Researcher Profile and Settings

Master

Affiliation (Master)

• Research Faculty of Agriculture　Fundamental AgriScience Research　Animal Science

Affiliation (Master)

• Research Faculty of Agriculture　Fundamental AgriScience Research　Animal Science

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Profile and Settings

Degree

• Ph.D（Hokkaido University）

Profile and Settings

• Name (Japanese)

  Hayakawa

• Name (Kana)

  Toru

• Name

  201201021252032780

Achievement

Research Interests

• imidazole compound   thick filament   protein solubilization   skeletal muscle   meat   myosin   

Research Areas

• Life sciences / Animal production science / Meat Science

Research Experience

• 2016/10 - Today Hokkaido University Faculty of Agriculture, Department of Animal Science
• 2012/10 - 2016/10 Obihiro University of Agriculture and Veterinary Medicine Department of Animal and Food Hygiene
• 2011/04 - 2012/09 University of Massachusetts Medical school Research scholar
• 2009/04 - 2011/03 日本学術振興会 特別研究員（DC2）
• 2005/04 - 2008/03 Nippon Meat Packers Inc. R&D center

Education

• 2008/04 - 2011/03  Hokkaido University  Graduate school of Agriculture
• 2003/04 - 2005/03  北海道大学大学院
• 1999/04 - 2003/03  Hokkaido University  Faculty of Agriculture  Department of Animal Science

Awards

• 2009/03 日本畜産学会 日本畜産学会第110回大会優秀発表賞
   L-ヒスチジンを含む低イオン強度溶液へのミオシンの溶解機構の解明 

  受賞者: 早川 徹

Published Papers

• Identification of cheese rancidity-related lipases in Aspergillus oryzae AHU 7139.

  Napaporn Chintagavongse, Haruto Kumura, Toru Hayakawa, Jun-Ichi Wakamatsu, Koichi Tamano

  Journal of bioscience and bioengineering 2024/03/01 

  The adjunct product with enzymatic activity from Aspergillus oryzae is beneficial for flavor enrichment in the ripened cheese. However, an excessive lipolytic reaction leads to the release of volatile free fatty acids. Accordingly, a strong off-flavor (i.e., rancidity) has been detected when A. oryzae AHU 7139 is used. To identify the rancidity-related lipase from this strain, we evaluated the substrate specificity and lipase distribution using five mutants cultured on a whey-based solid medium under different initial pH conditions. The results showed a higher diacylglycerol lipase activity than triacylglycerol lipase activity. Moreover, an initial pH of 6.5 for the culture resulted in higher lipolytic activity than a pH of 4.0, and most of the activity was found in the extracellular fraction. Based on the gene expression analysis by real-time polymerase chain reaction and location and substrate specificity, five genes (No. 1, No. 19, mdlB, tglA, and cutL) were selected among 25 annotated lipase genes to identify the respective knockout strains. Because ΔtglA and ΔmdlB showed an outstanding involvement in the release of free fatty acids, these strains were applied to in vitro cheese curd experiments. In conclusion, we posit that triacylglycerol lipase (TglA) plays a key role as the trigger of rancidity and the resulting diglycerides have to be exposed to diacylglycerol lipase (MdlB) to stimulate rancidity in cheese made with A. oryzae AHU 7139. This finding could help screen suitable A.oryzae strains as cheese adjuncts to prevent the generation of the rancid-off flavor.
• Water extractability of the zinc protoporphyrin IX-myoglobin complex from Parma ham is pH-dependent.

  Haruka Abe, Yang Zhai, Yu Toba, Hiroki Masumo, Toru Hayakawa, Haruto Kumura, Jun-Ichi Wakamatsu

  Food chemistry 441 138317 - 138317 2024/01/02 

  The bright red color of Parma ham is mainly derived from zinc protoporphyrin IX (ZnPP), which exists in both water-soluble and insoluble states. Water-soluble ZnPP mainly binds to hemoglobin, however, the presence of water-insoluble ZnPP remains unexplained. Therefore, we aimed to elucidate how ZnPP exists in a water-insoluble state by focusing on its binding substance. Depending on the skeletal muscle, water-insoluble ZnPP comprised 30-50% of total ZnPP. The ZnPP water extractability was positively correlated with muscle pH. Water-insoluble ZnPP was extractable with a high-pH solution and existed as a complex with myoglobin or hemoglobin; nevertheless, myoglobin-binding ZnPP was more abundant. Furthermore, the water solubility of the myoglobin globin moiety at pH 5.5-6.0 was reduced by ZnPP binding. These results suggest that water-insoluble ZnPP mainly exists as a ZnPP-Mb complex, with low solubility attributed to the low pH of the ham.
• Dissociation of ferriheme from oxidized heme proteins and re-reduction of ferriheme to ferroheme are crucial for the formation of zinc protoporphyrin IX in nitrite/nitrate-free dry-cured meat products.

  Yang Zhai, Haruka Abe, Hung-Cheng Wang, Toru Hayakawa, Haruto Kumura, Jun-Ichi Wakamatsu

  Food chemistry 427 136755 - 136755 2023/11/30 

  Zinc protoporphyrin IX (ZnPP) is the dominant red pigment in nitrate/nitrite-free dry-cured meat products such as Parma ham, and it is considered to be a potential alternative to nitrite/nitrate for reddening dry-cured meat products. Ferroheme and ferriheme dissociated from heme proteins in meat were proposed as substrates to form ZnPP. To elucidate their specific formation mechanism, nitric oxide, carbon monoxide, and azide were used to stable heme in heme proteins. The exogenous hemoglobin derivatives bound with these ligands showed lower heme dissociation compared with exogenous oxyhemoglobin and did not contribute to ZnPP formation. Meanwhile, azide inhibited almost all ZnPP formation by binding to ferriheme, indicating ferriheme dissociation from oxidized heme proteins, predominantly for ZnPP formation. Free ferriheme could not be converted to ZnPP unless it was reduced to ferroheme. Overall, ferriheme dissociated from oxidized heme proteins was the dominant substrate for conversion to ZnPP after re-reduction to ferroheme.
• Supplementary effect of whey components on the monascin productivity of Monascus sp.

  Qingyun Huang, Nodoka Miyaki, Zongfei Li, Yutaroh Takahashi, Satoshi Ishizuka, Toru Hayakawa, Jun-Ichi Wakamatsu, Haruto Kumura

  Journal of the science of food and agriculture 103 (8) 4234 - 4241 2023/06 

  BACKGROUND: Monascus sp. has been used in fermented foods for centuries. It can synthesize yellow, red, and orange pigments as secondary metabolites. Here, we focused on yellow pigment monascin, responsible for anti-inflammation and antidiabetic effects, and investigated whether whey could be a suitable substrate with or without rice powder for monascin production using M. purpureus AHU 9085, M. pilosus NBRC 4520 and M. ruber NBRC 32318. RESULTS: The growth and monascin production of the three Monascus strains were dependent on three liquid media consisting of whey and/or rice. All strains showed the best growth in a rice and whey mixed medium, in which M. ruber NBRC 32318 exhibited the highest total monascin production. Subsequent investigation of the effects of whey components indicated that a mineral cocktail in whey was particularly effective in stimulating the monascin production efficiency of M. ruber NBRC 32318. However, this recipe exhibited less stimulation, or even inhibition, for M. pilosus NBRC 4520 and M. purpureus AHU 9085, respectively. In terms of total monascin production, rice with whey provided the highest amount due to growth promotion along with relatively high production efficiency. CONCLUSION: The effect of whey on growth and monascin production was strongly dependent on the Monascus strains. Even a mineral cocktail in whey could regulate monascin productivity in a strain-specific manner. Further studies are needed to elucidate the mechanism behind the diverse responses by the minerals in the production of monascin from Monascus. © 2023 Society of Chemical Industry.
• L‐histidine inhibits the heat‐induced gelation of actomyosin in a low ionic strength solution

  Toru Hayakawa, Yu Kubono, Shuji Fujii, Jun‐ichi Wakamatsu, Haruto Kumura

  Animal Science Journal 94 (1) 1344-3941 2023/01 [Refereed]
  
• Zinc protoporphyrin IX predominantly exists as a complex non-enzymatically bound to apo-hemoglobin in Parma ham.

  Yang Zhai, Hung-Cheng Wang, Toru Hayakawa, Haruto Kumura, Jun-Ichi Wakamatsu

  Food chemistry 395 133604 - 133604 2022/11/30 

  Most of the water-soluble zinc protoporphyrin IX (ZnPP) in Parma ham mainly exists as complexes with hemoglobin and myoglobin (ZnPP-Hb and ZnPP-Mb). To elucidate the formation mechanism of these complexes, a new experimental model to produce higher amount of water-soluble ZnPP complexes was established. ZnPP-Hb was detected as the main water-soluble ZnPP complex in this model, which is the same as that in Parma ham. Adding exogenous Hb into this model promoted higher ZnPP formation than with Mb added, indicating that Hb was the superior substrate for generating ZnPP compared to Mb. The increase in non-heme iron content with ZnPP formation in both the Hb- and Mb-added groups indicated that the release of iron ion from heme was a crucial step in ZnPP formation. ZnPP-Hb was formed when ZnPP non-enzymatically bound with apo-Hb. These results revealed the mechanism of why ZnPP-Hb is more dominant in Parma ham than to ZnPP-Mb.
• A study of lipolysis induced by adjuncts from edible Aspergillus sp. solid culture products on ripened semi-hard cheese.

  Napaporn Chintagavongse, Hayate Takiguchi, Chi Ming-Hsuan, Koichi Tamano, Toru Hayakawa, Jun-Ichi Wakamatsu, Tomohiro Mitani, Haruto Kumura

  Journal of the science of food and agriculture 2022/01/23 

  BACKGROUND: Aspergillus sp. has been used in traditional Japanese fermented foods. Protease-containing culture products of A. oryzae have been applied as the adjunct enzyme source to enrich the flavor in ripened cheese. Although proteolysis was stimulated, the increase of free fatty acids (FFA) was recognized in some products. Since an excess amount of FFA accumulation can cause rancidity in cheese products, the assessment of lipase activity was considered to be essential for the cheese adjunct preparation. RESULTS: Although an equal lipase activity from the adjunct materials of A. kawachii NBRC 4308, A. luchuensis RIB 2604 and A. oryzae AHU 7139 was applied to semi-hard cheese, the FFA level was significantly higher in A. oryzae cheese than in the others. Furthermore, the profiles of volatile components were different in experimental cheeses. An in vitro study with experimental curds demonstrated that the high FFA might not depend on the lipase retainability on curds. On the contrary, the pronounced activation of the lipases occurred in A. oryzae after incubation with the curds. Moreover, incubation of the insoluble lipase that had been attached to the cells with skim milk curd extracts allowed the release of lipases from the cells into the medium with remarkable activation. CONCLUSION: A. oryzae AHU 7139 possessed a complex lipolytic system comprising extracellular and cell-binding lipases that were attributed to the increase in FFA in A. oryzae cheese. © 2022 Society of Chemical Industry.
• Water-extractable zinc protoporphyrin IX in Parma ham predominantly exists as complexes with hemoglobin and myoglobin

  Hung-Cheng Wang, Toru Hayakawa, Haruto Kumura, Jun-ichi Wakamatsu

  Food Bioscience 40 100870 - 100870 2212-4292 2021/04 [Refereed]
  
• High ZnPP-forming food-grade lactic acid bacteria as a potential substitute for nitrite/nitrate to improve the color of meat products.

  Md Kauser-Ul-Alam, Toru Hayakawa, Haruto Kumura, Jun-Ichi Wakamatsu

  Meat science 176 108467 - 108467 2021/02/19 [Refereed]
   

  Zinc protoporphyrin IX (ZnPP)-forming food-grade lactic acid bacteria (LAB) were screened from various sources for their ability to improve the color of meat products. The effects of salt and nitrite on the ZnPP-forming ability of these bacteria were also investigated. Finally, these bacteria were applied in salt-added minced meat to assess their ability to improve the color. Twenty-five LAB were screened for their ZnPP-forming ability in pork. Most of the strains exhibited maximum growth anaerobically in 3% salt at 30 °C and grew well at pH 5.5 and 6.5. Moreover, 3% salt slightly retarded ZnPP formation; however, nitrite completely inhibited ZnPP formation in all the ZnPP-forming LAB. Thirteen LAB (avoiding duplication and non-food-grade) could form ZnPP in salt-added minced meat, resulting in improvement of the bright red color, high ZnPP autofluorescence, and increased fluorescence intensity. Finally, considering the safety, Lactobacillus plantarum, Lactococcus lactis subsp. cremoris, and Leuconostoc lactis were suggested as promising candidates to improve the color of meat products.
• 鉄，亜鉛およびポルフィリンの推移からみた食肉中の亜鉛プロトポルフィリンIX形成機構

  王鴻誠, 大屋桃, 早川徹, 玖村朗人, 若松純一

  Nihon Chikusan Gakkaiho 91 (4) 389 - 394 1346-907X 2020/11/25 [Refereed]
  
• Lactococcus lactis Subsp. Cremoris Produces Zinc Protoporphyrin IX Both Aerobically and Anaerobically and Improves the Bright Red Color of Fermented Meat Products.

  Md Kauser-Ul-Alam, Yu Toba, Shoji Hioki, Toru Hayakawa, Haruto Kumura, Jun-Ichi Wakamatsu

  Foods (Basel, Switzerland) 9 (11) 2020/10/31 [Refereed]
   

  This study assessed the color improvement via zinc protoporphyrin IX (ZnPP) formation in nitrite-free, dry-cured sausages processed using five varieties of ZnPP-forming lactic acid bacteria (LAB). The ZnPP contents and color intensity of the sausages and other technological properties were analyzed during the processing of sausages. LAB count and acidity significantly increased in the LAB-inoculated sausages compared to the control group. The bright red color was observed both inside and outside the sausages inoculated with Lactococcus lactis subsp. cremoris and Leuconostoc lactis. However, a brown color was observed on the surface of the sausage inoculated with Lactobacillus spp. The redness of Lactococcus lactis subsp. cremoris-inoculated sausages was close to that of the nitrite-added group. Moreover, the external bright red color was improved by Lactococcus lactis subsp. cremoris due to the aerobic formation of ZnPP. Therefore, Lactococcus lactis subsp. cremoris can be used to improve the color of fermented meat products.
• Adjunctive application of solid‐state culture products and its freeze‐dried powder from Aspergillus sojae for semi‐hard cheese

  Napaporn Chintagavongse, Tomoki Yoneda, Chi Ming‐Hsuan, Toru Hayakawa, Jun‐ichi Wakamatsu, Koichi Tamano, Haruto Kumura

  Journal of the Science of Food and Agriculture 100 (13) 4834 - 4839 0022-5142 2020/10 [Refereed]
   

  BACKGROUND: Species belonging to the genus Aspergillus have been used in traditional Japanese fermented foods. Aspergillus sojae is a species responsible for strong proteolytic activity. Freeze-drying treatments followed by physical disruption enables the pulverization of the mycelia of A. sojae RIB 1045 grown in whey protein-base solid media. Intracellular proteases were extracted using this protocol to compare extracellular protease activity in terms of the reaction's pH dependence in the presence or absence of inhibitors. RESULT: With different sensitivities to inhibitors, intracellular and extracellular proteases showed the strongest activity under acidic conditions, which were considered suitable for cheese application. The raw culture product (CP) and its freeze-dried product (FDP) were mixed with cheese curds, prepared according to Gouda-type cheese-making methods, and were allowed to ripen for 3 months. Chemical analysis of the products showed 13.3% water-soluble nitrogen (WSN) in the control, which had received noncultured media, whereas 20.0% and 21.1% WSN was found in the CP and FDP experimental cheeses, respectively. Although these adjuncts significantly increased WSN, an insignificant difference was found between CP and FDP. Free fatty acids in all experimental cheeses were similar, showing that CP and FDP caused no rancid defects. CONCLUSION: The introduction of freeze-drying treatments accompanied by cell disruption resulted in a negligible effect in terms of WSN. However, the application of A. sojae can be beneficial when it comes to increasing the level of WSN compared with A. oryzae, as shown in our previous study. © 2020 Society of Chemical Industry.
• Searching for high ZnPP-forming edible bacteria to improve the color of fermented meat products without nitrite/nitrate.

  Md Asaduzzaman, Momo Ohya, Haruto Kumura, Toru Hayakawa, Jun-Ichi Wakamatsu

  Meat science 165 108109 - 108109 2020/07 [Refereed]
   

  In order to improve the color of meat products by producing zinc protoporphyrin IX (ZnPP) in meat, we searched for edible bacteria with high ZnPP-forming ability. Eleven bacteria used in different animal products and 126 bacteria isolated from environmental and probiotic sources were assessed for their ability to form ZnPP. Many bacteria from both sources showed a high ZnPP-forming ability. Only three edible bacteria were identified from the 44 high ZnPP-forming isolates with 16S rRNA gene sequencing. High ZnPP-forming bacteria from both sources were inoculated in aseptic salt-added minced meat, and their ZnPP-forming abilities were evaluated. Lactococcus lactis, Leuconostoc mesenteroides, and Enterococcus faecium from environmental isolates produced a brighter red color, higher ZnPP autofluorescence and fluorescence intensity in salt-added minced meat than control. Furthermore, after heating, the color and ZnPP autofluorescence of the inoculated minced meat persisted to a degree. Therefore, it is possible to improve the color of meat products without nitrite/nitrate by using these promising ZnPP-forming edible bacteria.
• Improving the color of meat products without adding nitrite/nitrate using high zinc protoporphyrin IX-forming microorganisms.

  Wakamatsu JI, Kawazoe H, Ohya M, Hayakawa T, Kumura H

  Meat science 161 107989 - 107989 0309-1740 2019/10 [Refereed][Not invited]
   

  Zinc protoporphyrin IX (ZnPP) mainly contributes to the red color of dry cured ham without nitrites/nitrates. Here, we examined the effects of acids used for pH adjustment, pH, and microorganisms on ZnPP formation. The results showed that ZnPP formation and optimal pH were dependent upon the acid type. In the presence of microorganisms, the optimal pH for ZnPP formation shifted to higher values, with the amount of formed ZnPP markedly increased at the shifted optimal pH. Additionally, two bacterial strains isolated from incubated pork homogenate exhibited an enhanced ability to form ZnPP. Although the two isolated bacteria are not edible, inoculation with one bacterium into minced meat resulted in formation of large amounts of ZnPP and color closer to that of nitrite-added meat. These results suggest that appropriate food-grade bacterial strains can improve the color of various fermented meat products in the absence of nitrites/nitrates.
• 'Lipase and protease production of dairy Penicillium sp. on milk-protein-based solid substrates'

  Kumura Haruto, Satoh Megumi, Machiya Taiki, Hosono Makoto, Hayakawa Toru, Wakamatsu Jun-Ichi

  INTERNATIONAL JOURNAL OF DAIRY TECHNOLOGY 72 (3) 403 - 408 1364-727X 2019/08 [Refereed][Not invited]
   

  The lipolytic and proteolytic activity of Penicillium camemberti PC TT033 and Penicillium roqueforti PR G3, cultured on the whey solids or simulated cheese media, were compared under several pH reaction conditions. Lipolytic activity was higher when both strains had been cultured on the whey medium than on the simulated cheese medium, whereas proteolytic activity was less influenced by the culture medium. The relationship between the reaction pH and these enzyme activities was dependent on the culture medium, which suggested that the expression level and balance of isozyme rely on the culture substrate.
• Investigation of contributors to zinc protoporphyrin IX formation at optimum pH 5.5 in pork.

  Akter M, Shiraishi A, Kumura H, Hayakawa T, Wakamatsu JI

  Animal science journal = Nihon chikusan Gakkaiho 90 (6) 774 - 780 1344-3941 2019/06 [Refereed][Not invited]
  
• Optimal pH of zinc protoporphyrin IX formation in porcine muscles: Effects of muscle fiber type and myoglobin content

  Wakamatsu Jun-ichi, Akter Mofassara, Honma Fumika, Hayakawa Toru, Kumura Haruto, Nishimura Takanori

  LWT-FOOD SCIENCE AND TECHNOLOGY 101 599 - 606 0023-6438 2019/03 [Refereed][Not invited]
  
• Application of red pigment producing edible fungi for development of a novel type of functional cheese

  Kumura Haruto, Ohtsuyama Takeru, Matsusaki Yoh-hey, Taitoh Miho, Koyanagi Haruka, Kobayashi Ken, Hayakawa Toru, Wakamatsu Jun-ichi, Ishizuka Satoshi

  JOURNAL OF FOOD PROCESSING AND PRESERVATION 42 (10) 0145-8892 2018/10 [Refereed][Not invited]
  
• Role of Heavy Meromyosin in Heat-Induced Gelation in Low Ionic Strength Solution Containing l-Histidine

  Toru Hayakawa, Yuri Yoshida, Masanori Yasui, Toshiaki Ito, Jun-ichi Wakamatsu, Akihito Hattori, Takanori Nishimura

  JOURNAL OF FOOD SCIENCE 80 (8) C1641 - C1645 0022-1147 2015/08 [Refereed][Not invited]
   

  The gelation of myosin has a very important role in meat products. We have already shown that myosin in low ionic strength solution containing l-histidine forms a transparent gel after heating. To clarify the mechanism of this unique gelation, we investigated the changes in the nature of myosin subfragments during heating in solutions with low and high ionic strengths with and without l-histidine. The hydrophobicity of myosin and heavy meromyosin (HMM) in low ionic strength solution containing l-histidine was lower than in high ionic strength solution. The SH contents of myosin and HMM in low ionic strength solution containing l-histidine did not change during the heating process, whereas in high ionic strength solution they decreased slightly. The heat-induced globular masses of HMM in low ionic strength solution containing l-histidine were smaller than those in high ionic strength solution. These findings suggested that the polymerization of HMM molecules by heating was suppressed in low ionic strength solution containing l-histidine, resulting in formation of the unique gel. Practical Application The heat-induced gelation of myosin has an important role in meat products and contributes to its quality. Our previous study showed the unique gelation of myosin in low ionic strength solution with l-histidine was different from gelation already known. Understanding the mechanism of this unique gelation of myosin in low ionic strength solution with histidine will lead to development of new meat-based products and to innovation in the meat industry.
• Dietary L-cysteine inhibits D-galactosamine-induced acute liver injury in rats

  Seulki Lee, Kyu-Ho Han, Erina Yabuki, Yumi Nakamura, Sakura Kawakami, Kenichiro Shimada, Toru Hayakawa, Hirotake Onoue, Michihiro Fukushima

  FOOD SCIENCE AND BIOTECHNOLOGY 24 (3) 1151 - 1157 1226-7708 2015/06 [Refereed][Not invited]
   

  The effects of l-cysteine (1 and 2%) on the antioxidative system were examined in rats with d-galactosamine (d-GalN)-induced injury. These rats showed increases in serum antioxidative enzyme and hepatic thiobarbituric acid reactive substances (TBARS) activities, with decreased hepatic/serum glutathione (GSH) levels and GSH-related enzyme activities. However, l-cysteine supplementation resulted in a decrease of hepatic TBARS levels, and increased catalase and serum GSH levels. The activities of serum enzymes in rats receiving 2% l-cysteine were significantly (p < 0.05) lower than in d-GalN-injected group rats, and similar to levels in control group rats without acute liver injury. In addition, 2% l-cysteine increased the glutathione reductase activity and decreased the serum TBARS level in liver injury group rats. Dietary l-cysteine, especially at a 2% level, exerts a hepatoprotective effect by alteration of the GSH level and antioxidative enzyme activities.
• Porcine Splenic Hydrolysate has Antioxidant Activity in vivo and in vitro

  Kyu-Ho Han, Kenichiro Shimada, Toru Hayakawa, Taek Joan Yoon, Michihiro Fukushima

  KOREAN JOURNAL FOR FOOD SCIENCE OF ANIMAL RESOURCES 34 (3) 325 - 332 1225-8563 2014/06 [Refereed][Not invited]
   

  The antioxidant capacity of porcine splenic hydrolysate (PSH) was studied in vitro and in vivo. Peptide hydrolysates were prepared, using the proteolytic enzyme Alcalase (R). The molecular weights of PSH were 37,666, 10,673, 6,029, and 2,918 g/mol. Rats were fed a 5% (w/v) PSH diet, instead of a casein diet, for 4 wk. The food intake, body weight gain, and liver weight of rats in the PSH group were similar to those in the control (CONT) group. There were no differences in the serum total cholesterol, triglyceride, total protein, or albumin levels between PSH and CONT groups. However, the level of in vivo hepatic lipid peroxidation in PSH group was significantly lower than that in CONT. In vivo hepatic catalase and glutathione peroxidase activities in the PSH group were significantly higher than those in the control group. The in vitro protein digestibility of PSH was lower than that of casein. The in vitro trolox equivalent antioxidant capacity of PSH was significantly higher than that of the peptide hydrolysate from casein. The in vitro radical scavenging activities of PSH were significantly higher than those of the peptide hydrolysate from casein. The present findings suggest that porcine splenic peptides improve the antioxidant status in rats by enhancing hepatic catalase and GSH-Px activities, and indicate a potential mechanism of radical scavenging activity during gastrointestinal passage.
• Heat-induced gelation of myosin in a low ionic strength solution containing L-histidine

  T. Hayakawa, Y. Yoshida, M. Yasui, T. Ito, T. Iwasaki, J. Wakamatsu, A. Hattori, T. Nishimura

  MEAT SCIENCE 90 (1) 77 - 80 0309-1740 2012/01 [Refereed][Not invited]
   

  Binding properties are important for meat products and are substantially derived from the heat-induced gelation of myosin. We have shown that myosin is solubilized in a low ionic strength solution containing L-histidine. To clarify its processing characteristics, we investigated properties and structures of heat-induced gels of myosin solubilized in a low ionic strength solution containing t-histidine. Myosin in a low ionic strength solution formed transparent gels at 40-50 degrees C, while myosin in a high ionic strength solution formed opaque gels at 60-70 degrees C. The gel of myosin in a low ionic strength solution with t-histidine showed a fine network consisting of thin strands and its viscosity was lower than that of myosin in a high ionic strength solution at 40-50 degrees C. The rheological properties of heat-induced gels of myosin at low ionic strength are different from those at high ionic strength. This difference might be caused by structural changes in the rod region of myosin in a low ionic strength solution containing t-histidine. (C) 2011 Elsevier Ltd. All rights reserved.
• Myosin filament depolymerizes in a low ionic strength solution containing L-histidine

  T. Hayakawa, T. Ito, J. Wakamatsu, T. Nishimura, A. Hattori

  MEAT SCIENCE 84 (4) 742 - 746 0309-1740 2010/04 [Refereed][Not invited]
   

  Myosin, one of the major myofibrillar proteins, forms a filamentous polymer and is insoluble in physiological and low ionic strength solutions. We have shown that myosin is soluble in a low ionic strength solution containing L-histidine. In this study, to clarify the role of L-histidine in the solubilization of myosin, we investigated effects of L-histidine on the filament formation and the morphology of myosin at a low ionic strength. In the presence of L-histidine, myosin formed a filamentous polymer in a physiological ionic strength solution and dispersed in a low ionic strength solution. Transmission electron microscopy showed that light meromyosin (LMM), the rod region of myosin, in a low ionic strength solution containing L-histidine was longer than that in a high ionic strength solution without L-histidine. L-histidine causes the elongation of LMM region of myosin contributing to the weakening of the myosin filament and the dissociation of myosin in a low ionic strength solution. (C) 2009 Elsevier Ltd. All rights reserved.
• Myosin is solubilized in a neutral and low ionic strength solution containing L-histidine

  T. Hayakawa, T. Ito, J. Wakamatsu, T. Nishimura, A. Hattori

  MEAT SCIENCE 82 (2) 151 - 154 0309-1740 2009/06 [Refereed][Not invited]
   

  Myosin, one of the major myofibrillar proteins, is insoluble at low and physiological ionic strength and soluble at high ionic strength. In this study, the behavior and morphology of myosin solubilized in a low ionic strength Solution containing L-histidine (L-His) was investigated. More than 80% of myosin was solubilized in a low ionic strength solution with dialysis against a solution containing 1 mM KCl and 5 MM L-His. Transmission electron microscopy with rotary shadowing demonstrated that the rod of myosin in a low ionic strength solution containing L-His is longer than that of myosin in a high ionic strength solution. The elongation of the myosin rod in a low ionic strength solution containing L-His would inhibit the formation of a filament, resulting in the solubilization of myosin. (c) 2009 Elsevier Ltd. All rights reserved.
• Antihypertensive Effects and Endothelial Progenitor Cell Activation by Intake of Chicken Collagen Hydrolysate in Pre- and Mild-Hypertension

  Ai Saiga-Egusa, Koji Iwai, Toru Hayakawa, Yoshihisa Takahata, Fumiki Morimatsu

  BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY 73 (2) 422 - 424 0916-8451 2009/02 [Refereed][Not invited]
   

  Chicken collagen hydrolysate was given to 15 mildly hypertensive subjects for 4 weeks. Blood pressure was significantly decreased by 11.8 mmHg (P < 0.01). A reduction in plasma renin activity was observed in blood test after intake. A colony assay of endothelial progenitor cells in blood samples from non-smokers revealed an approximately 30% increase in the number of colonies.
• Angiotensin I-Converting Enzyme-inhibitory Peptides Obtained from Chicken Collagen Hydrolysate

  Ai Saiga, Koji Iwai, Toru Hayakawa, Yoshihisa Takahata, Shiniich Kitamura, Toshihide Nishimura, Fumiki Morimatsu

  JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 56 (20) 9586 - 9591 0021-8561 2008/10 [Refereed][Not invited]
   

  In this study, collagen extracted from chicken legs (which are the yellow keratin parts containing a nail) was hydrolyzed with various enzymes, and the angiotensin I-converting enzyme (ACE)-inhibitory activity of each hydrolysate was determined. The hydrolysate by treatment with an Aspergillus species-derived enzyme had the highest activity (IC50 = 260 mu g/mL). The fraction of this hydrolysate obtained by ultrafiltration with a molecular-weight cutoff of 3000 Da (low fraction) had a stronger activity (IC50 = 130 mu g/mL) than the fractionated one. This fraction was further fractionated by HPLC, and the peptides in the fraction with high ACE-inhibitory activity were identified. The amino acid sequences of the four peptides were identified using a protein sequencer. These peptides were synthesized to confirm their ACE-inhibitory activities; this showed that peptides with a Gly-Ala-Hyp-Gly-Leu-Hyp-Gly-Pro sequence had the highest activity (IC50 = 29 mu M). When the low fraction was administered to spontaneous hypertensive rats, a decrease in their blood pressure was observed after 2 h of administration, and a significant decrease in blood pressure (-50 mmHg) was observed after 6 h. Moreover, long-term administration studies indicated that the low fraction showed a significant suppression of increased blood pressure.
• Oral administration of chicken breast extract increases brain carnosine and anserine concentrations in rats

  Shozo Tomonaga, Toru Hayakawa, Haruka Yamane, Hirohiko Maemura, Mikako Sato, Yoshihisa Takahata, Fumiki Morimatsu, Mitsuhiro Furuse

  NUTRITIONAL NEUROSCIENCE 10 (3-4) 181 - 186 1028-415X 2007 [Refereed][Not invited]
   

  Carnosine(beta-alanyl-L-histidine) and its derivative anserine (beta-alanyl-1-methyl-L- histidine) are antioxidants and putative neurotransmitters in the brain. These dipeptides are rich in the commercially available supplement chicken breast extract (CBEX). To clarify the effects of CBEX on the brain, we examined whether single oral administration of CBEX (20ml/kg) affects brain dipeptide and free amino acid concentrations in male Wistar rats. CBEX significantly and time-dependently increased carnosine and anserine levels in the plasma (at 120 min after injection, increase rates were 2976 and 4142%, respectively), hippocampus (64 and 78%), and hypothalamus (188 and 120%), but not in cerebral cortex. Significant and time-dependent increases in citrulline in the hippocampus (49%) and hypothalamus (41%) demonstrated generation of nitric oxide due to the increased carnosine and/or anserine levels in these brain regions. These findings suggest that CBEX modifies brain functions by increasing levels of these dipeptides.

MISC

• チーズの風味強化剤としての麹調製~酵素活性と香気特性を指標とした検討~

  川上倖奈, CHINTAGAVONGSE Napaporn, 原聡美, 玉野孝一, 早川徹, 若松純一, 玖村朗人, 三谷朋弘  ミルクサイエンス(Web)  72-  (2)  2023
• Establishment of new experimental model to investigate the mechanism by which water-soluble ZnPP is formed in Parma ham

  YANG Zhai, 早川徹, 玖村朗人, 若松純一  日本食肉研究会総会提出議案及び大会講演要旨  62nd (CD-ROM)-  2021
• パルマハムから弱アルカリで抽出される亜鉛プロトポルフィリンIXの存在形態の解明

  阿部悠, 早川徹, 玖村朗人, 若松純一  日本食肉研究会総会提出議案及び大会講演要旨  62nd (CD-ROM)-  2021
• カルノシンは死後硬直条件下におけるアクトミオシンのATP分解を促進する

  岡田実那美, 若松純一, 玖村朗人, 早川徹  日本食肉研究会総会提出議案及び大会講演要旨  62nd (CD-ROM)-  2021
• ヒスチジンによるアクトミオシン加熱ゲル形成の抑制について

  早川徹, 窪野佑, 若松純一, 玖村朗人  日本バイオレオロジー学会誌(Web)  34-  (2)  2020
• パルマハムにおけるダークスポットの特性

  王鴻誠, 尾崎あかり, 早川徹, 玖村朗人, 若松純一  食肉の科学  60-  (1)  140  2019/06/30  [Not refereed][Not invited]
  
• L‐ヒスチジンは低塩濃度条件下の天然アクトミオシンの加熱ゲル形成を抑制する

  窪野佑, 早川徹, 若松純一, 玖村朗人  食肉の科学  60-  (1)  140  2019/06/30  [Not refereed][Not invited]
  
• L‐ヒスチジンは低塩濃度条件下の天然アクトミオシンの加熱ゲル形成を抑制する

  窪野佑, 若松純一, 玖村朗人, 早川徹  日本畜産学会大会講演要旨  125th-  203  2019/03/28  [Not refereed][Not invited]
  
• 小型乾塩漬ハムにおける亜鉛プロトボルフィリンIXの形成様相の観察

  尾崎あかり, 早川徹, 玖村朗人, 若松純一  日本畜産学会大会講演要旨  125th-  203  2019/03/28  [Not refereed][Not invited]
  
• パルマハムにおけるダークスポットの特性

  王鴻誠, 尾崎あかり, 早川徹, 玖村朗人, 若松純一  日本畜産学会大会講演要旨  125th-  202  2019/03/28  [Not refereed][Not invited]
  
• 糸状菌の菌体破砕処理が菌体内二次代謝産物の人工消化液による抽出性に及ぼす影響

  高橋勇太郎, LI Zongfei, 早川徹, 若松純一, 玖村朗人  日本農芸化学会大会講演要旨集(Web)  2019-  ROMBUNNO.4C1a15 (WEB ONLY)  2019/03/05  [Not refereed][Not invited]
  
• ホエイ固形培地上におけるAspergillus oryzaeのリパーゼ及びプロテアーゼ産生に及ぼす糖質の影響

  細野誠, 玉野孝一, 若松純一, 早川徹, 玖村朗人  日本農芸化学会東北支部大会プログラム・講演要旨集  153rd-  64  2018/09/22  [Not refereed][Not invited]
  
• 野生エゾシカの肉質に及ぼす狙撃部位と銃の口径の影響

  桑子和洋, 亀井利活, 稲富佳洋, 早川徹, 玖村朗人, 近藤誠司, 若松純一  北海道畜産草地学会報  6-  (2)  23  2018/08/20  [Not refereed][Not invited]
  
• Identification of myosin rod region involved in the solubilization under the low ionic strength condition

  早川徹  食肉に関する助成研究調査成果報告書  35-  40‐45  2017/11  [Not refereed][Not invited]
  
• カルシウムの添加がヒスチジンによるミオシン水溶化作用を阻害する

  早川徹, 窪野佑, 若松純一, 玖村朗人  日本畜産学会大会講演要旨  123rd-  122  2017/09/06  [Not refereed][Not invited]
  
• 鶏・牛の各種骨格筋におけるZnPP形成に及ぼす至適pHの探索

  青井綾花, 早川徹, 玖村朗人, 若松純一  北海道畜産草地学会報  5-  (2)  28  2017/08/24  [Not refereed][Not invited]
  
• 亜鉛プロトポルフィリン9形成機構のクロマトグラフィによる検証

  齋藤貴洋, 早川徹, 玖村朗人, 若松純一  日本畜産学会大会講演要旨  122nd-  192  2017/03/28  [Not refereed][Not invited]
  
• 食肉由来消化・吸収ペプチドの畜種による違い

  中原健人, 早川徹, 玖村朗人, 若松純一  日本畜産学会大会講演要旨  122nd-  193  2017/03/28  [Not refereed][Not invited]
  
• ホエイ固形培地上における食用Penicillium属由来のリパーゼ産生

  佐藤恵実, 町谷泰紀, 早川徹, 曾根輝雄, 若松純一, 木村彰, 玖村朗人  日本農芸化学会大会講演要旨集(Web)  2017-  ROMBUNNO.3A05p10 (WEB ONLY)  2017/03/05  [Not refereed][Not invited]
  
• The identification of myosin rod region involved in the solubilization under the low ionic strength condition

  早川徹  食肉に関する助成研究調査成果報告書  34-  29‐33  2016/11  [Not refereed][Not invited]
  
• ミオシンのヒスチジンによる水溶化現象

  早川徹  食肉の科学  57-  (1)  19‐24  -24  2016/06/30  [Not refereed][Not invited]
  
• ミオシンの水溶化現象における尾部領域の表面電荷の影響

  早川徹, 尾嶋孝一, 竹内薫, 島田謙一郎  日本畜産学会大会講演要旨  121st-  215  2016/03/27  [Not refereed][Not invited]
  
• The identification of myosin rod region involved in the solubilization under the low ionic strength condition

  早川徹  食肉に関する助成研究調査成果報告書  33-  79  -83  2015/11  [Not refereed][Not invited]
  
• 日本短角種去勢牛の早期出荷は肉質に影響を及ぼさない

  竹内薫, 中江佑, 韓圭鎬, 福島道広, 早川徹, 口田圭吾, 島田謙一郎  日本畜産学会大会講演要旨  120th-  106  2015/09/11  [Not refereed][Not invited]
  
• 牛骨とエゾシカ骨より調製したスープストックの品質に関する検討

  菊池亨, 韓圭鎬, 福島道広, 早川徹, 島田謙一郎  日本畜産学会大会講演要旨  119th-  241  2015/03/28  [Not refereed][Not invited]
  
• 微生物資材を用いたふん尿処理に伴う臭気低減化の検討

  川上秋桜, 中村有美, 早川徹, 島田謙一郎, 韓圭鎬, 山本一夫, 関山真一, 合屋佳代, 上坂欽也, 佐々木勝彦, 西村直道, 福島道広  北海道畜産草地学会報  2-  146  2014/03/31  [Not refereed][Not invited]
  
• エゾシカ骨より調製したスープストックの品質に関する研究

  菊池亨, 小林彩花, 韓圭鎬, 福島道広, 早川徹, 島田謙一郎  日本畜産学会大会講演要旨  117th-  111  2013/09/09  [Not refereed][Not invited]
  
• Dietary L-Cysteine Improves the Antioxidative Potential and Lipid Metabolism in Rats Fed a Normal Diet

  Seulki Lee, Kyu-Ho Han, Yumi Nakamura, Sakura Kawakami, Ken-ichiro Shimada, Touru Hayakawa, Hirotake Onoue, Michihiro Fukushima  BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY  77-  (7)  1430  -1434  2013/07  [Not refereed][Not invited]
   

  L-Cysteine works as a precursor of the antioxidant, glutathione. We investigated the effects of L-cysteine (1% and 2%) on lipid metabolism and the antioxidative system in rats fed a normal diet. Administering L-cysteine dependently decreased the food intake, fat mass weight and body weight dose. Dietary L-cysteine also decreased the triglyceride levels in the serum and liver. However, there were no significant differences in the hepatic TSARS and glutathione (GSH) levels among the groups. The activities of catalase and glutathione reductase in the rats receiving 2% L-cysteine were significantly higher (p < 0.05) than in the control rats. These results suggest that dietary L-cysteine dose-dependently affected the antioxidative enzyme activities, and the lipid levels in the serum and liver which might be related to the reduced food intake.
• 豚肉中に残留する血液量の推定

  永井孝典, 早川徹, 韓圭鎬, 福島道広, 島田謙一郎  北海道畜産草地学会報  1-  80  2013/03/29  [Not refereed][Not invited]
  
• ベーコン塩漬時のアズキポリフェノールの浸透について

  島田謙一郎, 高橋佑佳, 韓圭鎬, 早川徹, 福島道広  日本畜産学会大会講演要旨  116th-  199  2013/03/28  [Not refereed][Not invited]
  
• ミオシンの水溶化機構に関する研究

  早川 徹, 安川 裕也, 吉田 有里, 若松 純一, 西邑 隆徳  食肉の科学  53-  (1)  144  -147  2012/06/30
• ミオシンの水溶化機構に関する研究

  早川徹, 安川裕也, 吉田有里, 若松純一, 西邑隆徳  日本食肉研究会総会提出議案及び大会講演要旨  53rd-  36  -39  2012  [Not refereed][Not invited]
  
• 低イオン強度下におけるミオシンの溶解性に及ぼすpHとL‐ヒスチジンの影響

  安川裕也, 西邑隆徳, 若松純一, 早川徹  日本畜産学会大会講演要旨  114th-  178  2011/08/26  [Not refereed][Not invited]
  
• L‐ヒスチジンを含む中性低イオン強度溶液におけるミオシンの水溶化について

  早川徹, 若松純一, 西邑隆徳  食肉の科学  52-  (1)  116  -119  2011/06/30  [Not refereed][Not invited]
  
• Rheological properties of heat-induced gels of myosin solubilized in a low ionic strength solutioncontaining L-histidine

  Yoshida Y, Hayakawa T, Wakamatsu J, Iwasaki T, Kaneda I, Nishimura T  Proceeding of 57th International Conference of Meat Science and Technology  1-  172  2011  [Not refereed][Not invited]
  
• L-ヒスチジンを含む中性低イオン強度溶液におけるミオシンの水溶化について (第52回日本食肉研究会大会発表要旨)

  早川 徹, 若松 純一, 西邑 隆徳  食肉の科学  52-  (1)  116  -119  2011  [Not refereed][Not invited]
  
• 水溶化ミオシンの加熱ゲル化特性

  吉田有里, 早川徹, 若松純一, 岩崎智仁, 西邑隆徳  日本畜産学会大会講演要旨  112th-  118  2010/03/28  [Not refereed][Not invited]
  
• L‐ヒスチジンおよびイオン強度がミオシンの存在形態に及ぼす影響

  早川徹, 若松純一, 西邑隆徳  日本畜産学会大会講演要旨  112th-  118  2010/03/28  [Not refereed][Not invited]
  
• 低イオン強度下におけるL‐メロミオシン分子の性状に及ぼすL‐ヒスチジンの影響

  早川徹, 若松純一, 西邑隆徳  日本畜産学会大会講演要旨  111th-  90  2009/09/28  [Not refereed][Not invited]
  
• Effect of porcine arterial elastin peptide to the moisture content of mice skin

  HAYAKAWA Toru, SATO Mikako, SAIGA EGUSA Ai, TAKAHATA Yoshihisa, MORIMATSU Fumiki, NOMURA Yoshihiro  Nihon Chikusan Gakkaiho  80-  (2)  215  -222  2009/05/25  [Not refereed][Not invited]
   

  We prepared hydrolysate of elastin from porcine aorta and evaluated its effect on skin by oral administration. In this study, the photoaging model which hairless mice were exposed by ultraviolet-B was adopted as a model of skin aging. Seven-week-old male hairless mice were fed a commercial diet and water for 63 days, and a hydrolysate dissolved in distilled water was adiministered. Ultraviolet-B irradiations were done 3 times per week. Moisture content of back skin was measured once or twice per week. After the administration term, skin pieces were taken from back of mouse, and then histopathological analysis was done and amino acid composition of skin was determined. Significant increases of skin moisture were observed in groups of the mixture of elastin peptide and collagen peptide and of collagen peptide after 52 and 55 days. In the administration of elastin peptide, skin moisture tended to increase. From the histopathological analysis, thickness of epidermis induced by ultrabiolet-B irradiation was depressed by the administration of the mixture of elastin and collagen peptide. Desmosine and isodesmosine content in skin was also depressed by the administration of the mixture of elastin and collagen peptide and of the collagen peptide only, while those of control mice irradiated ultraviolet-B was increased. Compared with each administration of elastin peptide and collagen peptide, the administration of mixture of these peptides in ratio of these skin contents or near ratio gave synergism, and then the improvement of skin condition, such as skin moisture and thickness of epidermis, against photoaging was observed. These results indicated that elastin peptide increased the effect of the administration of collagen peptide on skin moisture.
• L‐ヒスチジンを含む低イオン強度溶液へのミオシン溶解機構の解明

  早川徹, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  110th-  7  2009/03/27  [Not refereed][Not invited]
  
• Hypotensive Action of Chicken Collagen Hydrolysate in Lactic Acid Beverage on Mildly Hypertensive Subjects

  KOUGUCHI Tomomi, OHMORI Takashi, HAYAKAWA Toru, TAKAHATA Yoshihisa, MORIMATSU Fumiki, KAJIMOTO Yoshitaka  Journal of Japanese Society of Clinical Nutrition  29-  (4)  414  -424  2008/07/20  [Not refereed][Not invited]
  
• Hypotensive Action of Chicken Collagen Hydrolysate in Lactic Acid Beverage on Mildly Hypertensive Subjects

  KOUGUCHI Tomomi, OHMORI Takashi, HAYAKAWA Toru, TAKAHATA Yoshihisa, MORIMATSU Fumiki, KAJIMOTO Yoshitaka  Journal of Japanese Society of Clinical Nutrition  29-  (4)  414  -424  2008/07/20  [Not refereed][Not invited]
  
• Safety of Excess Administration of Lactic Acid Beverage Containing Chicken Collagen Hydrolysate

  河口友美, 大森丘, 早川徹, 高畑能久, 前山佳昭, 梶本佳孝, 森松文毅  薬理と治療  36-  (6)  549  -559  2008/06/20  [Not refereed][Not invited]
  
• Hypotensive Effects and Safety of Intake of Lactic Acid Beverage Containing Chicken Collagen Hydrolysate in Subjects with Mild Hypertension or High-normal Blood Pressure

  河口友美, 大森丘, 早川徹, 高畑能久, 前山佳昭, 梶本佳孝, 北風政史, 森松文毅  薬理と治療  36-  (6)  561  -575  2008/06/20  [Not refereed][Not invited]
  
• 豚由来エラスチンペプチドの長期摂取が皮膚に及ぼす影響

  神尾美智子, 鬼塚英一郎, 早川徹, 佐藤美佳子, 高畑能久, 森松文毅, 佐藤雄二  日本栄養・食糧学会大会講演要旨集  62nd-  231  2008/04/01  [Not refereed][Not invited]
  
• 鶏コラーゲン加水分解物(C‐COP)の安全性について

  清水宗茂, 早川徹, 河口友美, 雑賀愛, 大森丘, 高畑能久, 森松文毅  日本栄養・食糧学会大会講演要旨集  62nd-  278  -278  2008/04/01  [Not refereed][Not invited]
  
• 鶏コラーゲン加水分解物(C‐COP)によるeNOS活性化作用

  伊東亜衣, 早川徹, 雑賀愛, 河口友美, 清水宗茂, 大森丘, 高畑能久, 森松文毅, 西村敏英  日本栄養・食糧学会大会講演要旨集  62nd-  272  -272  2008/04/01  [Not refereed][Not invited]
  
• 鶏コラーゲン加水分解物(C‐COP)を配合した乳酸菌飲料の軽症高血圧者に対する効果

  河口友美, 早川徹, 大森丘, 高畑能久, 森松文毅, 梶本佳孝  日本栄養・食糧学会大会講演要旨集  62nd-  207  2008/04/01  [Not refereed][Not invited]
  
• 豚エラスチンペプチドの血管保全作用

  早川徹, 雜賀愛, 河口友美, 大森丘, 高畑能久, 森松文毅  日本畜産学会大会講演要旨  109th-  8  2008/03/27  [Not refereed][Not invited]
  
• 機能性食品素材の近況 畜産由来の機能性食品素材の近況

  早川徹  ジャパンフードサイエンス  47-  (1)  33  -40  2008/01/05  [Not refereed][Not invited]
  
• An Angiotensin I-converting Enzyme (ACE)-inhibitory Peptide Derived from Chicken Collagen Hydrolysate Lowers Blood Pressure in Spontaneously Hypertensive Rats

  Koji Iwai, Ai Saiga-Egusa, Toru Hayakawa, Muneshige Shimizu, Yoshihisa Takahata, Fumiki Morimatsu  JOURNAL OF THE JAPANESE SOCIETY FOR FOOD SCIENCE AND TECHNOLOGY-NIPPON SHOKUHIN KAGAKU KOGAKU KAISHI  55-  (12)  602  -605  2008  [Not refereed][Not invited]
   

  We studied the antihypertensive effect of an octapeptide (Gly-Ala-Hyp-Gly-Leu-Hyp-Gly-Pro), which is derived from chicken collagen hydrolysates and has strong angiotensin I-converting enzyme (ACE)inhibitory activity, on spontaneously hypertensive rats (SHRs). 6 h after a single oral administration of the octapeptide (4.5 mg/kg SHR body weight), the systolic blood pressure was significantly reduced. The octapeptide was not digested by digestive enzymes from the epithelia of the porcine small intestines in vitro. These results suggest that this ACE-inhibitory peptide is absorbed by SHRs in the peptide: form and that it lowers blood pressure.
• 鶏コラーゲン加水分解物(C‐COP)の高齢高血圧自然発症ラットへの投与における血管保全効果について

  早川徹, 雜賀愛, 河口友美, 大森丘, 高畑能久, 森松文毅  機能性食品と薬理栄養  4-  (5)  330  2007/11/30  [Not refereed][Not invited]
  
• 豚由来エラスチンペプチドの経口投与による光老化モデルマウス皮膚への影響

  早川徹, 佐藤三佳子, 雜賀愛, 高畑能久, 森松文毅, 野村義宏  日本畜産学会大会講演要旨  108th-  86  2007/09/26  [Not refereed][Not invited]
  
• Chicken breast extract and carnosine improve learning performance in mice.

  Tomonaga S, Hayakawa T, Oikawa D, Sato M, Takahata Y, Morimitsu F, Furuse M  53rd International Congress of Meat Science and Technology  2007/08  [Not refereed][Not invited]
  
• エラスチンペプチドの開発と機能性について

  早川徹, 佐藤三佳子, 雜賀愛, 高畑能久, 森松文毅  食肉の科学  48-  (1)  145  -150  2007/06/30  [Not refereed][Not invited]
  
• エラスチンペプチドの開発と機能性について

  早川 徹, 佐藤 三佳子, 雜賀 愛, 高畑 能久, 森松 文毅  食肉の科学  48-  (1)  145  -150  2007/06/30  [Not refereed][Not invited]
  
• 豚プラセンタエキスの安全性について

  佐藤三佳子, 早川徹, 前村公彦, 高畑能久, 森松文毅  日本栄養・食糧学会大会講演要旨集  61st-  262  2007/04/20  [Not refereed][Not invited]
  
• トリ胸肉抽出物の単回経口投与がラットの脳内遊離アミノ酸およびジペプチド含量に及ぼす影響

  友永省三, 前村公彦, 山根春香, 早川徹, 佐藤三佳子, 高畑能久, 森松文毅, 古瀬充宏  日本栄養・食糧学会大会講演要旨集  61st-  259  2007/04/20  [Not refereed][Not invited]
  
• エラスチンペプチド経口摂取後のヒト血中動態

  岩井浩二, 早川徹, 佐藤三佳子, 高畑能久, 森松文毅  日本栄養・食糧学会大会講演要旨集  61st-  121  2007/04/20  [Not refereed][Not invited]
  
• 豚由来エラスチンペプチドの安全性について

  早川徹, 佐藤三佳子, 高畑能久, 森松文毅  日本栄養・食糧学会大会講演要旨集  61st-  262  2007/04/20  [Not refereed][Not invited]
  
• 鶏コラーゲン加水分解物の血管保全作用

  雑賀愛, 早川徹, 河口友美, 高畑能久, 森正文毅  日本栄養・食糧学会大会講演要旨集  61st-  267  2007/04/20  [Not refereed][Not invited]
  
• 豚由来エラスチンペプチドの摂取によるマウス皮膚粘弾性への影響

  早川徹, 佐藤三佳子, 高畑能久, 森松文毅, 野村義宏  日本畜産学会大会講演要旨  107th-  134  2007/03/27  [Not refereed][Not invited]
  
• トリ胸肉抽出物(CBEX)の経口投与がラットの脳内カルノシンおよびアンセリン含量に及ぼす影響

  友永省三, 早川徹, 山根春香, 前村公彦, 佐藤三佳子, 高畑能久, 森松文毅, 古瀬充宏  日本畜産学会大会講演要旨  107th-  4  2007/03/27  [Not refereed][Not invited]
  
• 鶏コラーゲン加水分解物(C‐COP)の血圧が高めの方に対する効果

  雜賀愛, 岩井浩二, 早川徹, 河口友美, 高畑能久, 森松文毅  日本農芸化学会大会講演要旨集  2007-  282  2007/03/05  [Not refereed][Not invited]
  
• アンチエイジングをターゲットとした畜産物由来の機能性食品

  早川徹  日本栄養・食糧学会中国・四国支部大会講演要旨集  40th-  23  2007  [Not refereed][Not invited]
  
• エラスチンペプチドの開発と機能性について

  早川徹, 佐藤三佳子, 雜賀愛, 高畑能久, 森松文毅  日本食肉研究会総会提出議案及び大会講演要旨  48th-  26  -31  2007  [Not refereed][Not invited]
  
• 新製品開発と新素材 15)機能性食品素材「P‐エラスチン」

  早川徹  Beverage Jpn  29-  (10)  76  -77  2006/10/20  [Not refereed][Not invited]
  
• トリ胸肉抽出物およびカルノシンの経口投与がマウスの学習行動に及ぼす影響

  友永省三, 早川徹, 及川大地, 佐藤三佳子, 高畑能久, 森松文毅, 橘哲也, 古瀬充宏  日本栄養・食糧学会総会講演要旨集  60th-  356  2006/04/01  [Not refereed][Not invited]
  
• 豚コラーゲンペプチドの血圧上昇抑制作用

  雜賀愛, 岩井浩二, 早川徹, 高畑能久, 森松文毅  日本栄養・食糧学会総会講演要旨集  60th-  375  2006/04/01  [Not refereed][Not invited]
  
• 鶏コラーゲン加水分解物の血圧上昇抑制作用(第2報)

  岩井浩二, 早川徹, 雑賀愛, 高畑能久, 森松文毅  日本畜産学会大会講演要旨  106th-  163  2006/03/20  [Not refereed][Not invited]
  
• 鶏コラーゲン加水分解物の血圧上昇抑制作用(第1報)

  雑賀愛, 岩井浩二, 早川徹, 高畑能久, 森松文毅  日本畜産学会大会講演要旨  106th-  163  2006/03/20  [Not refereed][Not invited]
  
• 中性低イオン強度下における鶏骨格筋ミオシンの挙動

  早川徹, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  104th-  168  2005/03/20  [Not refereed][Not invited]
  
• 鶏骨格筋ミオシンの低イオン強度下における挙動

  早川徹, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  103rd-  159  2004/03/20  [Not refereed][Not invited]
  

Presentations

• カルシウムの添加がヒスチジンによるミオシン水溶化作用を阻害する  [Not invited]

  早川 徹, 窪野 佑, 若松 純一, 玖村 朗人

  日本畜産学会第123回大会  2017/09
• L-ヒスチジンおよびイオン強度がミオシンの存在形態におよぼす影響  [Not invited]

  早川 徹, 若松 純一, 西邑 隆徳

  日本畜産学会第112回大会  2010/03
• 低イオン強度下におけるL-メロミオシン分子の性状に及ぼすL-ヒスチジンの影響  [Not invited]

  早川 徹, 若松 純一, 西邑 隆徳

  日本畜産学会第111回大会  2009/09
• Myosin filamment depolymerized in a low ionic strength solution containing L-histidine  [Not invited]

  Hayakawa, T, Wakamatsu, J, Nishimura, T, Hattori, A

  55th International Congress of Meat Science and Technology  2009/08
• L-ヒスチジンを含む低イオン強度溶液へのミオシン溶解機構の解明  [Not invited]

  早川 徹, 若松 純一, 西邑 隆徳, 服部 昭仁

  日本畜産学会第110回大会  2009/03
• 豚由来エラスチンペプチドの血管保全作用  [Not invited]

  早川 徹, 雑賀 愛, 河口 友美, 大森 丘, 高畑 能久, 森松 文毅

  日本畜産学会第109回大会  2008/03
• アンチエイジングをターゲットとした畜産物由来の機能性食品  [Not invited]

  早川 徹

  日本栄養・食糧学会 中四国・近畿支部大会  2007/11
• 豚由来エラスチンペプチドの経口摂取による光老化モデルマウス皮膚への影響  [Not invited]

  早川 徹, 佐藤 三佳子, 雑賀 愛, 高畑 能久, 森松 文毅, 野村 義宏

  日本畜産学会第108回大会  2007/09
• Functional properties of porcine aortic elastin peptide 'P-Elastin'  [Not invited]

  Hayakawa, T, Sato, M, Saiga, A, Takahata, Y, Morimatsu, F

  53rd International Congress of Meat Science and Technology  2007/08
• 豚由来エラスチンペプチドの安全性について  [Not invited]

  早川 徹, 佐藤 三佳子, 高畑 能久, 森松 文毅

  第61回日本栄養・食糧学会  2007/05
• 豚由来エラスチンペプチドの摂取によるマウス皮膚粘弾性への影響  [Not invited]

  早川 徹, 佐藤 三佳子, 高畑 能久, 森松 文毅, 野村 義宏

  日本畜産学会第107回大会  2007/03
• トリ胸肉抽出物（CBEX）の経口投与がマウスの学習行動に及ぼす影響  [Not invited]

  早川 徹, 友永 省三, 及川 大地, 佐藤 三佳子, 高畑 能久, 森松 文毅, 橘 哲也, 古瀬 充宏

  日本抗加齢学会  2006/05
• 中性低イオン強度下における鶏骨格筋ミオシンの挙動  [Not invited]

  早川 徹, 若松 純一, 西邑 隆徳, 服部 昭仁

  日本畜産学会第104回大会  2005/03
• Behavior of chicken breast muscle myosin solubilized in neutral and low ionic strength solution  [Not invited]

  Hayakawa, T, Wakamatsu, J, Nishimura, T, Hattori, A

  50th International Congress of Meat Science and Technology  2004/08
• 鶏骨格筋ミオシンの低イオン強度下における挙動  [Not invited]

  早川 徹, 若松 純一, 西邑 隆徳, 服部 昭仁

  日本畜産学会第103回大会  2004/03

Research Projects

• イミダゾールジペプチドの死後骨格筋における生理機能の解明

  日本学術振興会：科学研究費助成事業 基盤研究(C)

  Date (from‐to) : 2022/04 -2027/03 

  Author : 早川 徹
• イミダゾール化合物との相互作用によるミオシン分子機能への影響

  日本学術振興会：科学研究費補助金 若手研究

  Date (from‐to) : 2018/04 -2021/03 

  Author : 早川 徹
• 中性低イオン強度下における鶏骨格筋ミオシンの溶解機構の解明

  日本学術振興会：特別研究員奨励費

  Date (from‐to) : 2009/04 -2011/03 

  Author : 早川 徹