻パワー Media report
• 特色ある研究

  Date : 2023/08

  Writer: Myself

  Publisher, broadcasting station: 北海道大学 大学院水産科学研究院

  Program, newspaper magazine: 令和5年度 北海道大学 水産学部 概要

  Pr
• 「ダルスの 赤い色のタンパク質」に関するイベント紹介

  Date : 2023/07

  Publisher, broadcasting station: 北海道大学

  Program, newspaper magazine: 北海道大学のLASBOS

  岸村 栄毅 KISHIMURA Hideki、ダルスのタンパク質成分について Internet
• 海洋深層水を用いた北方系未利用紅藻「ダルス」の周年栽培技術開

  Date : 2023/04

  Writer: Myself

  Publisher, broadcasting station: 北海道大学

  Program, newspaper magazine: ロバスト農林水産工学国際連携研究教畜拠点

  https://seeds.mcip.hokudai.ac.jp/jp/view/85/ Pr
• 特色ある研究紹介

  Date : 2022/08

  Writer: Myself

  Publisher, broadcasting station: 北海道大学 大学院水産科学研究院

  Program, newspaper magazine: 令和4年度 北海道大学 水産学部 概要

  Pr
• 理科研究部『北海道大学 岸村 栄毅 教授のご講演』

  Date : 2022/08

  Writer: Other than myself

  Publisher, broadcasting station: 函館大学付属柏稜高等学校

  Program, newspaper magazine: 函館大学付属柏稜高等学校 ホームページ

  函館大学付属柏稜高等学校 ホームページ トップページ Internet
• Health Benefit of Red Algae Phycobiliprotein

  Date : 2022/06

  Publisher, broadcasting station: Hokkaido University

  Program, newspaper magazine: Hokkaido University, Research Profiles

  https://seeds.mcip.hokudai.ac.jp/en/view/85/kishimura%20hideki Internet
• 紅藻フィコビリタンパク質のヘルスベネフィット

  Date : 2022/03

  Writer: Myself

  Publisher, broadcasting station: 北海道大学産学・地域協働推進機構

  Program, newspaper magazine: 北海道大学研究シーズ集Vol.9

  Pr
• 函館の学生ら研究発表「アカデミックリンク」

  Date : 2021/12

  Writer: Other than myself

  Program, newspaper magazine: 北海道新聞

  Paper
• アカデミックリンク2021 北海道大学水産学部から3チームが受賞！

  Date : 2021/12

  Writer: Other than myself

  Publisher, broadcasting station: 北海道大学大学院水産科学研究院

  Program, newspaper magazine: 大学院水産科学研究院ホームページ

  お知らせ Internet
• 特色ある研究紹介

  Date : 2021/08

  Writer: Myself

  Publisher, broadcasting station: 北海道大学 大学院水産科学研究院

  Program, newspaper magazine: 令和3年度 北海道大学 水産学部 概要

  Pr
• 「北海道大学 オンライン講演」

  Date : 2021/07

  Writer: Other than myself

  Publisher, broadcasting station: 函館大学付属柏稜高等学校

  Program, newspaper magazine: 函館大学付属柏稜高等学校 ホームページ

  函館大学付属柏稜高等学校 ホームページ トップページ Internet
• 紅藻フィコビリタンパク質のヘルスベネフィット

  Date : 2021/03

  Writer: Myself

  Publisher, broadcasting station: 北海道大学産学・地域協働推進機構

  Program, newspaper magazine: 北海道大学研究シーズ集Vol.8

  Pr
• 紅藻中の健康機能成分の探索

  Date : 2021/01

  Publisher, broadcasting station: 北海道大学水産科学研究院 バランスドオーシャン運用部

  Program, newspaper magazine: Twitter

  https://twitter.com/FNinKochi/status/1351355329309601794 Internet
• 【教材】比重計を用いたメタノール濃度の算出

  Date : 2020/10

  Publisher, broadcasting station: 北海道大学大学院水産科学研究院 バランスドオーシャン運用部

  Program, newspaper magazine: YouTube

  https://www.youtube.com/watch?v=vrOSgYjY59Q&list=PLUEc4MwRlJfhoXC-P9VSM3R4IwfLD6oSj&index=8&t=7s Internet
• 【教材】連続蒸留装置 安全に扱うために

  Date : 2020/10

  Publisher, broadcasting station: 北海道大学大学院水産科学研究院 バランスドオーシャン運用部

  Program, newspaper magazine: YouTube

  https://www.youtube.com/watch?v=6F5TcfRhd08&t=2s Internet
• 【教材】連続蒸留装置 管理盤

  Date : 2020/10

  Publisher, broadcasting station: 北海道大学大学院水産科学研究院 バランスドオーシャン運用部

  Program, newspaper magazine: YouTube

  https://www.youtube.com/watch?v=RpEone1MSUw&t=3s Internet
• 【教材】連続蒸留装置 冷却水の流れ

  Date : 2020/10

  Publisher, broadcasting station: 北海道大学大学院水産科学研究院 バランスドオーシャン運用部

  Program, newspaper magazine: YouTube

  https://www.youtube.com/watch?v=QRWrQWrUaa8&t=4s Internet
• 【教材】連続蒸留装置 蒸気の流れ

  Date : 2020/10

  Publisher, broadcasting station: 北海道大学大学院水産科学研究院 バランスドオーシャン運用部

  Program, newspaper magazine: YouTube

  https://www.youtube.com/watch?v=_xziqXiOrAw&t=2s Internet
• 【教材】連続蒸留装置 原料の流れ

  Date : 2020/10

  Publisher, broadcasting station: 北海道大学大学院水産科学研究院 バランスドオーシャン運用部

  Program, newspaper magazine: YouTube

  https://www.youtube.com/watch?v=OZeFYF0-nhk&t=2s Internet
• 【教材】二段圧縮冷凍機

  Date : 2020/10

  Publisher, broadcasting station: 北海道大学大学院水産科学研究院 バランスドオーシャン運用部

  Program, newspaper magazine: YouTube

  https://www.youtube.com/watch?v=HcBOou5XXbU&t=506s Internet
• 【教材】一段圧縮冷凍機

  Date : 2020/10

  Publisher, broadcasting station: 北海道大学大学院水産科学研究院 バランスドオーシャン運用部

  Program, newspaper magazine: YouTube

  https://www.youtube.com/watch?v=Z87Bg0TdxGw Internet
• バランスドオーシャン事業による『LASBOS Moodle』の一般公開：全学教育科目の授業紹介（魚をたべる）

  Date : 2020/10

  Publisher, broadcasting station: 北海道大学

  Program, newspaper magazine: 北大時報

  部局ニュース（20ページ） Pr
• 特色ある研究紹介

  Date : 2020/08

  Writer: Myself

  Publisher, broadcasting station: 北海道大学 大学院水産科学研究院

  Program, newspaper magazine: 令和2年度 北海道大学 水産学部 概要

  Pr
• 紅藻フィコビリタンパク質のヘルスベネフィット

  Date : 2020/03

  Writer: Myself

  Publisher, broadcasting station: 北海道大学産学・地域協働推進機構

  Program, newspaper magazine: 北海道大学研究シーズ集Vol.7

  Pr
• 紅藻類ダルスのフィコエリスリンに脳機能改善効果！コンブ養殖の厄介者を新たな資源として活用 北大

  Date : 2019/11

  Publisher, broadcasting station: (株)ziten

  Program, newspaper magazine: 日本の身土不二

  Internet
• 特色ある研究紹介

  Date : 2019/08

  Writer: Myself

  Publisher, broadcasting station: 北海道大学 大学院水産科学研究院

  Program, newspaper magazine: 令和1年度 北海道大学 水産学部 概要

  Pr
• 紅藻フィコビリタンパク質のヘルスベネフィット

  Date : 2019/03

  Publisher, broadcasting station: 北海道大学産学・地域協働推進機構

  Program, newspaper magazine: 北海道大学研究シーズ集Vol.6

  Pr
• 特色ある研究紹介

  Date : 2018/08

  Publisher, broadcasting station: 北海道大学 大学院水産科学研究院

  Program, newspaper magazine: 平成30年度 北海道大学 水産学部 概要

  Pr
• 紅藻フィコビリタンパク質のヘルスベネフィット

  Date : 2018/03

  Publisher, broadcasting station: 北海道大学産学・地域協働推進機構

  Program, newspaper magazine: 北海道大学研究シーズ集Vol.5

  Pr
• 紅藻フィコビリタンパク質のヘルスベネフィット

  Date : 2017/07/10

  Publisher, broadcasting station: 筑波大学 産学・地域恊働推進機構

  Program, newspaper magazine: 産学連携プラットフォーム

  Pr
• 特色ある研究紹介

  Date : 2017/04

  Publisher, broadcasting station: 北海道大学 大学院水産科学研究院

  Program, newspaper magazine: 平成29年度 北海道大学 水産学部 概要

  Pr
• 紅藻フィコビリタンパク質のヘルスベネフィット

  Date : 2017/03

  Publisher, broadcasting station: 北海道大学 産学連携本部

  Program, newspaper magazine: 北海道大学研究シーズ集Vol.4

  Pr
• 特色ある研究紹介

  Date : 2016/04

  Publisher, broadcasting station: 北海道大学

  Program, newspaper magazine: 平成28年度 北海道大学 水産学部 概要

  Pr
• 紅藻フィコビリタンパク質のヘルスベネフィット

  Date : 2016/03

  Publisher, broadcasting station: 北海道大学 産学連携本部

  Program, newspaper magazine: 北海道大学研究シーズ集Vol.3

  Pr
• ダルスのタンパク質成分について

  Date : 2015/09/04

  Publisher, broadcasting station: 北水同窓会

  Program, newspaper magazine: 親潮 第305号

  Pr
• 脇役の海産物にスポットライトをあてる

  Date : 2015/06/01

  Publisher, broadcasting station: リバネス出版

  Program, newspaper magazine: someone

  Paper
• ダルスの利用

  Date : 2015/04/02

  Publisher, broadcasting station: NHK函館放送局

  Program, newspaper magazine: 「ほっとニュース北海道」「おうはよう日本」「つながる@道南」

  Media report
• 特色ある研究紹介

  Date : 2015/04

  Publisher, broadcasting station: 北海道大学 大学院水産科学研究院

  Program, newspaper magazine: 平成27年度 北海道大学 水産学部 概要

  Pr
• 研究最前線

  Date : 2015/02/07

  Publisher, broadcasting station: 北海道新聞社

  Program, newspaper magazine: 北海道新聞

  Paper
• 北大生がホタテのミミなどの健康機能研究

  Date : 2014/11/24

  Publisher, broadcasting station: 函館新聞社

  Program, newspaper magazine: 函館新聞

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• Toward sustainable use of marine resources

  Date : 2014/10/29

  Publisher, broadcasting station: 北海道大学 産学連携本部

  Program, newspaper magazine: 平成27年度 産学連携の手引き 技術シーズ紹介（北海道大学）

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• 私の研究人生：すべては偶然の重なり

  Date : 2014/04/03

  Publisher, broadcasting station: 公益財団法人 秋山記念生命科学振興財団

  Program, newspaper magazine: 平成25年度 秋山財団年報

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• 特色ある研究紹介

  Date : 2014/04/01

  Publisher, broadcasting station: 北海道大学 大学院水産科学研究院

  Program, newspaper magazine: 平成26年度 北海道大学 水産学部 概要

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• 紅藻フィコビリタンパク質のヘルスベネフィット

  Date : 2014/01/10

  Publisher, broadcasting station: 北海道大学 産学連携本部

  Program, newspaper magazine: 北海道大学研究シーズ集2014 産業イノベーションを担う北大の最先端研究

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• 水産資源の持続的利用をめざして

  Date : 2013/04/01

  Publisher, broadcasting station: 北海道大学 産学連携本部

  Program, newspaper magazine: 平成25年度 産学連携の手引き 技術シーズ紹介（北海道大学）

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• 血圧上昇酵素を抑制 紅藻『ダルス』

  Date : 2012/08/05

  Publisher, broadcasting station: 函館新聞社

  Program, newspaper magazine: 函館新聞

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• ヒトデをペットの健康食に 道立水産試験場で研究

  Date : 2009/12/30

  Publisher, broadcasting station: 時事通信社

  Program, newspaper magazine: 各社新聞記事

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• イカゴロ、ヒトデ、魚類内臓

  Date : 2008/04/01

  Publisher, broadcasting station: 経済産業省北海道経済産業局

  Program, newspaper magazine: 北海道 第一次産業由来 副産物 廃棄物 利活用GUIDE2008

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