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Wakamatsu Jun-ichi

Research Faculty of Agriculture Fundamental AgriScience Research Animal ScienceProfessor

Researcher basic information

■ Degree
  • 博士(農学), 北海道大学, Dec. 2002
■ URL
researchmap URLホームページURL■ Various IDs
J-Global ID■ Research Keywords and Fields
Research Keyword
  • Diet-induced thermogenesis
  • パルマハム
  • 亜鉛プロトポルフィリンIX
  • 食肉製品
  • プロトポルフィリンIX
  • 亜鉛
  • ヘム
  • 筋原線維
  • タンパク質
  • 食肉
  • ペプチド
  • 筋原線維タンパク質
  • 機能性物質
  • 食肉タンパク質
  • 食肉利用学
  • 食肉生化学
Research Field
  • Life Science, Animal production science
  • Life Science, Food sciences
  • Humanities & Social Sciences, Family and consumer sciences, and culture and living
■ Educational Organization

Career

■ Career
Career
  • Apr. 2024 - Present
    Hokkaido University, Graduate School of Agriculture Research Faculty of Agriculture Division of Applied Bioscience, Professor
  • Apr. 2021 - Mar. 2024
    Hokkaido University, Graduate School of Agriculture Research Faculty of Agriculture Division of Applied Bioscience, Associate Professor
  • Jan. 2013 - Mar. 2021
    Hokkaido Univ., 北方生物圏フィールド科学センター, Associate professor
  • Jul. 2012 - Dec. 2012
    Hokkaido Univ., Associate Professor
  • Apr. 2007 - Jun. 2012
    Hokkaido Univ., Assistant Professor
  • May 2002 - Mar. 2007
    Hokkaido Univ., Assistant Professor
  • Apr. 1994 - May 2002
    Itoham Inc., 研究員
Educational Background
  • Apr. 1992 - Mar. 1994, 北海道大学大学院, 農学研究科, 畜産学専攻
  • Apr. 1986 - Mar. 1992, Hokkaido Univ., 農学部, 畜産学科
Committee Memberships
  • Apr. 2025 - Present
    北海道畜産草地学会, 評議員, Society
  • Apr. 2023 - Present
    北海道環境生活部, エゾシカ肉品質管理のための検討懇話会, Autonomy
  • Apr. 2015 - Present
    日本食肉科学会, 広報委員, Society
  • Apr. 2015 - Present
    日本食肉科学会, 常務理事, Society
  • Apr. 2023 - Mar. 2025
    北海道畜産草地学会, 会計幹事, Society
  • 2015 - Mar. 2025
    日本畜産学会, 機関紙編集委員, Society
  • Oct. 2017 - Mar. 2019
    北海道環境生活部, エゾシカわな捕獲技術等検討会委員, Autonomy
  • Apr. 2015 - Mar. 2019
    日本食肉科学会, 評議員, Society
  • Apr. 2014 - Mar. 2015
    北海道畜産草地学会, 監事, Society
  • Apr. 1998 - Mar. 2015
    日本食肉研究会, 編集幹事, Society
  • Dec. 2012 - Mar. 2014
    北海道畜産草地学会, 会計幹事, Society
  • Apr. 2010 - Dec. 2012
    北海道畜産学会, 会計幹事, Society
  • Apr. 2007 - Mar. 2009
    日本食肉研究会, 庶務幹事, Society

Research activity information

■ Awards
  • Jun. 2016, The Ito Foundation, Ito Foundation Award
    WAKAMATSU Jun-ichi
  • 2008, 畜産技術協会賞
    Japan
■ Papers
  • Maintaining a neutral range disperses myosin molecules under salt-free conditions.
    Toru Hayakawa; Yu Shishido; Yuki Ikeuchi; Jun-Ichi Wakamatsu; Haruto Kumura
    Journal of biochemistry, 178, 3, 209, 215, 03 Sep. 2025, [Peer-reviewed], [International Magazine]
    English, Scientific journal, Skeletal muscle myosin is generally considered insoluble under physiological, low ionic strength, or salt-free conditions due to its tendency to self-assemble into filamentous polymers in vitro. Our previous study showed that myosin can be solubilized in low ionic strength solutions containing l-histidine. However, another report suggested that 1-methylhistidine could not solubilize myosin, and the factors essential for myosin solubilization remain unclear. To elucidate the role of l-histidine in the water solubilization of myosin, we examined myosin solubility and the molecular properties of its rod domain, l-meromyosin, using structurally related buffer compounds. Under salt-free conditions, solubility depended heavily on the acid dissociation constant of buffer, indicating that maintaining a neutral pH is critical. The rod domain showed molecular elongation regardless of the buffer type, yet surface charge and hydrophobicity remained comparable to conditions with high ionic strength. These results suggest that myosin is inherently soluble and maintains its structural integrity under neutral, salt-free conditions. The apparent insolubility under such conditions is likely to result from hydrochloric acid used for pH adjustment. Since l-histidine and imidazole achieve neutrality without acid addition, they are ideal buffers for myosin solubilization.
  • Evaluation of postprandial thermal feeling in mice using a behavioral thermoregulation analysis: Differences in meat species and their fractions
    Jun-ichi Wakamatsu; Yeying Tan; Seiya Kato; Haruka Abe; Manabu Kawahara; Toru Hayakawa; Haruto Kumura
    Journal of Thermal Biology, 129, 104101, Apr. 2025, [Peer-reviewed], [Lead author, Corresponding author]
    English, Scientific journal
  • Application of glucose to prepare Aspergillus oryzae koji as an adjunct to prevent rancidity in cheese products.
    Napaporn Chintagavongse; Tomohiro Mitani; Koichi Tamano; Toru Hayakawa; Jun-Ichi Wakamatsu; Haruto Kumura
    Bioscience, Biotechnology, and Biochemistry, 89, 2, 275, 283, 28 Nov. 2024, [Peer-reviewed], [International Magazine]
    English, Scientific journal, Koji made using Aspergillus oryzae shows potential for application as a cheese adjunct; however, flavor defects resulting from volatile free fatty acid (FFA) accumulation should be avoided. Hence, a modified glucose-containing whey solid medium was used to culture A. oryzae AHU 7139, and the triacylglycerol (TG) lipase activity and lipase gene (tglA and mdlB) expression were compared with those of a culture using a conventional whey solid medium. The results showed that TG lipase activity and the expression of both lipase genes were reduced in the modified medium. Moreover, the expression level of farA, a positive transcription factor of the lipase genes, was also reduced. The cheese adjunct prepared by culturing the AHU 7139 strain in the modified medium lowered the FFA content in the cheese products, resulting in comparable FFA levels with those in the adjunct-free cheese. Thus, adding glucose is recommended to prepare the koji adjunct for cheesemaking.
  • 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, 137, 5, 381, 387, 01 Mar. 2024, [Peer-reviewed], [Domestic magazines]
    English, Scientific journal, 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.
  • Zinc Protoporphyrin-Rich Pork Liver Homogenates as Coloring Ingredients in Nitrite-Free Liver Pâtés
    Mar Llauger; Luis Guerrero; Jacint Arnau; Afra Morera; Jun-ichi Wakamatsu; Jose Manuel Lorenzo Rodriguez; RICARD BOU
    Foods, 13, 4, 533, 09 Feb. 2024, [Peer-reviewed]
    English, Scientific journal
  • 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, 02 Jan. 2024, [Peer-reviewed], [Last author, Corresponding author], [International Magazine]
    English, Scientific journal, 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, 30 Nov. 2023, [Peer-reviewed], [Last author, Corresponding author], [International Magazine]
    English, Scientific journal, 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.
  • 銃捕獲した野生エゾシカの肉質に及ぼす被弾部位と口径の影響
    桒子和洋; 近藤誠司; 木富正裕; 亀井利活; 稲富佳洋; 河合正人; 日置昭二; 鳥羽悠; 早川徹; 玖村朗人; 若松純一
    食肉の科学, 64, 1, 29, 38, Jun. 2023, [Peer-reviewed], [Last author, Corresponding author]
    Japanese, Scientific journal
  • 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, Jun. 2023, [Peer-reviewed], [International Magazine]
    English, Scientific journal, 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 = Nihon chikusan Gakkaiho, 94, 1, e13825, 2023, [Peer-reviewed], [International Magazine]
    English, Scientific journal, The heat-induced gelation of actomyosin plays a key role in meat processing. Our previous study showed that L-histidine could affect the characteristics of a heat-induced gel of myosin on a low ionic strength. To apply the specific effect of L-histidine to meat processing, the heat-induced gel properties of actomyosin in the presence of L-histidine were investigated. Actomyosin in a low ionic strength solution containing L-histidine did not form a gel upon heating. The dynamic rheological properties of actomyosin in low ionic strength solutions were distinct depending on the presence or absence of L-histidine. Electron microscopy showed that, heated at 50°C, actomyosin in a low ionic strength solution containing L-histidine remained a filamentous structure. The surface hydrophobicity of actomyosin was stable up to 50°C in a low ionic strength solution containing L-histidine. In conclusion, L-histidine might suppress the aggregation of actomyosin and inhibit heat-induced gelation in a low ionic strength solution.
  • 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, 30 Nov. 2022, [Last author, Corresponding author], [International Magazine]
    English, Scientific journal, 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.
  • Evidence of the mechanism underlying zinc protoporphyrin IX formation in nitrite/nitrate-free dry-cured Parma ham.
    Jun-Ichi Wakamatsu
    Meat science, 192, 108905, 108905, Oct. 2022, [Peer-reviewed], [Invited], [Lead author, Corresponding author], [International Magazine]
    English, Scientific journal, A large amount of zinc protoporphyrin IX (ZnPP) is found in nitrite/nitrate-free dry-cured meat products, such as Parma ham, and is known to contribute to the favorable bright red color of the latter. ZnPP is a metalloporphyrin, in which zinc is coordinated, instead of iron, in the porphyrin ring. ZnPP proved to be more stable than heme, and its formation should be favored in dried meat products to improve color without the addition of nitrites or nitrates. Toward that, understanding the mechanisms of formation of ZnPP in nitrite/nitrate-free dry-cured ham would be important. In this lecture, I introduce some of our research group's findings regarding the endogenous and exogenous factors contributing to the formation and distribution of ZnPP in Parma ham and why ZnPP formation is suppressed in common cured meat products.
  • 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, 23 Jan. 2022, [Peer-reviewed], [International Magazine]
    English, Scientific journal, 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, Elsevier BV, Apr. 2021, [Peer-reviewed], [Last author, Corresponding author]
    English, Scientific journal
  • 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, 19 Feb. 2021, [Peer-reviewed], [Last author, Corresponding author], [International Magazine]
    English, Scientific journal, 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.
  • 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, 31 Oct. 2020, [Peer-reviewed], [Last author, Corresponding author], [International Magazine]
    English, Scientific journal, 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.
  • 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, Jul. 2020, [Peer-reviewed], [Last author, Corresponding author], [International Magazine]
    English, Scientific journal, 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.
  • Adjunctive application of solid-state culture products and its freeze-dried powder from Aspergillus sojae for semihard cheese.
    Chintagavongse N; Yoneda T; Ming-Hsuan C; Hayakawa T; Wakamatsu JI; Tamano K; Kumura H
    Journal of the Science of Food and Agriculture, 100, 13, 4834, 4839, Jun. 2020, [Peer-reviewed], [International Magazine]
    English, Scientific journal, BACKGROUND: Some species belonging to the genus Aspergillus have been used in traditional Japanese fermentation foods. A. sojae is the species responsible for high proteolytic activity. Freeze-drying treatments followed by physical disruption enables the pulverisation of mycelia of A. sojae RIB 1045 grown in whey protein base solid media. Through this protocol, intracellular proteases were extracted to compare extracellular protease activity in terms of the reaction pH dependence in the presence or absence of the inhibitors. RESULT: With different sensitivities to inhibitors, intracellular and extracellular proteases showed the highest activity under the acidic region, which was 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 and were allowed to ripen for three 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 were found in CP and FDP experimental cheese, 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: An 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 degree of WSN compared with A. oryzae, as shown in our previous study. This article is protected by copyright. All rights reserved.
  • 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
    日本畜産学会報, 91, 4, 389, 394, 2020, [Peer-reviewed], [Last author, Corresponding author]
    Japanese, Scientific journal
  • 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, Oct. 2019, [Peer-reviewed], [Last author, Corresponding author], [International Magazine]
    English, Scientific journal, 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, Aug. 2019, [Peer-reviewed]
    English, Scientific journal
  • 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, Wiley, Jun. 2019, [Peer-reviewed], [Last author, Corresponding author]
    English, Scientific journal
  • Optimal pH of zinc protoporphyrin IX formation in porcine muscles: Effects of muscle fiber type and myoglobin content
    Jun-ichi Wakamatsu; Mofassara Akter; Fumika Honma; Toru Hayakawa; Haruto Kumura; Takanori Nishimura
    LWT, 101, 599, 606, Elsevier {BV}, Mar. 2019, [Peer-reviewed], [Lead author, Corresponding author]
    Scientific journal
  • Application of red pigment producing edible fungi for development of a novel type of functional cheese
    Kumura, H.; Ohtsuyama, T.; Matsusaki, Y.-H.; Taitoh, M.; Koyanagi, H.; Kobayashi, K.; Hayakawa, T.; Wakamatsu, J.-I.; Ishizuka, S.
    Journal of Food Processing and Preservation, 42, 10, 2018, [Peer-reviewed]
    Scientific journal
  • Myosin substitution rate is affected by the amount of cytosolic myosin in cultured muscle cells
    Koichi Ojima; Emi Ichimura; Yuya Yasukawa; Mika Oe; Susumu Muroya; Takahiro Suzuki; Jun-ichi Wakamatsu; Takanori Nishimura
    ANIMAL SCIENCE JOURNAL, 88, 11, 1788, 1793, Nov. 2017, [Peer-reviewed]
    English, Scientific journal
  • Enhancement of sperm motility and viability by turmeric by-product dietary supplementation in roosters
    Wenjing Yan; Chihiro Kanno; Eiki Oshima; Yukiko Kuzuma; Sung Woo Kim; Hanako Bai; Masashi Takahashi; Yojiro Yanagawa; Masashi Nagano; Jun-ichi Wakamatsu; Manabu Kawahara
    ANIMAL REPRODUCTION SCIENCE, 185, 195, 204, Oct. 2017, [Peer-reviewed]
    English, Scientific journal
  • ターメリック製造副産物の給与がニワトリ精子運動能に及ぼす影響
    厳 文静; 菅野 智裕; 葛間 風花子; 大嶋 栄喜; 唄 花子; 高橋 昌志; 柳川 洋二郎; 永野 昌志; 若松 純一; 川原 学
    北海道畜産草地学会報, 4, 2, 26, 26, 北海道畜産草地学会, Aug. 2016
    Japanese
  • Diet-Induced Thermogenesis and Expression Levels of Thyroid Hormone Target Genes and Their Products in Rats Differ between Meat Proteins
    Misako Ezoe; Jun-ichi Wakamatsu; Yoshihisa Takahata; Takanori Hasegawa; Fumiki Morimatsu; Takanori Nishimura
    JOURNAL OF NUTRITIONAL SCIENCE AND VITAMINOLOGY, 62, 2, 93, 100, Apr. 2016, [Peer-reviewed], [Corresponding author]
    English, Scientific journal
  • Effect of zinc protoporphyrin IX on dietary zinc bioavailability
    WAKAMATSU JUN'ICHI; KATO AYANA; EZOE MISAKO; NISHIMURA TAKANORI
    日本畜産学会報, 86, 4, 481, 489, 25 Nov. 2015, [Peer-reviewed], [Lead author, Corresponding author]
    Japanese
  • Dynamics of myosin replacement in skeletal muscle cells
    Koichi Ojima; Emi Ichimura; Yuya Yasukawa; Jun-ichi Wakamatsu; Takanori Nishimura
    AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY, 309, 10, C669, C679, Nov. 2015, [Peer-reviewed]
    English, Scientific journal
  • 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, Aug. 2015, [Peer-reviewed]
    English, Scientific journal
  • A comparative study of zinc protoporphyrin IX-forming properties of animal by-products as sources for improving the color of meat products
    Jun-ichi Wakamatsu; Naoko Murakami; Takanori Nishimura
    ANIMAL SCIENCE JOURNAL, 86, 5, 547, 552, May 2015, [Peer-reviewed], [Lead author, Corresponding author]
    English, Scientific journal
  • Comparative study of muscle regeneration following cardiotoxin and glycerol injury
    Mohamed A. A. Mahdy; Hsiao Yin Lei; Jun-Ichi Wakamatsu; Yoshinao Z. Hosaka; Takanori Nishimura
    ANNALS OF ANATOMY-ANATOMISCHER ANZEIGER, 202, 18, 27, 2015, [Peer-reviewed]
    English, Scientific journal
  • Postprandial Thermic Effect of Chicken Involves Thyroid Hormones and Hepatic Energy Metabolism in Rats
    Jun-ichi Wakamatsu; Naomasa Takabayashi; Misako Ezoe; Takanori Hasegawa; Tatsuya Fujimura; Yoshihisa Takahata; Fumiki Morimatsu; Takanori Nishimura
    JOURNAL OF NUTRITIONAL SCIENCE AND VITAMINOLOGY, 59, 6, 516, 525, Dec. 2013, [Peer-reviewed], [Lead author, Corresponding author]
    English, Scientific journal
  • Decorin activates Akt downstream of IGF-IR and promotes myoblast differentiation
    Keisuke Suzuki; Yasuhiro Kishioka; Jun-Ichi Wakamatsu; Takanori Nishimura
    Animal Science Journal, 84, 9, 669, 674, Sep. 2013, [Peer-reviewed]
    English, Scientific journal
  • Laminin binds to myostatin and attenuates its signaling
    Naofumi Yasaka; Keisuke Suzuki; Yasuhiro Kishioka; Jun-ichi Wakamatsu; Takanori Nishimura
    ANIMAL SCIENCE JOURNAL, 84, 9, 663, 668, Sep. 2013, [Peer-reviewed]
    English, Scientific journal
  • Effects of meat species on the postprandial thermic effect in rats
    Jun-ichi Wakamatsu; Ryoji Fujii; Kimikazu Yamaguchi; Syouhei Miyoshi; Takanori Nishimura; Akihito Hattori
    ANIMAL SCIENCE JOURNAL, 84, 5, 416, 425, 2013, [Peer-reviewed], [Lead author, Corresponding author]
    English, Scientific journal
  • Myostatin regulates proliferation and extracellular matrix mRNA expression in NIH3T3 fibroblasts
    Yoshinao Z. Hosaka; Mika Ishibashi; Jun-ichi Wakamatsu; Masato Uehara; Takanori Nishimura
    BIOMEDICAL RESEARCH-TOKYO, 33, 6, 355, 361, Dec. 2012, [Peer-reviewed]
    English, Scientific journal
  • 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, Jan. 2012, [Peer-reviewed]
    English, Scientific journal
  • Effect of liquid straight whey feeding on reproductive performance, productivity and carcass characteristics of pigs in a commercial pig farm
    TAKAHAGI YOICHI; IWABUCHI OSAMU; SUKEGAWA SHIN; NAKAEBISU TAKASHI; KOSHIDA YUZO; WAKAMATSU JUN'ICHI; FUJIMURA TATSUYA; ISHIGURO TOMOKO; MURAKAMI HIROSHI; IIMURA YUJI; KOBAYASHI YASUO; MORIMATSU FUMIKI; KAWASHIMA TOMOYUKI; HISHINUMA TAKESHI
    日本畜産学会報, 82, 3, 325, 331, Japanese Society of Animal Science, Aug. 2011, [Peer-reviewed]
    Japanese, An enormous amount of whey is discharged from daily factories, and farms in which pigs are fed with whey are increasing because of its high protein content and nutritive value. However, effects of whey feeding have not been fully investigated. In the present study, we investigated the reproductive performance, the productivity and the carcass characteristics of pigs fed with commercial formula feed supplemented with liquid straight whey. Sows were fed with three to five L of liquid straight whey per day per head. Litter size, rate of return to estrus within seven days and conception rate of whey-fed sows were significantly higher than those of control sows : they improved by 0.2 heads (P < 0.001), 3.2% (P < 0.05) and 3.4% (P < 0.001), respectively, in whey-fed sows. One point three to 1.5 L per day per head of liquid straight whey was fed to fattening pigs. Shipping age of whey-fed pigs was significantly younger than that of control pigs (3.4 days, P < 0.05). Significant differences in the carcass characteristics between whey-fed and control pigs were not observed. Meanwhile, when 0.2 L per day per head of liquid straight whey was fed to pigs only in the weaning period, shipping age and daily gain were not improved in whey-fed pigs. Significant differences in the carcass characteristics were not observed either. These results showed that liquid straight whey feeding is effective in improving the reproductive performance of sows in a commercial pig farm. Improvement of productivity was also observed when whey was fed to fattening pigs.
  • Effect of liquid whey feeding on fecal microbiota of mature and growing pigs
    Yasuo Kobayashi; Aya Itoh; Kanae Miyawaki; Satoshi Koike; Osamu Iwabuchi; Yuji Iimura; Yuri Kobashi; Tomoyuki Kawashima; Junichi Wakamatsu; Akihito Hattori; Hiroshi Murakami; Fumiki Morimatsu; Takashi Nakaebisu; Takeshi Hishinuma
    ANIMAL SCIENCE JOURNAL, 82, 4, 607, 615, 2011, [Peer-reviewed]
    English, Scientific journal
  • 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, Apr. 2010, [Peer-reviewed]
    English, Scientific journal
  • Interaction between myostatin and extracellular matrix components
    Takayuki Miura; Yasuhiro Kishioka; Jun-ichi Wakamatsu; Akihito Hattori; Takanori Nishimura
    ANIMAL SCIENCE JOURNAL, 81, 1, 102, 107, 2010, [Peer-reviewed]
    English, Scientific journal
  • Nitric oxide inhibits the formation of zinc protoporphyrin IX and protoporphyrin IX
    Jun-ichi Wakamatsu; Nobutaka Hayashi; Takanori Nishimura; Akihito Hattori
    MEAT SCIENCE, 84, 1, 125, 128, Jan. 2010, [Peer-reviewed], [Lead author, Corresponding author]
    English, Scientific journal
  • Effect of L-histidine and ionic strength on disassembly of myosin filaments
    Proceeding ICoMST2010, B026, 2010
    English, International conference proceedings
  • Thermic effect of chicken
    Proceeding ICoMST2010, B026, 2010
    English, International conference proceedings
  • Effects of liquid whey supplement on the productivity of pigs in a commercial pig farm
    KOBASHI Yuri; ISHIGURO Tomoko; WAKAMATSU Junichi; OKUMURA Tomoyuki; TAKAHAGI Yoichi; IWABUCHI Osamu; IIMURA Yuji; KAWASHIMA Tomoyuki; KOBAYASHI Yasuo; HATTORI Akihito; MURAKAMI Hiroshi; MORIMATSU Fumiki
    Nihon Chikusan Gakkaiho, 80, 4, 443, 450, 社団法人日本畜産学会, Nov. 2009, [Peer-reviewed]
    Japanese, The productivity of pigs given commercial formula feed supplemented with liquid whey, which was discharged from a dairy factory, was examined. A total of 66 weaned piglets from 9 litters were divided into the group of pigs given commercial formula feed supplemented with liquid whey (Whey) and the group given commercial formula feed alone (CN), considering possible hereditary interference. A total of 267 L of liquid whey was given per animal. Body weight was measured periodically. The blood sample was taken to compare innate immune function between the Whey group and CN group immediately before shipment of pigs. Mean body weight at ages of 65 days and 173 days was significantly higher in the Whey group than in the CN group (P < 0.05). Daily weight gain was significantly higher in the Whey group at ages from 29 to 65 days (P < 0.01) and from 105 to 173 days (P < 0.05), as compared with the control group. There were no significant differences in carcass traits of meat quality or innate immune function between the Whey group and the CN group. These results showed that liquid whey supplement allows acceleration of age at slaughter without affecting carcass traits or meat quality and is useful in improving the productivity of pigs.
  • 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, Jun. 2009, [Peer-reviewed]
    English, Scientific journal
  • Quantitative determination of Zn protoporphyrin IX, heme and protoporphyrin IX in Parma ham by HPLC
    Jun-ichi Wakamatsu; Hiroko Odagiri; Takanori Nishimura; Akihito Hattori
    MEAT SCIENCE, 82, 1, 139, 142, May 2009, [Peer-reviewed]
    English, Scientific journal
  • Formation of zinc protoporphyrin IX in Parma-like ham without nitrate or nitrite
    Jun-Ichi Wakamatsu; Juichi Uemura; Hiroko Odagiri; Jun Okui; Nobutaka Hayashi; Shoji Hioki; Takanori Nishimura; Akihito Hattori
    ANIMAL SCIENCE JOURNAL, 80, 2, 198, 205, Apr. 2009, [Peer-reviewed]
    English, Scientific journal
  • Relationships between physical and structural properties of intramuscular connective tissue and toughness of raw pork
    Takanori Nishimura; Suhong Fang; Jun-ichi Wakamatsu; Koui Takahashi
    ANIMAL SCIENCE JOURNAL, 80, 1, 85, 90, Feb. 2009, [Peer-reviewed]
    English, Scientific journal
  • Structural weakening of intramuscular connective tissue during postmortem aging of pork
    Takanori Nishimura; Suhong Fang; Toshiaki Ito; Jun-ichi Wakamatsu; Koui Takahashi
    ANIMAL SCIENCE JOURNAL, 79, 6, 716, 721, Dec. 2008, [Peer-reviewed]
    English, Scientific journal
  • Decorin enhances the proliferation and differentiation of myogenic cells through suppressing myostatin activity
    Yasuhiro Kishioka; Mark Thomas; Jun-Ichi Wakamatsu; Akihito Hattori; Mridula Sharma; Ravi Kambadur; Takanori Nishimura
    JOURNAL OF CELLULAR PHYSIOLOGY, 215, 3, 856, 867, Jun. 2008, [Peer-reviewed]
    English, Scientific journal
  • Decorin expression in quiescent myogenic cells
    Takanori Nishimura; Kenjiro Nozu; Yasuhiro Kishioka; Jun-ichi Wakamatsu; Akihito Hattori
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 370, 3, 383, 387, Jun. 2008, [Peer-reviewed]
    English, Scientific journal
  • Inhibition of matrix metalloproteinases suppresses the migration of skeletal muscle cells
    Takanori Nishimura; Kazuki Nakamura; Yasuhiro Kishioka; Yuko Kato-Mori; Jun-ichi Wakamatsu; Akihito Hattori
    JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY, 29, 1, 37, 44, Jan. 2008, [Peer-reviewed]
    English, Scientific journal
  • Zn protoporphyrin IX is formed not from heme but from protoporphyrin IX
    Jun-ichi Wakamatsu; Jun Okui; Nobutaka Hayashi; Takanori Nishimura; Akihito Hattori
    MEAT SCIENCE, 77, 4, 580, 586, Dec. 2007, [Peer-reviewed]
    English, Scientific journal
  • Spatiotemporal expression of decorin and myostatin during rat skeletal muscle development
    Takanori Nishimura; Kohei Oyama; Yasuhiro Kishioka; Jun-ichi Wakamatsu; Akihito Hattori
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 361, 4, 896, 902, Oct. 2007, [Peer-reviewed]
    English, Scientific journal
  • Direct demonstration of the presence of zinc in the acetone-extractable red pigment from Parma ham
    Jun-ichi Wakamatsu; Toshiaki Ito; Takanori Nishimura; Akihito Hattori
    MEAT SCIENCE, 76, 2, 385, 387, Jun. 2007, [Peer-reviewed]
    English, Scientific journal
  • Observation of the distribution of Zn protoporphyrin IX (ZPP) in Parma ham by using purple LED and image analysis
    J. Wakamatsu; H. Odagiri; T. Nishimura; A. Hattori
    MEAT SCIENCE, 74, 3, 594, 599, Nov. 2006, [Peer-reviewed]
    English, Scientific journal
  • Decorin binds myostatin and modulates its activity to muscle cells
    T Miura; Y Kishioka; J Wakamatsu; A Hattori; A Hennebry; CJ Berry; M Sharma; R Kambadur; T Nishimura
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 340, 2, 675, 680, Feb. 2006, [Peer-reviewed]
    English, Scientific journal
  • Species and muscle differences in L-carnitine levels in skeletal muscles based on a new simple assay
    K Shimada; Y Sakuma; J Wakamatsu; M Fukushima; M Sekikawa; K Kuchida; M Mikami
    MEAT SCIENCE, 68, 3, 357, 362, Nov. 2004, [Peer-reviewed]
    English, Scientific journal
  • Establishment of a model experiment system to elucidate the mechanism by which Zn-protoporphyrin IX is formed in nitrite-free dry-cured ham
    J Wakamatsu; J Okui; Y Ikeda; T Nishimura; A Hattori
    MEAT SCIENCE, 68, 2, 313, 317, Oct. 2004, [Peer-reviewed]
    English, Scientific journal
  • A Zn-porphyrin complex contributes to bright red color in Parma ham
    J Wakamatsu; T Nishimura; A Hattori
    MEAT SCIENCE, 67, 1, 95, 100, May 2004, [Peer-reviewed]
    English, Scientific journal
  • Physicochemical properties of water-soluble myofibrillar proteins prepared from chicken breast muscle
    Yukiko Ito; Shinji Toki; Takashi Omori; Hiroshi Ide; Ryuichi Tatsumi; Jun-Ichi Wakamatsu; Takanori Nishimura; Akihito Hattori
    Animal Science Journal, 75, 1, 59, 65, Feb. 2004, [Peer-reviewed]
    English, Scientific journal
  • Effect of skeletal muscle decorin on collagen fibrillogenesis in vitro
    Takanori Nishimura; Ayaka Taneichi; Jun-Ichi Wakamatsu; Akihito Hattori
    Animal Science Journal, 74, 5, 399, 405, Oct. 2003, [Peer-reviewed]
    English, Scientific journal
  • The solubilization of myofibrillar proteins of vertebrate skeletal muscle in water
    Yukiko Ito; Ryuichi Tatsumi; Jun-Ichi Wakamatsu; Takanori Nishimura; Akihito Hattori
    Animal Science Journal, 74, 5, 417, 425, Oct. 2003, [Peer-reviewed]
    English, Scientific journal
  • Identification and characterization of proteoglycans in bovine neonatal skeletal muscle
    Takanori Nishimura; Eiko Futami; Jun-Ichi Wakamatsu; Akihito Hattori
    Animal Science Journal, 74, 5, 407, 416, Oct. 2003, [Peer-reviewed]
    English, Scientific journal
  • Localization of paratropomyosin in chicken skeletal muscle myofibrils and its behavior during postmortem storage of muscles revealed by immunoelectron microscopy
    A Hattori; S Fujimoto; T Nishimura; R Tatsumi; J Wakamatsu; T Ito
    JOURNAL OF MUSCLE FOODS, 14, 1, 1, 10, Mar. 2003, [Peer-reviewed]
    English, Scientific journal
  • Presence of ubiquitin in bovine post-mortem cardiac muscle
    M Sekikawa; K Shimada; M Fukushima; T Ishikawa; J Wakamatsu; M Mikami
    FOOD CHEMISTRY, 69, 3, 315, 318, May 2000, [Peer-reviewed]
    English, Scientific journal
  • Anti-Fatigue Effects of Beef
    WAKAMATSU Jun-ichi; NAGAO Tetsuji; NUMATA Masahiro; NAKAMURA Toyoo; FUJIMAKI Masao
    Nihon Chikusan Gakkaiho, 68, 6, 579, 586, 社団法人 日本畜産学会, Jun. 1997, [Peer-reviewed]
    Japanese, Scientific journal, The present in vivo study investigated whether beef intake can reduce fatigue of mice by examining exercise load. There was no difference in body weight of all mice in the experimental groups for 5 weeks. There were also no significant differences in the changes of dietary intake among the groups either. The long-term intake of beef and/or beef tallow did not negatively influence mice with regard to appearance, transition of body weight and food intake. The swimming time of mice fed Beef+Beef tallow (BT) was significantly prolonged (p<0.05). That of mice fed Casein+BT tended to be prolonged, but was not significantly different from that of the control (fed Casein+soybean oil (SO)). The hanging time in 3min after forced swimming in mice fed Beef+BT and Casein+BT was significantly prolonged (p<0.05). In 30min after forced swimming, only mice fed Beef+BT showed a significantly prolonged hanging time compared to that of controls (p<0.05). These results suggested that beef, especially lean meat may have an anti-fatigue effect. The glucose and L-lactic acid levels in plasma of mice fed the casein diet remarkably reduced compared to the levels prior to exercise. In the Beef+BT-fed mice, the preexercise glucose level equalled and the pre-exercise and L-lactic acid level was slightly increased compared to the post-exercise levels. The changes in these parameters in the Beef+BT-fed group were less than those in the control group.
  • ''Hanpen''-like whipped sausage: Its sensory evaluation and texture
    J Wakamatsu; M Numata; T Nakamura
    JOURNAL OF THE JAPANESE SOCIETY FOR FOOD SCIENCE AND TECHNOLOGY-NIPPON SHOKUHIN KAGAKU KOGAKU KAISHI, 44, 7, 516, 521, 1997, [Peer-reviewed]
    Japanese, Scientific journal
  • CHARACTERIZATION OF A NOVEL 550-KDA PROTEIN IN SKELETAL-MUSCLE OF CHICK-EMBRYO
    A HATTORI; J WAKAMATSU; T ISHII; K KUWAHARA; R TATSUMI
    BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 1245, 2, 201, 206, Oct. 1995, [Peer-reviewed]
    English, Scientific journal
  • A NOVEL 550-KDA PROTEIN IN SKELETAL-MUSCLE OF CHICK-EMBRYO - PURIFICATION AND LOCALIZATION
    A HATTORI; J WAKAMATSU; T ISHII; K KUWAHARA; R TATSUMI
    BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 1245, 2, 191, 200, Oct. 1995, [Peer-reviewed]
    English, Scientific journal
■ Other Activities and Achievements
■ Books and other publications
  • 乳肉卵の機能と利用
    玖村 朗人; 若松 純一; 八田 一; 朝隈 貞樹
    アイ・ケイコーポレーション, 2018, 9784874923542, Japanese
  • 肉の機能と科学
    若松 純一
    朝倉出版, Apr. 2015, 9784254435504, Japanese, [Contributor]
  • Frontiers of Agricultural Science
    WAKAMATSU Jun-ichi
    Shoukadoh Book Sellers, 2015, [Contributor]
  • 最新 畜産ハンドブック
    若松 純一, 9.2 食肉の構造・品質と加工品
    講談社, Jul. 2014, 9784061537392, Japanese, [Contributor]
  • 畜産物利用学
    齋藤 忠夫; 根岸 晴夫; 八田 一
    文永堂出版, 2011, 9784830041211, Japanese, [Contributor]
  • 食肉用語事典
    日本食肉研究会
    食肉通信社, 2010, 9784879881137, Japanese, [Contributor]
  • 栄養・食糧学用語辞典
    日本栄養食糧学会
    建帛社, 2007, 9784767961125, Japanese, [Contributor]
  • 畜産食品の事典
    細野 明義; 沖谷 明紘; 吉川 正明; 八田 一
    朝倉書店, 2007, 9784254431001, Japanese, [Contributor]
  • 乳肉卵の機能と利用
    阿久澤 良造; 坂田 亮一; 島崎 敬一; 服部 昭仁
    アイ・ケイコーポレーション, 2005, 4874922236, Japanese, [Joint work]
  • 畜産食品の事典
    細野 明義; 沖谷 明紘; 吉川 正明; 八田 一
    朝倉書店, 2002, 4254430795, Japanese, [Contributor]
  • 食品機能素材 2
    太田 明一
    シーエムシー, 2001, 488231312X, Japanese, [Contributor]
  • ハム・ソーセージ図鑑
    ハム・ソーセージ図鑑編集委員; 伊藤記念財団
    伊藤記念財団, 2001, Japanese, [Contributor]
  • 食品機能素材 4
    太田 明一
    シーエムシー, 9784781301969, Japanese
  • 食品機能素材 3
    太田 明一
    シーエムシー, 4882315386, Japanese
■ Lectures, oral presentations, etc.
  • 肉のかたさを科学的に考えてみよう!
    若松 純一
    北海道食文化研究会第7回セミナー, 14 Jun. 2018, Japanese, Public discourse
    [Invited], [Domestic Conference]
  • 肉を食べたい! 微生物の戦いと葛藤
    若松 純一
    北海道食文化研究会第4回セミナー, 08 Jun. 2017, Japanese, Nominated symposium
    [Invited], [Domestic Conference]
  • 体を温める食肉、冷やす食肉
    若松 純一
    第71回日本栄養・食糧学会大会 シンポジウム「 Meet the World of Meat! ~食肉のおいしさ・機能性・遺伝子制御の新展開~ 」, 20 May 2017, Japanese, Nominated symposium
    [Invited], [Domestic Conference]
  • 肉の発酵と熟成
    若松 純一
    第二回「食と健康の達人」拠点シンポジウム北海道の発酵~ワインと食~, 20 Aug. 2016, Japanese, Public discourse
    [Invited], [Domestic Conference]
  • 亜鉛プロトポルフィリンIXが発色剤無添加の非加熱食肉製品の色調に寄与する
    若松純一
    日本栄養・食糧学会関東支部大会シンポジウム講演要旨集, 2013, Japanese
■ Syllabus
  • 食品安全・機能性開発学特論, 2024年, 修士課程, 農学院
  • 食品安全・機能性開発学特論演習, 2024年, 修士課程, 農学院
  • 畜産食品衛生学, 2024年, 学士課程, 農学部
  • 畜産科学概論, 2024年, 学士課程, 農学部
  • 細胞組織生物科学, 2024年, 学士課程, 農学部
  • 細胞組織生物学実験, 2024年, 学士課程, 農学部
  • 一般教育演習(フレッシュマンセミナー), 2024年, 学士課程, 全学教育
  • 一般教育演習(フレッシュマンセミナー), 2024年, 学士課程, 全学教育
  • 基礎畜産物利用学Ⅱ, 2024年, 学士課程, 農学部
  • 畜産物利用学実習, 2024年, 学士課程, 農学部
■ Affiliated academic society
  • ANIMAL SCIENCE AND AGRICULTURE HOKKAIDO
  • 日本栄養・食糧学会
  • Japan Society for Meat Science and Technology
  • 日本畜産学会
  • Hokkaido Animal Science and Agriculture Society
  • Japanese Society of Nutrition and Food Science
  • Japanese Society of Animal Science
■ Research Themes
  • Searching for meat-inherent constituent(s) involved in the insertion of zinc into protoporphyrin IX
    令和7年度研究助成
    Jun. 2025 - Mar. 2026
    The Ito Foundation, Principal investigator, 169
  • シカ肉の科学的根拠に基づく品質基準と適切な取り扱い手法の確立
    科学研究費助成事業
    01 Apr. 2022 - 31 Mar. 2025
    松浦 友紀子; 若松 純一; 中下 留美子; 亀井 利活
    日本学術振興会, 基盤研究(C), 国立研究開発法人森林研究・整備機構, 22K05962
  • Elucidation of mechanism by which ferrochelatase acts to form zinc protoporphyrin IX in meat and meat products
    研究助成
    Apr. 2023 - Mar. 2024
    The Ito Foundation, Principal investigator, 19
  • Development of color improvement technique of meat products by using bacteria with high ZnPP-forming ability
    Grants-in-Aid for Scientific Research
    01 Apr. 2020 - 31 Mar. 2023
    若松 純一
    本研究で見出した、好気的条件下でも亜鉛プロトポルフィリンIX(ZnPP )を形成できる乳酸菌(LLC、略称とする)は、これまで改善できなかった表層部を含む発酵ドライソーセージ全体の色調を改善できることを示した。本年度は、実用化に向けた各種要因の調査、並びにLLCによる好気的条件下での形成機構を検討した。
    低温での乾燥を行わず高温熟成を行ったドライソーセージでは、LLC添加区では無添加区に比べてZnPP量が増加し、最終製品の断面全体は鮮やかな色調となった。ZnPP量は初めの1週間で最も上昇し、その後はほぼ一定の値となった。同様に、前駆物質であるプロトポルフィリンIX(PPIX)量の上昇も見られた。一方で、低温熟成で製造を行った場合、無添加区とLLC添加区間でZnPP自家蛍光強度および色調に差はなく、乳酸菌による効果は見られなかった。表面のネトや雑菌の増殖を防止する目的で予め低温乾燥を7日間行ったところ、高温熟成を経ても断面全体もしくは外側部分でZnPP形成が促進されなかった。以上より、乳酸菌LLC発酵ドライソーセージにおいてZnPP形成促進による色調改善を行うためには熟成初期の温度と菌の状態が重要であることが示唆された。
    LLCの好気的条件下でのZnPP形成機構については、ヘムから脱鉄して亜鉛を挿入するという経路が同じあったことと、肉中の関与する酵素によって阻害されること、嫌気的条件下ではより一層産生することから、LLCは肉中の好気的ではZnPP形成できないプロセスをバイパス的に補うことにより、ZnPPを酸素の影響に関係なくZnPPを産生させることが示唆された。さらに、菌体だけではなく培養した後の培地成分にも形成促進効果が見られ、菌体外に分泌した酵素だけでなく、代謝産物にも形成促進効果がある可能性が示された。
    Japan Society for the Promotion of Science, Grant-in-Aid for Scientific Research (C), Hokkaido University, 20K06356
  • Studies on ZnPP formation and color-improvement effect of meat products by food-grade Staphylococcus
    研究助成
    Apr. 2022 - Mar. 2023
    The Ito Foundation, Principal investigator, 54
  • Studies on the formation and the existence form of zinc protoporphyrin IX in dry-cured ham (III)
    研究助成
    Apr. 2021 - Mar. 2022
    The Ito Foundation, Principal investigator, 16
  • Studies on the formation and the existence form of zinc protoporphyrin IX in dry-cured ham (II)
    研究助成
    Apr. 2020 - Mar. 2021
    The Ito Foundation, Principal investigator, 148
  • Studies on the formation and the existence form of zinc protoporphyrin IX in dry-cured ham
    研究助成
    Apr. 2019 - Mar. 2020
    The Ito Foundation, Principal investigator, 33
  • 食肉タンパク質の抗肥満および脂質代謝促進効果に関する研究(II)
    平成30年度研究助成
    Apr. 2018 - Mar. 2019
    若松 純一
    公益財団法人伊藤記念財団, Principal investigator, Competitive research funding
  • Studies on chicken and sheep meat peptides which contribute to activation of brown adipose tissue and raise body temperature after consumption
    Grants-in-Aid for Scientific Research
    Apr. 2016 - Mar. 2019
    WAKAMATSU Jun-ichi
    In in vivo study, the hydrophilic fraction of chicken artificial-digested peptide was suggested to have thermogenesis activity after consumption. Since there were some difference in meat digested- and absorbed-peptide among animal species. a small amount of animal species-specific peptide digested after consumption might have activity of thermogenesis. However, in vivo study using hepatocyte, the opposite results about gene expression were observed in vivo study. Therefore, it suggests that the digested and absorbed peptide of meat protein, especially chicken, do not increase the body temperature by acting on liver after absorption directly.
    Japan Society for the Promotion of Science, Grant-in-Aid for Scientific Research (C), Hokkaido University, Principal investigator, Competitive research funding, 16K08002
  • 食肉タンパク質の抗肥満および脂質代謝促進効果に関する研究
    平成29年度研究助成
    Apr. 2017 - Mar. 2018
    若松 純一
    公益財団法人伊藤記念財団, Principal investigator, Competitive research funding
  • ZnPP形成能を有する微生物の探索と応用
    平成27年度研究助成
    Jun. 2015 - Mar. 2016
    若松 純一
    伊藤記念財団, Principal investigator, Competitive research funding
  • 国産赤身型牛肉である乳用種牛肉の輸入牛肉に対する差別化技術の開発
    14. 平成25年度農林水産業・食品産業科学技術研究推進事業「実用技術開発ステージ」
    2013 - 2015
    佐々木 啓介
    農林水産省, Competitive research funding
  • Improvement of chicken meat production by dietary zinc compounds
    Grants-in-Aid for Scientific Research
    2012 - 2014
    HONDA Kazuhisa; WAKAMATSU Jun-ichi
    In the present study, we investigated the effects of dietary supplementation of zinc on growth and meat color in broiler chickens. Dietary supplementation of peptide zinc for 3 weeks significantly increased body weight and breast muscle weight and improved meat color in broiler chicks. On the other hand, dietary supplementation of zinc sulfate and zinc carbonate for 3 weeks did not influence food intake, body weight, breast muscle weight, thigh weight, and meat color in broiler chicks. However, dietary supplementation of peptide zinc for 6 weeks did not influence body weight, breast muscle weight, thigh weight, meat color, and muscle zinc protoporphyrin content in broiler chicks. These results suggest that peptide zinc improves the growth of broiler chickens in the growing period but not in the finishing period.
    Japan Society for the Promotion of Science, Grant-in-Aid for Scientific Research (C), Kobe University, Coinvestigator not use grants, Competitive research funding, 24580389
  • Effect of zinc protoporphyrin IX on the qualities of meat products without nitrite/nitrate
    Grants-in-Aid for Scientific Research
    2011 - 2013
    WAKAMATSU JUN-ICHI
    We elucidated that ZnPP-formation in meat or meat products is strongly influenced from pH as well as acidifier. As to salami which pH was adjusted by using a certain acidifier, the color was almost same as that of salami with nitrite. In addition, we found several microorganisms that facilitated to form ZnPP in raw meat products. When we investigated the optimum pH to form ZnPP by using various muscles, another optimum pH differing from previous optimum pH was found. ZnPP-formation at the new optimum pH was significantly correlated positively with a proportion of type I muscle fiber. On the other hand, the effect of supplemental zinc by ZnPP was not higher than that of inorganic zinc.
    Japan Society for the Promotion of Science, Grant-in-Aid for Scientific Research (C), Hokkaido University, Principal investigator, Competitive research funding, 23580362
  • Studies on mechanism by which zinc protoporphyrin IX is formed in meat product and its applications
    Grants-in-Aid for Scientific Research(基盤研究(C))
    2008 - 2010
    Jun-ichi WAKAMATSU; 服部 昭仁; Takanori NISHIMURA; Akihito HATTORI
    Our objectives in this study are to elucidate the mechanism by which zinc protoporphyrin IX (ZPP) in meat products with no addition of nitrite or nitrate and to improve the color of meat products by using ZPP. Protoporphyrin IX (PPIX), to which metal ion is not coordinated, was formed both from heme biosynthesis route and heme. It seems to be that nitric oxide (NO) inhibits the formation of PPIX and consequently inhibits the formation of ZPP. Water-soluble component(s) and water-insoluble component(s) in meat are essential for the formation of ZPP. The water-soluble component(s) seems not t...
    Ministry of Education, Culture, Sports, Science and Technology, 基盤研究(C), 北海道大学, Principal investigator, Competitive research funding, 20580288
  • Production of additive-free meat products. Investigating into the mechanism leading to good colour dried pork meats without the use of nitrite and nitrate
    The Co-operative Research Programme Fellowship Awards for 2009
    2009 - 2009
    WAKAMATSU Jun-ichi
    Organization for Economic Co-operation and Development (OECD), Principal investigator, Competitive research funding
  • 食肉タンパク質のS-ニトロシル化と量的変化に及ぼす発色剤の影響について
    平成19年度研究助成
    Apr. 2007 - Mar. 2008
    WAKAMATSU Jun-ichi
    財団法人伊藤記念財団, Principal investigator, Competitive research funding
  • 食肉中のエネルギー代謝促進物質の探索と実用化
    地域イノベーション創出総合支援事業 平成20年度「シーズ発掘試験」A発掘型
    2008 - 2008
    若松 純一
    我々はこれまでの研究から、鶏肉や羊肉の摂取により、体温を上昇させることを確認した。そこで本研究では、鶏肉および羊肉による体温上昇機構を明らかにすることと有効成分を特定することを目的とし、動物実験を行って血液生化学検査、各種プロテオーム解析等により検討する。これにより、鶏肉および羊肉の機能を科学的に解明し、「食」を通じた生活の質改善を図るとともに、必要に応じて有効成分を抽出・濃縮し、エネルギー代謝改善のサプリメントの開発につなげる。
    独立行政法人科学技術振興機構, 北海道大学, Principal investigator, Competitive research funding
  • 発色剤無添加乾塩漬ハムの亜鉛プロトポルフィリンIX(ZPP)形成における海塩の役割について
    平成18年度研究助成
    Apr. 2006 - Mar. 2007
    若松 純一
    財団法人ソルト・サイエンス研究財団, Principal investigator, Competitive research funding
  • 亜鉛プロトポルフィリンIX形成による食肉製品の色調改善法
    「研究開発助成事業」若手研究補助金
    2007 - 2007
    若松 純一
    ノーステック財団, Principal investigator, Competitive research funding
  • 伝統的乾塩漬食肉製品中のヘム色素の亜鉛置換に関する研究
    科学研究費補助金(若手研究(B))
    2004 - 2006
    若松 純一
    我々はこれまでに、亜鉛プロトポルフィリンIX(ZPP)はヘムの鉄と亜鉛に置換によるものではなく、別に形成されたプロトポルフィリンIX(PPIX)に亜鉛を挿入することにより形成されることを明らかにした。パルマハムなどの伝統的乾塩漬食肉製品ではZPPは水で抽出できるが、一般に試薬などのZPPは水に溶解しないことからも、ZPPはミオグロビン(食肉中の主要なヘムタンパク質)以外のものと結合して存在していると考えられる。そこで、パルマハムの水抽出物から硫安分画、イオン交換クロマトグラフィならびに分取用等電点電気泳動により、ZPPを含む画分を精製し、SDS-PAGESより1本の主要なタンパク質のバンドが検出された。MALDI-TOF MSを用いて、このタンパク質は血清アルブミンと同定された。免疫沈降法によりパルマハム水抽出物からアルブミンを精製して、75%アセトン抽出法によりZPPの存在が確認された。一方、水抽出できないZPPが残存していることなどから、ZPPと結合しているタンパク質はアルブミン以外にも存在していると考えられる。亜硝酸塩などの発色剤を添加した食肉製品ではZPPはほとんど見られないことが知られている。この原因を解明するために、モデル実験を用いて検討したところ、亜硝酸塩の酸化作用が原因ではなく、一酸化窒素がZPPならびにその前駆物質であるPPIXの形成を阻害することにより、結...
    文部科学省, 若手研究(B), 北海道大学, Principal investigator, Competitive research funding, 16780184
  • 亜臨界水・水熱反応を用いた食肉資源のネオプロセシングに関する基礎的研究
    科学研究費補助金(萌芽研究)
    2004 - 2005
    西邑 隆徳; 服部 昭仁; 若松 純一
    家畜のと畜解体工程および食肉加工工程で生じる屑肉などはテーブルミートとしては利用できないが、良質なタンパク質が豊富に含まれており、これらのタンパク質の新たな利活用が求められている。近年、「水」を反応場としてタンパク質などの高分子を分解する亜臨界水・水熱反応が着目されており、本研究では、1.亜臨界水・水熱反応の諸条件(温度、時間)が食肉タンパク質の分解様相に及ぼす影響を明らかにするとともに、2.亜臨界水・水熱反応生成物の生理活性を調べることによって、亜臨界水・水熱反応を食肉タンパク質資源の利活用技術として応用するための基礎的データを得ることを自的とした。先ず、食肉タンパク質に対する適正な亜臨界水・水熱反応条件の概略を把握することを目的に、鶏筋肉、鶏筋原線維、鶏ミオシンおよびコラーゲンを試料として用い、亜臨界水・水熱反応条件がタンパク質分解に及ぼす影響を検討した。その結果、(1)250℃以上の亜臨界水処理では遊離してきたアミノ酸の分解が促進されること、(2)亜臨界水・水熱反応温度の上昇に伴ってアンモニア生成量が増加すること、(3)亜臨界水・水熱反応によって生成されたペプチドの大きさ(分子量)は処理温度の上昇に伴って低下すること、(4)生成されたペプチドのACE阻害活性は鶏ミオシンやコラーゲンでは亜臨界水・水熱反応温度の上昇に伴って顕著に低下した。以上の結果から、食肉タンパク質への...
    文部科学省, 萌芽研究, 北海道大学, Coinvestigator not use grants, Competitive research funding, 16658101
  • Moduration of myostatin activity through extracellular matrix
    Grants-in-Aid for Scientific Research(基盤研究(B))
    2002 - 2004
    Takanori NISHIMURA; 森 匡; 服部 昭仁; 若松 純一
    Myostatin, a member of TGF-β superfamily of growth factors, acts as a negative regulator of skeletal muscle mass. The mechanism whereby myostatin controls the proliferation and differentiation of myogenic cells is mostly clarified. However, the regulation of myostatin activity to myogenic cells after its secretion in the extracellular matrix (ECM) is still unknown. Decorin, a small leucine-rich proteoglycan, binds TGF-β and regulates its activity in the ECM. Thus, we hypothesized that decorin could also bind to myostatin and participate in modulation of its activity to myogenic cells. In or...
    Ministry of Education, Culture, Sports, Science and Technology, 基盤研究(B), 北海道大学, Coinvestigator not use grants, Competitive research funding, 14360156
  • The study on the mechanism of solubilization of myofibrillar proteins in water
    Grants-in-Aid for Scientific Research(基盤研究(B))
    2001 - 2003
    Akihito HATTORI; 辰巳 隆一; 西邑 隆徳; 若松 純一
    We have created an alternative solubilizing method that has resulted in solubilizing more than 80% of chicken breast muscle myofibrillar proteins in water The purpose of this study is to determine the solubilization mechanism of myosin in a low ionic strength solution. We have shown that myosin, a major myofibrillar protein, prepared from chicken skeletal muscle can also be solubilized in the same manner, and it is essential to maintain myosin suspensions at a neutral pH with L-histidine(L-His) and at a low ionic strength. The results from the SDS-PAGE with EDC reactions have shown water-so...
    Ministry of Education, Culture, Sports, Science and Technology, 基盤研究(B), 北海道大学, Coinvestigator not use grants, Competitive research funding, 13460115
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