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

Profile and Settings

• Name (Japanese)

  Wakamatsu

• Name (Kana)

  Jun-ichi

• Name

  200901099352812530

Alternate Names

http://lab.agr.hokudai.ac.jp/cell_tissue_biology/

Achievement

Research Interests

• 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   色   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 Areas

• Life sciences / Animal production science
• Life sciences / Food sciences
• Humanities & social sciences / Home economics, lifestyle science

Research Experience

• 2024/04 - Today Hokkaido University Graduate School of Agriculture Research Faculty of Agriculture Division of Applied Bioscience Professor
• 2021/04 - 2024/03 Hokkaido University Graduate School of Agriculture Research Faculty of Agriculture Division of Applied Bioscience Associate Professor
• 2013/01 - 2021/03 Hokkaido Univ. Associate professor
• 2012/07 - 2012/12 Hokkaido Univ. Associate Professor
• 2007/04 - 2012/06 Hokkaido Univ. Assistant Professor
• 2002/05 - 2007/03 Hokkaido Univ. Assistant Professor
• 1994/04 - 2002/05 Itoham Inc.

Education

• 1992/04 - 1994/03  北海道大学大学院
• 1986/04 - 1992/03  Hokkaido Univ.

Awards

• 2016/06 The Ito Foundation Ito Foundation Award
   

  受賞者: WAKAMATSU Jun-ichi
• 2008 畜産技術協会賞
  

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 [Refereed]
   

  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  2024/02/09 [Refereed][Not invited]
  
• 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 [Refereed][Not invited]
   

  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 [Refereed]
   

  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 2023/06 [Refereed]
  
• 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 [Refereed]
   

  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 [Refereed]
   

  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 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.
• 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 2022/10 [Refereed][Invited]
   

  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 2022/01/23 [Refereed]
   

  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.
• 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.
• 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.
• 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 2020/06 [Refereed][Not invited]
   

  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 1346-907X 2020 [Refereed]
  
• 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

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

  LWT Elsevier {BV} 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, 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 [Refereed][Not invited]
  
• 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 1344-3941 2017/11 [Refereed][Not invited]
   

  In striated muscles, approximately 300 myosin molecules form a single thick filament in myofibrils. Each myosin is continuously displaced by another myosin to maintain the thick filament structure. Our previous study using a fluorescence recovery after photobleaching (FRAP) technique showed that the myosin replacement rate is decreased by inhibition of protein synthesis, but myosin is still exchangeable. This result prompted us to examine whether myosin in the cytoplasm is involved in myosin replacement in myofibrils. To address this, FRAP was measured in green fluorescent protein (GFP)-tagged myosin heavy chain 3 (Myh3) expressing myotubes that were treated with streptolysin-O (SLO), which forms pores specifically in the plasma membrane to induce leakage of cytoplasmic proteins. Our biochemical data demonstrated that the cytoplasmic myosin content was reduced in SLO-permeabilized semi-intact myotubes. Furthermore, FRAP experiments showed a sluggish substitution rate of GFP-Myh3 in SLO-permeabilized myotubes. Taken together, these results demonstrate that the myosin substitution rate is significantly reduced by a decreased amount of myosin in the cytoplasm and that cytoplasmic myosin contributes to myosin replacement in myofibrils.
• 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 0378-4320 2017/10 [Refereed][Not invited]
   

  Improving sperm motility and viability are major goals to improve efficiency in the poultry industry. In this study, the effects of supplemental dietary turmeric by-product (TBP) from commercial turmeric production on sperm motility, viability, and antioxidative status were examined in domestic fowl. Mature Rhode Island Red roosters were divided into two groups controls (group C) without TBP administration and test subjects (group T) fed a basal diet supplemented with 0.8 g of TBP/day in a temperature-controlled rearing facility (Experiment 1) and 1.6 g/day under heat stress (Experiment 2) for 4 weeks. In Experiment 1, TBP dietary supplementation increased the sperm motility variables straight-line velocity, curvilinear velocity, and linearity based on a computer-assisted semen analysis, 2 weeks following TBP supplementation. In Experiment 2, using flow cytometry, sperm viability at 3 and 4 weeks following TBP supplementation was greater in Group T than C, and this increase was consistent with a reduction in reactive oxygen species (ROS) production at 2 and 4 weeks. The results of both experiments clearly demonstrate that dietary supplementation with TBP enhanced sperm motility in the controlled-temperature conditions as well as sperm viability, and reduced ROS generation when heat stress prevailed. Considering its potential application in a range of environments, TBP may serve as an economical and potent antioxidant to improve rooster fertility.
• 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 0301-4800 2016/04 [Refereed][Not invited]
   

  We compared the effects of purified meat proteins on postprandial thermogenesis and on the secretion of and responsiveness to thyroid hormones (THs) in rats. Body temperatures at 2 h after feeding were significantly higher in the chicken and mutton protein groups than in the other groups, and these proteins seem to have a strong thermogenic effect. There were no significant differences in plasma TH concentrations among the groups, but levels of TH-responsive Spot 14 protein in the liver and brown adipose tissue were significantly higher in the chicken and mutton protein groups than in the other groups. Levels of malic enzyme 1 protein in the liver and brown adipose tissue were significantly higher in the chicken protein group than in the other groups except for the mutton protein group. Furthermore, levels of uncoupling protein 1 were higher in the chicken and mutton protein groups than in the other groups. The results suggest that the difference in postprandial thermogenesis of meat is strongly dependent on meat proteins; chicken and mutton proteins are strong promoters of postprandial thermogenesis, and THs may contribute to this effect. Since strong postprandial thermogenesis and high expression levels of TH target genes and their products were not observed in the amino acid group, chicken and mutton proteins or their digested peptides might contribute to these effects.
• 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 1346-907X 2015/11/25 [Refereed][Not invited]
  
• 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 0363-6143 2015/11 [Refereed][Not invited]
   

  Highly organized thick filaments in skeletal muscle cells are formed from similar to 300 myosin molecules. Each thick-filament-associated myosin molecule is thought to be constantly exchanged. However, the mechanism of myosin replacement remains unclear, as does the source of myosin for substitution. Here, we investigated the dynamics of myosin exchange in the myofibrils of cultured myotubes by fluorescent recovery after photo-bleaching and found that myofibrillar myosin is actively replaced with an exchange half-life of similar to 3 h. Myosin replacement was not disrupted by the absence of the microtubule system or by actomyosin interactions, suggesting that known cytoskeletal systems are dispensable for myosin substitution. Intriguingly, myosin replacement was independent of myosin binding protein C, which links myosin molecules together to form thick filaments. This implies that an individual myosin molecule rather than a thick filament functions as an exchange unit. Furthermore, the myosin substitution rate was decreased by the inhibition of protein synthesis, suggesting that newly synthesized myosin, as well as preexisting cytosolic myosin, contributes to myosin replacement in myofibrils. Notably, incorporation and release of myosin occurred simultaneously in myofibrils, but rapid myosin release from myofibrils was observed without protein synthesis. Collectively, our results indicate that myosin shuttles between myofibrils and the nonmyofibrillar cytosol to maintain a dynamic equilibrium in skeletal muscle cells.
• 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.
• 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 1344-3941 2015/05 [Refereed][Not invited]
   

  The objective of this study was to obtain fundamental data for improving the color of meat products by using animal by-products. We investigated zinc protoporphyrin IX (ZnPP)-forming properties of various internal organs from pigs and chickens. ZnPP was formed in the liver, heart and kidney, whereas the porcine spleen and bile, which are involved in the metabolism of heme, did not have ZnPP-forming properties. The optimum pH values were different among the internal organs and the ZnPP-forming properties of porcine organs were better than those of chicken organs. The porcine liver showed the greatest ZnPP-forming properties among all of the internal organs investigated in this study. The optimum pH value for ZnPP formation in the liver was lower than that of skeletal muscle. Oxygen did not inhibit the formation of ZnPP in the liver, unlike in skeletal muscle. Animal by-products such as the liver have good ability for the formation of ZnPP and might be useful for improving the color of meat products.
• 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 0940-9602 2015 [Refereed][Not invited]
   

  In the present study, we examined muscle regeneration following two types of chemical injuries, cardiotoxin (CTX) and glycerol, in order to compare their effect on the morphological characteristics during muscle regeneration, in addition we studied the structural changes of the intramuscular connective tissue (IMCT) during the regeneration process, by scanning electron microscopy (SEM) after digestion of the cellular elements of the muscle with sodium hydroxide. Tibialis anterior (TA) muscles of adult male mice were injected either with CTX or glycerol. Muscle degeneration was greater in the CTX-injured model than in the glycerol-injured model at day 4 post injection. Muscle regeneration started at day 7 in both the CTX and glycerol models. However, the CTX-injured model showed a higher myotube density and larger myotube diameter than the glycerol-injured model at days 10 and 14 post injection. On other hand, adipocyte infiltration was detected in the glycerol-injured model. In contrast, no adipocytes could be detected in the CTX-injured model. Furthermore, ultrastructural analysis showed a significant difference in myofiber damage and regeneration between the two models. SEM of the IMCT showed a transient increase in endomysial collagen deposition at early stages of. regeneration in the CTX-injured model. In contrast, glycerol-injured model showed slight endomysial collagen deposition. Our results suggest that changes in IMCT affect the efficiency of muscle regeneration. Studying the three dimensional structure of IMCT may help clinical therapies to reduce skeletal muscle fibrosis. To our knowledge this is the first time the changes in IMCT following CTX and glycerol injury using SEM-cell maceration technique have been compared. (c) 2015 Elsevier GmbH. All rights reserved.
• 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 0301-4800 2013/12 [Refereed][Not invited]
   

  We investigated the postprandial thermic effect of chicken and its mechanisms in rats. A chicken diet showed a strong thermic effect after consumption, and the removal of fat induced more rapid and stronger thermogenesis. Although thermogenesis induced by a purified chicken protein diet was also strong, the thermic reaction was not so rapid and a remarkable rise of peripheral temperatures was not observed. Defatted chicken and purified chicken protein activated the thyroid hormone system and up-regulated rate-limiting enzyme genes of glucose metabolism and the tricarboxylic acid (TCA) cycle in the liver. Moreover, chicken protein up-regulated the mRNA expression of a rate-limiting enzyme of hepatic lipid metabolism. It is possible that the mechanisms by which body temperature is raised are different between chicken protein and defatted chicken. On the other hand, it is possible that chicken fat suppressed the expression of energy metabolism-related genes that was induced by the consumption of lean chicken. As a result, a rise of postprandial body temperature might not have been induced after consumption of chicken fat. These results suggest that the consumption of lean chicken activates the thyroid hormone system and hepatic energy metabolism and consequently induces the postprandial thermic effect of chicken.
• 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 1344-3941 2013/09 [Refereed][Not invited]
   

  Decorin, a small leucine-rich proteoglycan, plays an important role in cellular activities through modification of growth factors. It also acts as a signaling molecule to non-muscle cells through epidermal growth factor receptor or insulin-like growth factor I receptor (IGF-IR). However, it is unclear if decorin acts as a signaling molecule to myogenic cells. In this study, we investigated the effect of decorin on the differentiation of myoblasts and the signaling via IGF-IR to myogenic cells. C2C12 myoblasts cultured in media containing decorin for 72h showed more extensive formation of multinucleated myotubes than control cells cultured in the same media without decorin. The protein expressions of myogenin and myosin heavy chian were higher in decorn-treated cells than in control cells. These results suggest that decorin enhances the differentiation of myoblasts. Western blot analysis and immunocytochemistry showed that IGF-IR was expressed in myoblasts and myotubes. Furthermore, Akt, which is downstream of IGF-IR, was more phosphorylated in myoblasts cultured in media containing decorin than those in media without decorin. These results suggest that decorin activates Akt downstream of IGF-IR and enhances the differentiation of myogenic cells. © 2013 Japanese Society of Animal Science.
• 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 1344-3941 2013/09 [Refereed][Not invited]
   

  Myostatin is a growth and differentiation factor and acts as a negative regulator of skeletal muscle mass. Although the mechanism whereby myostatin controls muscle cell growth is mostly clarified, the regulation of myostatin activity after its secretion into the extracellular matrix (ECM) is still unclear. In the present study, we investigated the interaction between laminin and myostatin and the effect of laminin on myostatin signaling in vitro. The surface plasmon resonance assay showed that laminin bound to mature myostatin and activin receptor type IIB (ActRIIB), but did not bind to latency-associated protein, which remains non-covalently linked to mature myostatin. Furthermore, kinetic analysis demonstrated that the affinity of mature myostatin for laminin was similar to that for ActRIIB. Next, we examined the action of laminin on the myostatin signaling pathway using a conventional reporter assay. The luciferase activity of myostatin-treated cells was repressed significantly (P < 0.05) by coincubation of laminin. These results suggest that laminin has a potential to regulate myostatin activity through binding to mature myostatin and/or its receptor ActRIIB.
• 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 1344-3941 2013 [Refereed][Not invited]
   

  We examined animal species differences in the postprandial thermic effect of meat and investigated the postprandial thermic effect of mutton in rats. After intake of experimental diets containing each meat, body temperatures of rats fed mutton or venison were significantly higher than that of rats fed rabbit meat. After intake of experimental diets containing fractionized mutton, the body temperatures of rats fed diets containing lean mutton protein were higher than those of rats fed diets without lean mutton protein. In a two-dimensional fluorescence difference gel electrophoresis study of brown adipose tissue, it was shown that the intake of mutton up-regulated the expression of many signaling molecules that are involved in energy metabolism. The postprandial thermic effect of mutton seems to be due not to catecholamine and adrenocorticotropic hormone but to thyroid hormones. The results suggest that intake of lean mutton protein stimulates the secretion of thyroid hormones and facilitates energy metabolism in rats.
• 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 0388-6107 2012/12 [Refereed][Not invited]
   

  The aim of this study was to clarify the effects of myostatin, which is a negative regulator of skeletal muscle mass, on the proliferation of NIH3T3 fibroblasts and the synthesis of extracellular matrix (ECM) by them. A proliferation assay revealed that myostatin attenuated cell growth at any of the doses used. High doses of myostatin strongly inhibited cell proliferation. Moreover, myostatin receptor, activin receptor type-2B (ActRIIB), was found to be distributed on cells and it was also clarified that myostatin increased the expression of cyclin-dependent kinase inhibitor p21 (p21). These results suggested that a high dose of myostatin inhibits fibroblast proliferation by the same mechanism as that for inhibition of myoblast proliferation. We then examined the effects of myostatin on the mRNA expression of ECM molecules (decorin, biglycan, type I collagen, type III collagen, type IV collagen and type V collagen) by real-time PCR. Real-time PCR showed that myostatin increased the mRNA of decorin, biglycan and collagen (types I, IV and V) in fibroblasts. The results suggest that myostatin regulates ECM synthesis in cultured fibroblasts.
• 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.
• 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 Japanese Society of Animal Science 82 (3) 325 - 331 1346-907X 2011/08 [Refereed][Not invited]
   

  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 1344-3941 2011 [Refereed][Not invited]
   

  The effect of liquid whey feeding on fecal bacteria and their metabolites was assessed in five pregnant sows and 66 growing pigs. Sows were fed a control diet for 4 weeks (control period) followed by the same diet but with whey feeding (5 L/day/pig) for 4 weeks (whey period). One group of growing pigs was given 267 L of whey per pig (whey group), while the other group was not (control group). In both cases, liquid whey was given separately from control diet. Sows in the whey period had feces showing lower pH, lower ammonia concentration, and larger population sizes of total bacteria, lactobacilli and bifidobacteria. The bacterial gene library analysis indicated that Mitsuokella and Megasphaera were more frequently detected, while Clostridium disporicum were detected less frequently in the whey period. Feces from whey-fed growing pigs showed lower pH than that from control pigs in the early stage of growing. Also, larger populations of total bacteria, lactobacilli and bifidobacteria were recorded in the whey group. From the bacterial gene library analysis, the detection frequency of Lactobacillus reuteri tended to be higher in the whey group. These results indicate that whey feeding influences the hindgut microbiota of pigs, possibly leading to a fermentation shift that is favorable for animal health.
• 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.
• 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 1344-3941 2010 [Refereed][Not invited]
   

  Myostatin, a member of the TGF-beta superfamily, is a negative regulator of skeletal muscle mass. We have recently demonstrated that decorin binds to myostatin in vitro, and that immobilized decorin within the collagen matrix prevents myostatin-mediated inhibition of myoblast proliferation. However, little is known about other ECM molecules that bind to myostatin and modulate its activity. Thus, in the present study, we investigated the interaction of several other ECM molecules with myostatin. We here show that fibromodulin, fibronectin and laminin bind to myostatin in the presence of Zn(2+) with a dissociation constant (K(D) ) of 10(-10)similar to 10(-8) mol/L. Fibromodulin shows the highest affinity for myostatin among them. These results suggest that these ECM molecules may modulate myostatin activity like decorin does.
• 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 0309-1740 2010/01 [Refereed][Not invited]
   

  The aim of this study was to elucidate the mechanism by which curing agents, especially nitrite, inhibit the formation of zinc protoporphyrin IX (ZPP) in dry-cured hams such as Parma ham. The oxidation-reduction potential of model solutions was increased by the addition of nitrite, but it was not clear whether the formation of ZPP is inhibited by the oxidizing property of nitrite. The effect of nitric oxide (NO) produced from nitrite on the formation of ZPP was examined. The amount of ZPP formed was decreased by the addition of NO donors. The amount of protoporphyrin IX (PPIX), which is the precursor of ZPP, was also decreased by the addition of NO donors. It is concluded that NO produced from nitrite inhibited the formation of PPIX and ZPP was therefore not formed in cured meat products with the addition of nitrite or nitrate. (C) 2009 Elsevier Ltd. All rights reserved.
• Effect of L-histidine and ionic strength on disassembly of myosin filaments

  Proceeding ICoMST2010 B026  2010 [Not refereed][Not invited]
  
• Thermic effect of chicken

  Proceeding ICoMST2010 B026  2010 [Not refereed][Not invited]
  
• 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 社団法人日本畜産学会 80 (4) 443 - 450 1346-907X 2009/11 [Refereed][Not invited]
   

  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 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.
• 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 0309-1740 2009/05 [Refereed][Not invited]
   

  We measured the contents of Zn protoporphyrin IX (ZPP), heme and protoporphyrin IX (PPIX) in Parma ham by simultaneous analysis using high-performance liquid chromatography (HPLC). Extraction with ethyl acetate-acetic acid (4:1) was suitable for the quantitative analysis of ZPP. The contents of heme, ZPP and PPIX in Parma ham were 15.0-29.9, 27.7-47.0 and 0.4-1.1 mu g/g, respectively, and total content of porphyrin was 43.7-76.6 mu g/g. The amount of ZPP in Parma ham was larger than that of heme, and ZPP accounted for 60-70% of all porphyrins. (c) 2008 Elsevier Ltd. All rights reserved.
• 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 1344-3941 2009/04 [Refereed][Not invited]
   

  Zinc protoporphyrin IX (ZPP) is a characteristic red pigment in meat products that are manufactured without the addition of a curing agent such as nitrate or nitrite. To examine the effects of impurities such as mineral components in sea salt on the formation of ZPP, we manufactured Parmatype dry-cured hams that were salted with refined salt or sea salt and examined the involvement of oxidation-reduction potential (ORP) in the formation of ZPP. The content of ZPP was increased drastically after 40 weeks. Microscopic observation showed strong fluorescence caused by ZPP muscle fiber after 40 weeks. Conversely, heme content varied considerably during processing. ORP increased during processing. However, there was no obvious difference between ham salted with refined salt and that salted with sea salt. Therefore, it was concluded that impurities in sea salt were not involved in the formation of ZPP.
• 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 1344-3941 2009/02 [Refereed][Not invited]
   

  We studied the relationships between the shear-force value and physical and structural properties of the intramuscular connective tissue (IMCT) in six classes of porcine skeletal muscle to elucidate the contribution of IMCT to toughness of raw pork. The shear-force value of raw pork correlated significantly with that of the IMCT model prepared from each class of skeletal muscle (P < 0.05). The correlation suggested that the variable toughness of pork was caused by the mechanical strength of the endomysium and perimysium. The thickness of the secondary perimysium correlated significantly with the shear-force value of raw pork (P < 0.05) and with that of the IMCT model (P < 0.05). The shear-force value of raw pork correlated significantly with the total amount of collagen (P < 0.05) but not with the heat-solubility of collagen. We concluded therefore that the thickness of the secondary perimysium determines the mechanical strength of IMCT and contributes to toughness in raw pork.
• 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 1344-3941 2008/12 [Refereed][Not invited]
   

  We studied structural changes in the endomysium and perimysium during postmortem aging of pork using the cell-maceration/scanning electron microscope method. Immediately post mortem, endomysia sheaths that house individual muscle fibers displayed a honeycomb-like structure. The sheaths of the endomysium consisted of tightly arranged collagen fibrils in a random network. The perimysium comprised several layers of wavy sheets made up of tightly bundled collagen fibers. While the structure of the intramuscular connective tissues remained almost unchanged up to five days post mortem, the endomysium had resolved into individual collagen fibrils, and the thick sheets of the perimysium had separated into collagen fibers and fibrils at 8 days post mortem. These results provide direct evidence for structural weakening of the endomysium and perimysium during postmortem aging of pork. The shear-force value of raw pork decreased rapidly within six days post mortem and then decreased slowly until 14 days post mortem. Since the rapid increase in tenderness is mainly due to structural weakening of myofibrils, we conclude that the disintegration of the endomysium and perimysium contributes to tenderization of pork during extended postmortem aging.
• 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 0021-9541 2008/06 [Refereed][Not invited]
   

  Decorin, a small leucine-rich proteoglycan, plays an important role in the regulation of cell growth. Our recent study has shown that immobilized decorin in the collagen matrix sequesters myostatin into the extracellular matrix and prevents its inhibitory action to myoblast proliferation in vitro. However, it still remains unclear whether free decorin could affect the proliferation and differentiation of myogenic cells by regulating myostatin activity. In the present study, we generated stable clonal C2C 12 myoblasts that were over-expressing decorin, and showed that decorin over-expressing cells had an increased rate of proliferation as compared to control cells. Decorin over-expressing cells formed multi-giant hypertrophic myotubes with an elongated morphology and larger size as compared to control cells, although the initiation of differentiation in decorin over-expressing cells was somewhat delayed as compared to control cells. Western blot analysis demonstrated that MyoD expression in decorin over-expressing cells was lower than that in control cells until 12 h after induction to differentiate. At 48-h differentiation, the expressions of MyoD, p21 and myogenin were dramatically increased in cells that over-expressed decorin. Furthermore, we revealed that over-expression of decorin suppressed the activity of myostatin endogenously synthesized in C2C 12 myoblasts and attenuated the signaling of exogenous myostatin. Consistent with these results, knockdown of decorin impairs C2C 12 myoblast growth by increasing the sensitivity to exogenous myostatin. These results clearly show that decorin enhances the proliferation and differentiation of C2C 12 myoblasts through suppressing myostatin activity.
• 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 0006-291X 2008/06 [Refereed][Not invited]
   

  Satellite cells are quiescent muscle stem cells that promote postnatal muscle growth and repair. When satellite cells are activated by myotrauma, they proliferate, migrate, differentiate, and ultimately fuse to existing myofibers. The remainder of these cells do not differentiate, but instead return to quiescence and remain in a quiescent state until activation begins the process again. This ability to maintain their own population is important for skeletal muscle to maintain the capability to repair during postnatal life. However, the mechanisms by which satellite cells return to quiescence and maintain the quiescent state are still unclear. Here, we demonstrated that decorin mRNA expression was high in cell cultures containing a higher ratio of quiescent satellite cells when satellite cells were stimulated with various concentrations of hepatocyte growth factor. This result suggests that quiescent satellite cells express decorin at a high level compared to activated satellite cells. Furthermore, we examined the expression of decorin in reserve cells, which were undifferentiated myoblasts remaining after induction of differentiation by serum-deprivation. Decorin mRNA levels in reserve cells were higher than those in differentiated myotubes and growing myoblasts. These results suggest that decorin participates in the quiescence of myogenic cells. (c) 2008 Elsevier Inc. All rights reserved.
• 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 0142-4319 2008/01 [Refereed][Not invited]
   

  Skeletal muscle satellite cells are quiescent stem cells that localized between the plasmalemma and the basement membrane of muscle fiber. When muscle is injured, satellite cells are activated, migrate to the injured site and contribute to the regeneration of muscle. However, little is known about the mechanism by which satellite cells migrate underneath the basement membrane. To clarify this, we investigated the effect of MMP inhibition on the migration of C2C12 muscle cells in vitro using a time-lapse imaging system. The migration speed of cells cultured with an MMP-inhibitor reagent was significantly lower (P < 0.01) than the control cultured without an inhibitor reagent. The persistency index was significantly higher (P < 0.01) in cells cultured with an inhibitor than in those without an inhibitor. Furthermore, MMP-3 knockdown cells migrated faster than control cells. These results strongly suggest that MMPs synthesized in skeletal muscle cells play an important role in the migration of these cells.
• 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 0309-1740 2007/12 [Refereed][Not invited]
   

  We examined the effects of exogenous myoglobin, a bivalent chelator, and nitrite on Zn protoporphyrin IX (ZPP) formation by using model systems. ZPP was formed in a model solution without addition of exogenous myoglobin. After incubation, the amount of ZPP in a model solution was increased but that of heme was not decreased compared with the amounts before incubation. Protoporphyrin IX (PPIX) instead of ZPP also accumulated in a model solution with addition of EDTA, but the amount of heme was not reduced. These results suggested that ZPP was not formed by the Fe-Zn substitution in heme but was formed by the insertion of Zn into PPIX, which was formed independently. The fact that the effects of various factors in model systems with/without addition of a bivalent chelator were similar suggested that ZPP formation was strongly affected by PPIX formation. Inhibition of PPIX formation by nitrite might be the reason for the low levels of ZPP in cured meats. (C) 2007 Elsevier Ltd. All rights reserved.
• 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 0006-291X 2007/10 [Refereed][Not invited]
   

  Decorin, a small leucine-rich proteoglycans, plays an important role in tissue morphogenesis through the regulation of collagen fibrillogenesis and the modulation of some growth factors. Our recent study has shown that decorin binds to myostatin, a negative regulator of skeletal muscle mass, and modulates its inhibitory action to myogenic cell growth in vitro. However, it still remains unclear whether decorin binds to myostatin in vivo during the development of skeletal muscle. To clarify this, we investigated the spatiotemporal expression of decorin and myostatin in rat skeletal muscle by RT-PCR and immunohistochemistry. Decorin mRNA abundance in fetal skeletal muscle was significantly higher than those in neonates and adults (P < 0.05). Decorin mRNA expression decreased drastically at birth, and thereafter gradually up to 9 weeks of age. The mRNA expression pattern of myostatin was quite similar to that of decorin during prenatal and postnatal development of rat skeletal muscle. Immunohistochemical analysis demonstrated that myostatin was located in the muscle fibers, and that decorin was located in the periphery of muscle fibers in fetal rat skeletal muscle. Taken together with our previous data, these results suggest that decorin binds myostatin and sequesters it in the ECM during the development of rat skeletal. (C) 2007 Elsevier Inc. All rights reserved.
• 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 0309-1740 2007/06 [Refereed][Not invited]
   

  We studied the presence of zinc in the red pigment extracted from Parma ham by scanning electron microscopy/energy dispersive X-ray microanalysis. The large peak of about 8.6 keV and the small peaks at about 1.1 keV and 9.5 keV were derived from K-alpha L-alpha 1 and K-beta X-ray of zinc, respectively. Thus, the results suggested that zinc existed in the red pigment extracted from Parma ham. In contrast, the K X-ray peak of iron (6.4 keV) was not detected and the K-alpha X-ray peak of magnesium (1.3 keV) was hardly detected. These results revealed that the red pigment contained not iron but zinc. In addition to the results of mass analysis in previous studies, the red pigment was demonstrated to be zinc protoporphyrin IX. (c) 2006 Elsevier Ltd. All rights reserved.
• 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 0309-1740 2006/11 [Refereed][Not invited]
   

  We investigated the distribution of Zn protoporphyrin IX (ZPP) in Parma ham by using purple LED light and image analysis in order to elucidate the mechanism of ZPP formation. Autofluorescence spectra of Parma ham revealed that ZPP was present in both lean meat and fat, while red emission other than that of ZPP was hardly detected. Although ZPP was found to be distributed widely in Parma ham, it was more abundant in intermuscular fat and subcutaneous fat than in lean meat. The intensity of red emission was weak in muscles that were exposed during the processing. ZPP in both lean meat and subcutaneous fat tended to be more abundant in the inner region than in the outer region. It was thought that ZPP is transferred from lean meat to fat tissue during the processing, resulting in the small amount of ZPP in the lean meat adjacent to subcutaneous fat. Our results led to a completely new hypothesis that ZPP is formed in lean meat and transferred to fat tissue. (c) 2006 Elsevier Ltd. All rights reserved.
• 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 0006-291X 2006/02 [Refereed][Not invited]
   

  Myostatin, a member of TGF-beta 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-beta 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 order to test the hypothesis, we investigated the interaction between myostatin and decorin by surface plasmon assay. Decorin interacted with mature myostatin in the presence of concentrations of Zn2+ greater than 10 mu M, but not in the absence of Zn2+. Kinetic analysis with a 1:1 binding model resulted in dissociation constants (K-D) of 2.02 x 10(-8) M and 9.36 x 10(-9) M for decorin and the core protein of decorin, respectively. Removal of the glycosaminoglycan chain by chondroitinase ABC digestion did not affect binding, suggesting that decorin could bind to myostatin with its core protein. Furthermore, we demonstrated that immobilized decorin could rescue the inhibitory effect of myostatin on myoblast proliferation in vitro. These results suggest that decorin could trap myostatin and modulate its activity to myogenic cells in the ECM. (c) 2005 Elsevier Inc. All rights reserved.
• 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 0309-1740 2004/11 [Refereed][Not invited]
   

  We have adapted the enzymatic method [Biochemical and Biophysical Research Communications 176 (3) (1991) 1617] for the safe and rapid assay of L-carnitine (L-CA) in skeletal muscle using a microplate reader. The concentration of L-CA in fresh semitendinosus muscle from broiler chicken, pig, beef cattle, deer, horse and goat muscle were 0.69, 1.09, 1.86-3.57, 4.57, 4.95 and 11.36 mumol/g wet weight, respectively. The animals which had higher concentration of L-CA, also had the highest amounts of myoglobin as an index to the redness of the muscle. Furthermore, we investigated this relationship between white muscle, M. pectoralis profundus. and red muscle, M. soleus, in laying hens. The L-CA and myoglobin concentration in red muscle were significantly higher than those in white muscle (p < 0.01). These findings suggest that L-CA concentration in muscle is related to oxygen metabolism and to myofiber types. (C) 2004 Elsevier Ltd. All rights reserved.
• 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 0309-1740 2004/10 [Refereed][Not invited]
   

  The aim of this study was to establish a model experiment system to elucidate the mechanism by which Zn-protoporphyrin IX (ZPP) is formed in Parma ham. The established model consisted of myoglobin, meat and antibiotics, and incubation under anaerobic conditions resulted in a greater yield of ZPP. Formation of ZPP was observed even in the presence of various antiseptics. The amount of ZPP formed increased as the period of incubation increased. ZPP formation was inhibited by heating meat homogenate depending on the heating temperature. Our results show that anaerobic conditions are suitable for the formation of ZPP in meat products without nitrate or nitrite and that endogenous enzymes as well as microorganisms may be involved in ZPP formation. (C) 2004 Elsevier Ltd. All rights reserved.
• A Zn-porphyrin complex contributes to bright red color in Parma ham

  J Wakamatsu, T Nishimura, A Hattori

  MEAT SCIENCE 67 (1) 95 - 100 0309-1740 2004/05 [Refereed][Not invited]
   

  The Italian traditional dry-cured ham (Parma ham) shows a stable bright red color that is achieved without the use of nitrite and/or nitrate. In this study we examined the pigment spectroscopically, fluoroscopically and by using HPLC and ESI-HR-MASS analysis. Porphyrin derivative other than acid hematin were contained in the HO-containing acetone extract from Parma ham. A strong fluorescence peak at 588 nm and a weak fluorescence peak at 641 mn were observed. By HPLC analysis the acetone extract of Parma ham was observed at the single peak, which eluted at the same time as Zn-protoporphyrin IX and emitted fluorescence. The results of ESI-HR-MS analysis showed both agreement with the molecular weight of Zn-protoporphyrin IX and the characteristic isotope pattern caused by Zn isotopes. These results suggest that the bright red color in Parma ham is caused by Zn-protoporphyrin IX. (C) 2003 Elsevier Ltd. All rights reserved.
• 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 1344-3941 2004/02 [Refereed][Not invited]
   

  The solubility of skeletal muscle myofibrillar proteins in water was examined. The solubility of the proteins was found to be sensitive to ionic strength and pH of the solution. At the ionic strength of less than 12 mM and neutral pH, more than 80% of myofibrillar proteins were solubilized. Heating at a temperature of more than 70°C was required for the proteins to retain their solubility. The solubility of freeze-dried protein powder prepared from water-soluble myofibrillar proteins was also examined, and it was found that addition of trehalose and heating were essential for re-solubilization in water. Amino acid composition of water-soluble myofibrillar proteins was found to be almost the same as that of myofibrillar proteins.
• 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 1344-3941 2003/10 [Refereed][Not invited]
   

  The effect of skeletal muscle decorin on collagen fibrillogenesis was investigated, in order to provide background for understanding the functions of decorin in skeletal muscle. The self-assembly of type I and III collagen with the addition of decorin or the core protein of decorin from bovine neonatal skeletal muscle was monitored using a spectrophotmeter. Time course changes in the absorbance of collagen solutions showed typical sigmoidal curves composed of three phases. The time of the initial phase was not different between the collagen solution with decorin and that without decorin. The increase rate of the absorbance in the second phase decreased with concentration of decorin added in collagen solutions. Similar effects on fibrillogenesis of type I and III collagens were observed when the core protein of decorin was added in collagen solutions. These results suggest that regulation of collagen fibrillogenesis by decorin depends on its core protein. The networks of reconstructed collagen fibrils with decorin were looser than those without decorin. Bovine skeletal muscle decorin could participate in the regulation of collagen fibrillogenesis and in the arrangement of collagen fibrils in the intramuscular connective tissue.
• 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 1344-3941 2003/10 [Refereed][Not invited]
   

  Myofibrillar proteins of vertebrate skeletal muscles are insoluble in solutions of ionic strength that approximate physiological conditions. We established a method to solubilize more than 80% of chicken breast muscle myofibrillar proteins in water for the use of meat as a source of food protein. SDS-polyacrylamide gel electrophoretic patterns of water-soluble myofibrillar proteins demonstrated that all identified myofibrillar proteins except connectin/titin were soluble in water. A part of α-actinin was released from myofibrils by repeated washing with 2.5 mmol/L NaCl and 5 mmol/L L-histidine solution, and subsequent destruction of connectin/titin in washed myofibrils by ultrasonication resulted in solubilization of a large fraction of chicken breast muscle myofibrillar proteins in water. Myofibrillar proteins of chicken leg, pork loin, beef shoulder loin, and lamb were also solubilized in water using this procedure.
• 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 1344-3941 2003/10 [Refereed][Not invited]
   

  In order to provide background for understanding biological roles of proteoglycans (PG) in developing skeletal muscle, we have isolated and characterized PG in bovine neonatal skeletal muscle. Two types of PG were isolated from skeletal muscle by density gradient ultracentrifugation and ion-exchange chromatography. One was a small PG (PG-S) with a molecular size of 100-130 kDa, another was a large PG (PG-L) with a molecular size of 300-500 kDa. The glycosaminoglycan chains of PG-S and PG-L were dermatan sulfate and chondroitin sulfate, respectively, judged by cellulose acetate membrane electrophoresis. Immunoblot assays revealed that both PG bound to type I, II, III and IV collagen, laminin and fibronectin. Unlike PG-S, PG-L bound to type V collagen and hyaluronic acid. Small proteoglycans had a core protein of 45 kDa, which reacted with the antibody against the decorin core protein. The N-terminal amino acid sequence of the PG-S core protein was consistent with that of decorin from bovine bone and tendon. Thus, PG-S from neonatal skeletal muscle was identified as decorin in bovines. Immunohistochemical analysis with antibodies against PG-L and PG-S demonstrated that PG-L was located both in the perimysium and endomysium, but PG-S was localized exclusively in the perimysium. These findings suggest that the characterized PG may have distinct roles in the ECM construction of developing skeletal muscle.
• 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 1046-0756 2003/03 [Refereed][Not invited]
   

  Paratropomyosin is a minor myofibrillar protein which in freshly prepared myofibrils is exclusively localized at the A-I junction region of sarcomeres. We investigated the ultrastructural localization of paratropomyosin in intact and postrigor myofibrils by immunoelectron microscopy. Paratropomyosin was localized as two distinct stripes at the A-I junction in intact myofibrils. It also was localized at the position corresponding to the original A-I junction in thick filament-free myofibrils (I-Z-I brushes). However, following postmortem storage, paratropomyosin was found broadly distributed in thin filaments of myofibrils.
• 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 0308-8146 2000/05 [Refereed][Not invited]
   

  We prepared sarcoplasmic proteins from bovine cardiac muscle immediately after slaughter (1.0 h; 0 days) and from stored muscle at 1, 2 and 7 days post-mortem for SDS-PAGE and Western blotting analysis. Characterization of the ubiquitin antiserum (Sigma, St Louis) showed clear and strong recognition of the ubiquitin band (8.6 kDa) and another minor band (17 kDa) in the purified ubiquitin sample (Sigma, St Louis). Among the sarcoplasmic proteins prepared from stored muscle at 0 and 7 days, this antiserum also reacted with bands corresponding to purified ubiquitin and small amounts of some other, higher-molecular-mass proteins (about 25 and 30 kDa) which were considered to be ubiquitin-protein conjugates. However, the 25 kDa band was faint in the 7 days sample, suggesting that it had degraded. We compared these results with those from oar previous study of bovine skeletal muscles, in which both ubiquitin and the ubiquitin-protein conjugates had almost disappeared in the samples tested at 10 days post mortem. (C) 2000 Elsevier Science Ltd. All rights reserved.
• Anti-Fatigue Effects of Beef

  WAKAMATSU Jun-ichi, NAGAO Tetsuji, NUMATA Masahiro, NAKAMURA Toyoo, FUJIMAKI Masao

  Nihon Chikusan Gakkaiho 社団法人 日本畜産学会 68 (6) 579 - 586 1346-907X 1997/06 [Refereed][Not invited]
   

  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 社団法人 日本食品科学工学会 44 (7) 516 - 521 1341-027X 1997 [Refereed][Not invited]
   

  ''Hanpen''-like whipped sausages with powdered yam as a foaming material were produced and evaluated by an organoleptic test and texture analysis. As the results of using a continuous whipping machine, cohesiveness of the product decreased only about 20%, but hardness, adhesiveness and gumminess decreased 67 similar to 75%. Ten% fat content was most desirable in an organoleptic test. In the experiment, the organoleptically most desirable fat and powdered yam content were 10% and 1%, respectively. Varying the specific gravity by the amount of flowing air of a continuous whipping machine, the specific gravity of the organoleptically most desirable product was 0.6 +/- 0.05. Xanthan gum and/or monoglyceride were added to improve the form stability and emulsification of products. Each evaluations of the added products was higher than a product with no addition.
• 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 0304-4165 1995/10 [Refereed][Not invited]
   

  Some characteristics of a novel 550-kDa protein which is abundant in skeletal muscle tissues at an early stage of the chick embryo, and localized in the peripheries of adult muscle fibers and at the Z-disks of isolated myofibrils, was investigated, A cosedimentation experiment and solid phase immunoabsorbent assay showed that the 550-kDa protein binds directly to F-actin. Therefore, it is concluded that the 550-kDa protein is a novel actin-binding protein. The 550-kDa protein was also interacted with alpha-actinin, taminin, fibronectin and Type IV collagen, Reactions with several kinds of lectin revealed that the 550-kDa protein is a glycoprotein containing oligosaccharides. Electron microscopic observation of negatively stained 550-kDa protein showed that native 550-kDa protein molecules are particles with an average diameter of 26.5 nm, but those particles treated with ethanol/ether are filamentous structures. These results suggest that the 550-kDa protein in the cytoplasm of unorganized skeletal muscle tissues exists as lipid-protein complex. Consequently, the 550-kDa protein may play an important role in the binding of myofibrils to the basal lamina by interaction with F-actin, cu-actinin, laminin, fibronectin or Type IV collagen.
• 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 0304-4165 1995/10 [Refereed][Not invited]
   

  We have found a novel protein with a molecular mass of 550 kDa on SDS-polyacrylamide gels, which is abundant in skeletal muscle tissues at an early stage of chick embryonic development. The 550-kDa protein decreased with the progress of development, and only a slight amount of the protein was present in adult chicken skeletal muscle. The 550-kDa protein was purified from the cytoplasm of 18 day embryos by a procedure including ultracentrifugation and gel filtration. The purified 550-kDa protein was essentially free of contaminants as judged by SDS-PAGE. By immunofluorescence and immunoelectron microscopy using the antibody raised against the 550-kDa protein, this protein was shown to be localized in the peripheries of adult muscle fibers and at the Z-disks of isolated myofibrils. These findings have led us to conclude that the 550-kDa protein is a novel myofibrillar protein in chicken skeletal muscle.

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
• Nutrition and functionality of meat protein: Difference in thermogenesis after consumption among meat species

  若松純一  アミノ酸研究  13-  (1)  21  -26  2020/02  

  食肉の新しい機能性として、摂取した食肉の食後の体熱産生能は畜種により違いがあることを明らかにし、そのメカニズムの一端を紹介した。温熱性食物は単に身体を温めるだけでなく、血流や代謝を促進し、内臓の働きを活発化し、気力を増強し、体内の水分バランスも調整し、その作用の強弱により「熱性」と「温性」に分けられる。羊肉や鶏肉などが温性に分類され、牛肉や豚肉はどちらの作用もない平性に分類される。寒涼性食物は、身体を冷やすだけでなく、炎症の抑制作用や血液の浄化作用、解毒や利尿作用、老廃物の除去作用を有するとされており、馬肉は「寒性」に、兎肉は「涼性」に分類される。鶏肉や羊肉の摂取による体温が上昇する作用には、両者の赤身部分のタンパク質が大きく寄与していることが示唆されている。
• Postprandial thermic effect of meat protein

  若松純一, 若松純一  アグリバイオ  4-  (6)  2020
• Studies on the formation and the existence form of zinc protoporphyrin IX in dry-cured ham

  若松純一  食肉に関する助成研究調査成果報告書  38-  2020
• 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]
  
• 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]
  
• 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]
  
• 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]
  
• Dietary effect of meat protein on anti‐obesity and lipid metabolism

  若松純一  食肉に関する助成研究調査成果報告書  36-  107‐112  2018/11  [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]
  
• 捕獲ストレスに着目したエゾシカの肉質評価の試み

  亀井利活, 稲富佳洋, 宇野裕之, 桑子和洋, 若松純一, 柳川洋二郎, 近藤誠司  日本哺乳類学会大会プログラム・講演要旨集  2018-  124  2018/09/08  [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]
  
• 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]
  
• 食肉・食肉製品に魅せられて

  若松純一  食肉の科学  58-  (1)  1‐10  -10  2017/06/30  [Not refereed][Not invited]
  
• 体を温める食肉,冷やす食肉

  若松純一  日本栄養・食糧学会大会講演要旨集  71st-  161  2017/04/28  [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]
  
• 胆汁酸誘導性未病状態の脱脂乳チーズによる改善作用

  高橋勇太郎, LEE Dongguen, LEE Yeonmi, JOE Gahyun, 加茂佳恵, 多田幸司, 堀将太, 花井健人, 竹内あかり, 田中愛健, 清水英寿, 若松純一, 原博, 石塚敏, 玖村朗人  日本農芸化学会大会講演要旨集(Web)  2017-  ROMBUNNO.2A08a08 (WEB ONLY)  2017/03/05  [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]
  
• 発酵乳製品用風味強化剤としてのAspergillus oryzaeの応用に関する研究

  細野誠, 齋藤千春, 谷口悠子, 小林謙, 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.3A05p09 (WEB ONLY)  2017/03/05  [Not refereed][Not invited]
  
• Searching for microorganisms with a high ZnPP-forming ability and its application to meat products

  若松純一  食肉に関する助成研究調査成果報告書  34-  12‐16  2016/11  [Not refereed][Not invited]
  
• 長期塩漬ハムの風味に寄与する微生物の探索

  森綾音, 鈴木貴弘, 西邑隆徳, 生田稔, 日置昭二, 若松純一  日本畜産学会大会講演要旨  121st-  217  2016/03/27  [Not refereed][Not invited]
  
• 馬肉摂取による体温低下作用に関する研究

  黒田裕介, 鈴木貴弘, 西邑隆徳, 若松純一  日本畜産学会大会講演要旨  121st-  216  2016/03/27  [Not refereed][Not invited]
  
• 国産乳用種牛肉と種々の牛肉に対する消費者嗜好の比較

  名倉直登, 佐々木啓介, 本山三知代, 成田卓美, 中島郁世, 小林美穂, 大江美香, 萩達朗, 尾嶋孝一, 室谷進, 野村将, 渡邊彰, 大井幹記, 宝寄山裕直, 若松純一, 西邑隆徳  日本畜産学会大会講演要旨  121st-  211  2016/03/27  [Not refereed][Not invited]
  
• 亜鉛プロトポルフィリンIX形成能が高い微生物の探索

  大屋桃, 川添穂高, 鈴木貴弘, 西邑隆徳, 若松純一  日本畜産学会大会講演要旨  121st-  216  2016/03/27  [Not refereed][Not invited]
  
• 筋原線維内の太いフィラメントにおけるミオシン分子の置換

  ICHIMURA EMI, OJIMA KOICHI, WAKAMATSU JUN'ICHI, NISHIMURA TAKANORI  日本畜産学会大会講演要旨  120th-  42  2015/09/11  [Not refereed][Not invited]
  
• 国産乳用種牛肉に対する消費者嗜好の多様性

  SASAKI KEISUKE, NAGURA NAOTO, MOTOYAMA MICHIYO, OE MIKA, NAKAJIMA IKUYO, HAGI TATSURO, OJIMA KOICHI, KOBAYASHI MIHO, NOMURA MASARU, MUROYA SUSUMU, AKAMA KYOKO, HAYASHI TAKESHI, OI MIKINORI, FUJIKAWA AKIRA, HOKIYAMA HIRONAO, IKUTA MINORU, HIKI SHOJI, CHIKUNI KOICHI, WAKAMATSU JUN'ICHI, KOBAYASHI KUNIYUKI, NISHIMURA TAKANORI  日本畜産学会大会講演要旨  120th-  106  2015/09/11  [Not refereed][Not invited]
  
• 脂肪細胞との共培養が筋芽細胞の分化に及ぼす影響

  SEO KANGMIN, WAKAMATSU JUN'ICHI, NISHIMURA TAKANORI  日本畜産学会大会講演要旨  120th-  93  2015/09/11  [Not refereed][Not invited]
  
• 鶏肉摂取が末梢体温および末梢血流に及ぼす影響

  EZOE MISAKO, WAKAMATSU JUN'ICHI, OKUMURA TOMOYUKI, MATSUMOTO TAKAYUKI, MORIMATSU FUMIKI  日本畜産学会大会講演要旨  119th-  151  2015/03/28  [Not refereed][Not invited]
  
• 鶏肉エキス摂取後の末梢体温上昇と末梢血流量および血管拡張との関係

  KUSUNOSE MUTSUMI, EZOE MISAKO, OKUMURA TOMOYUKI, MATSUMOTO TAKAYUKI, MORIMATSU FUMIKI, NISHIMURA TAKANORI, WAKAMATSU JUN'ICHI  日本畜産学会大会講演要旨  119th-  190  2015/03/28  [Not refereed][Not invited]
  
• 国産乳用種牛肉と輸入牛肉および和牛肉の消費者嗜好の比較

  NAGURA NAOTO, SASAKI KEISUKE, MOTOYAMA MICHIYO, OE MIKA, NAKAJIMA IKUYO, HAGI TATSURO, OJIMA KOICHI, KOBAYASHI MIHO, NOMURA MASARU, MUROYA SUSUMU, AKAMA KYOKO, HAYASHI TAKESHI, OI MIKINORI, FUJIKAWA AKIRA, HOKIYAMA HIRONAO, IKUTA MINORU, HIDAKA SHOJI, WAKAMATSU JUN'ICHI, KOBAYASHI KUNIYUKI, NISHIMURA TAKANORI  日本畜産学会大会講演要旨  119th-  233  2015/03/28  [Not refereed][Not invited]
  
• 各種豚骨格筋におけるZnPP形成の至適pHと筋線維型との関係

  HONMA FUMIYOSHI, NISHIMURA TAKANORI, WAKAMATSU JUN'ICHI  日本畜産学会大会講演要旨  119th-  234  2015/03/28  [Not refereed][Not invited]
  
• 分子シャペロンが太いフィラメントにおけるミオシン分子の置換に及ぼす影響

  ICHIMURA EMI, OJIMA KOICHI, WAKAMATSU JUN'ICHI, NISHIMURA TAKANORI  日本畜産学会大会講演要旨  119th-  223  2015/03/28  [Not refereed][Not invited]
  
• 国産乳用種牛肉と輸入牛肉および和牛肉の官能特性の比較

  SASAKI KEISUKE, MOTOYAMA MICHIYO, NAGURA NAOTO, NARITA TAKUMI, WAKAMATSU JUN'ICHI, CHIKUNI KOICHI, NISHIMURA TAKANORI  日本畜産学会大会講演要旨  119th-  233  2015/03/28  [Not refereed][Not invited]
  
• Myosin dynamically shuttles between myofibrils and non-myofibrillar cytosol in living skeletal muscle cells.

  E. Ichimura, K. Ojima, Y. Yasukawa, J. Wakamatsu, T. Nishimura  MOLECULAR BIOLOGY OF THE CELL  26-  2015  [Not refereed][Not invited]
  
• Replacement of myosin molecules in thick filament of cultured skeletal muscle.

  E. Ichimura, Y. Yasukawa, K. Ojima, J. Wakamatsu, T. Nishimura  MOLECULAR BIOLOGY OF THE CELL  25-  2014/12  [Not refereed][Not invited]
  
• 発色剤無添加食肉製品であるパルマハム中の新規色素,亜鉛プロトポルフィリンⅨ (2014年度(平成26年)(公社)日本畜産学会創立90周年記念号) -- (90周年記念講演ミニレビュー)

  若松 純一  日本畜産学会報  85-  (3)  428  -430  2014/08
• 鶏肉タンパク質の長期摂取は食餌性肥満ラットの褐色脂肪組織を増量させ白色脂肪組織を減少させる

  EZOE MISAKO, TAKAHATA YOSHIHISA, HASEGAWA TAKANORI, MORIMATSU FUMITAKE, NISHIMURA TAKANORI, WAKAMATSU JUN'ICHI  日本栄養・食糧学会大会講演要旨集  68回-  276  -276  2014/04  [Not refereed][Not invited]
  
• 太いフィラメントにおけるミオシン結合タンパク質の置換様相

  市村恵美, 安川裕也, 尾嶋孝一, 若松純一, 西邑隆徳  日本畜産学会大会講演要旨  118th-  154  2014/03/27  [Not refereed][Not invited]
  
• 亜鉛プロトポルフィリンIXの形成に及ぼす筋線維型の影響

  下田啓介, 西邑隆徳, 若松純一  日本畜産学会大会講演要旨  117th-  112  2013/09/09  [Not refereed][Not invited]
  
• 筋肉内結合組織を培養基質とした脂肪細胞培養系の確立

  雷暁瑩, 鈴木健司, 若松純一, 西邑隆徳  日本畜産学会大会講演要旨  117th-  108  2013/09/09  [Not refereed][Not invited]
  
• 筋細胞との共培養が脂肪前駆細胞の分化に及ぼす影響

  松本しおり, 若松純一, 西邑隆徳  日本畜産学会大会講演要旨  116th-  207  2013/03/28  [Not refereed][Not invited]
  
• 太いフィラメント内のミオシン分子はダイナミックに置き換わっている

  安川裕也, 尾嶋孝一, 若松純一, 服部昭仁, 西邑隆徳  日本畜産学会大会講演要旨  116th-  95  2013/03/28  [Not refereed][Not invited]
  
• 赤身型国産牛肉における消費者嗜好の輸入牛肉に対する違い

  佐々木啓介, 本山三知代, 千国幸一, 澤田裕介, 大井幹記, 藤川朗, 若松純一, 西邑隆徳  日本畜産学会大会講演要旨  116th-  203  2013/03/28  [Not refereed][Not invited]
  
• 食肉の食餌誘発性体熱産生能の違いは甲状腺ホルモン分泌に及ぼす赤肉タンパク質の影響の違いに起因する

  江副美紗子, 高畑能久, 長谷川隆則, 森松文毅, 西邑隆徳, 若松純一  日本畜産学会大会講演要旨  116回-  99  -99  2013/03  [Not refereed][Not invited]
  
• 酸の種類,pHおよび微生物が亜鉛プロトポルフィリンIX形成に及ぼす影響

  川添穂高, 白石阿紀子, 若松純一, 西邑隆徳  日本畜産学会大会講演要旨  115th-  242  2012/03  [Not refereed][Not invited]
  
• 水溶化ミオシンの表面疎水性およびSH基含量の加熱に伴う変化

  吉田有里, 安川裕也, 若松純一, 西邑隆徳  日本畜産学会大会講演要旨  115th-  249  2012/03  [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  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]
  
• 非加熱食肉製品における亜鉛プロトポルフィリンIX形成および色調に及ぼすpHの影響

  川添穂高, 若松純一, 西邑隆徳  日本畜産学会大会講演要旨  114th-  180  2011/08/26  [Not refereed][Not invited]
  
• 脂肪細胞におけるフォリスタチンおよびデコリンの発現

  佐竹光平, 西邑隆徳, 若松純一  日本畜産学会大会講演要旨  114th-  157  2011/08/26  [Not refereed][Not invited]
  
• 食肉中の亜鉛プロトポルフィリンIX形成に寄与する成分の探索

  白石阿紀子, 若松純一, 西邑隆徳  日本畜産学会大会講演要旨  114th-  77  2011/08/26  [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]
  
• ブタ皮下脂肪前駆細胞の分化に及ぼすミオスタチンの影響

  斎藤央, 西邑隆徳, 若松純一  日本畜産学会大会講演要旨  114th-  97  2011/08/26  [Not refereed][Not invited]
  
• 豚生産農場における液状ストレートホエイ給与が繁殖性,生産性および枝肉形質に及ぼす影響

  高萩陽一, 岩渕修, 助川慎, 中胡隆, 越田雄三, 若松純一, 村上博, 飯村裕二, 小林泰男, 森松文毅, 川島知之, 菱沼毅  日本畜産学会大会講演要旨  114th-  118  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  -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]
  
• 生ハムの都, パルマ滞在記

  若松 純一  食肉の科学  51-  (1)  25  -30  2010/06/30  [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]
  
• 鶏肉摂取による体熱産生亢進作用に関する検討

  高林尚将, 藤井亮二, 佐藤三佳子, 高畑能久, 森松文毅, 若松純一, 西邑隆徳  日本畜産学会大会講演要旨  112回-  119  -119  2010/03  [Not refereed][Not invited]
  
• ブタ皮下脂肪前駆細胞株の増殖・分化に及ぼすミオスタチンの影響

  藤田有加, 中島郁世, 千国幸一, 若松純一, 西邑隆徳  日本畜産学会大会講演要旨  111th-  69  2009/09/28  [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]
  
• 羊肉摂取による体熱産生亢進作用に関する検討

  藤井亮二, 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-  138  2009/03/27  [Not refereed][Not invited]
  
• 国内豚生産農場におけるホエイを利用した豚肉生産

  小橋有里, 小橋有里, 石黒智子, 高萩陽一, 奥村朋之, 岩渕修, 飯村裕二, 川島知之, 小林泰男, 若松純一, 服部昭人, 村上博, 森松文毅  日本畜産学会大会講演要旨  110th-  45  2009/03/27  [Not refereed][Not invited]
  
• 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]
  
• チーズホエイの飲用が豚の糞便菌叢におよぼす影響

  伊藤綾, 小池聡, 小林泰男, 若松純一, 服部昭仁, 岩渕修, 飯村裕二, 小橋有里, 小橋有里, 村上博, 森松文毅, 川島知之  日本畜産学会大会講演要旨  110th-  45  2009/03/27  [Not refereed][Not invited]
  
• Effects of Curing Agents on S-nitrosylation and the Amount of Meat Proteins

  WAKAMATSU JUN'ICHI  食肉に関する助成研究調査成果報告書  26-  32-36  2008/12  [Not refereed][Not invited]
  
• パルマハムに存在する赤色色素「亜鉛プロトポルフィリンIX」

  若松 純一  食肉の科学  49-  (2)  157  -169  2008/11  [Not refereed][Not invited]
  
• ミオスタチンと細胞外マトリックス分子の相互作用

  八坂尚史, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  109th-  139  2008/03/27  [Not refereed][Not invited]
  
• 線維芽細胞に対するミオスタチンの作用

  石橋美佳, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  109th-  138  2008/03/27  [Not refereed][Not invited]
  
• ミオシンに対する亜臨界水処理がアミノ酸の遊離およびペプチド生成に及ぼす影響

  浦木健太郎, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  109th-  74  2008/03/27  [Not refereed][Not invited]
  
• デコリンは筋芽細胞の分化を促進する

  鈴木佳介, 岸岡康博, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  109th-  143  2008/03/27  [Not refereed][Not invited]
  
• 鶏肉の体熱産生亢進作用に関する検討

  三好祥平, 藤井亮二, 山口公一, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  108th-  87  2007/09/26  [Not refereed][Not invited]
  
• プロトポルフィリンIX(PPIX)の形成に及ぼす亜硝酸塩の影響

  林宣隆, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  107th-  132  2007/03/27  [Not refereed][Not invited]
  
• 豚各種骨格筋における死後硬直時のサルコメア長に関する研究

  林珍善, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  107th-  134  2007/03/27  [Not refereed][Not invited]
  
• 食肉タンパク質に対する亜臨界水処理がアミノ酸の遊離・分解に及ぼす影響

  浦木健太郎, 高橋潤一, 阿部茂, 錦織孝史, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  107th-  131  2007/03/27  [Not refereed][Not invited]
  
• 二価金属イオン存在下におけるミオスタチンと細胞外マトリックス分子の相互作用

  高石真樹, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  107th-  102  2007/03/27  [Not refereed][Not invited]
  
• パルマハムにおける亜鉛プロトポルフィリンIX(ZPP)の存在形態

  山崎さなえ, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  107th-  132  2007/03/27  [Not refereed][Not invited]
  
• 鹿,鶏,豚および鴨肉摂取後の体熱産生の違いについて

  三好祥平, 山口公一, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  107th-  127  2007/03/27  [Not refereed][Not invited]
  
• 羊,牛および兎肉摂取後の体熱産生の違いについて

  山口公一, 三好祥平, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  107th-  127  2007/03/27  [Not refereed][Not invited]
  
• 乾塩漬ハム製造過程における亜鉛プロトポルフィリンIX(ZPP)形成と酸化還元電位

  植村寿一, 奥井潤, 小田切浩子, 林宣隆, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  107th-  131  2007/03/27  [Not refereed][Not invited]
  
• Postmortem sarcomere length characterization between Psoas major and Longissimus dorsi muscles in cattle

  I. Zapata, M. Yamaguchi, J. Wakamatsu, A. Hattori, M. Wick  JOURNAL OF ANIMAL SCIENCE  85-  380  -380  2007  [Not refereed][Not invited]
  
• Postmortem sarcomere length characterization between Psoas major and Longissimus dorsi muscles in cattle

  I. Zapata, M. Yamaguchi, J. Wakamatsu, A. Hattori, M. Wick  POULTRY SCIENCE  86-  380  -380  2007  [Not refereed][Not invited]
  
• Postmortem sarcomere length characterization between Psoas major and Longissimus dorsi muscles in cattle

  I. Zapata, M. Yamaguchi, J. Wakamatsu, A. Hattori, M. Wick  JOURNAL OF DAIRY SCIENCE  90-  380  -380  2007  [Not refereed][Not invited]
  
• 亜臨界処理による豚血液利用の実証試験

  沖浦 智紀, 飯倉 一雄, 大石 泰之, 森松 文毅, 若松 純一, 西邑 隆徳, 服部 昭仁, 山田 良司  食肉の科学  47-  (1)  159  -163  2006/06/30  [Not refereed][Not invited]
  
• デコリンは筋細胞の増殖を調節している

  野津健次郎, 岸岡康博, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  106th-  135  2006/03/20  [Not refereed][Not invited]
  
• 亜鉛プロトポルフィリンIX(ZPP)形成に及ぼすpHと遊離亜鉛濃度の影響

  植村寿一, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  106th-  165  2006/03/20  [Not refereed][Not invited]
  
• 紫色LEDとだいだい色フィルターを用いたパルマハムにおける亜鉛プロトポルフィリンIX(ZPP)の局在の観察

  小田切浩子, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  106th-  165  2006/03/20  [Not refereed][Not invited]
  
• 食肉製品中のプロトポルフィリンIX(PP IX)の形成について

  奥井潤, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  106th-  165  2006/03/20  [Not refereed][Not invited]
  
• Matrix Metalloproteinase Inhibitor Suppresses Skeletal Muscle Cell Migration In Vitro

  K. Nakamura, J. Wakamatsu, A. Hattori, T. Nishimura  MOLECULAR BIOLOGY OF THE CELL  17-  2006  [Not refereed][Not invited]
  
• 亜臨界処理による豚血液利用の実証試験

  沖浦智紀, 飯倉一雄, 大石泰之, 森松文毅, 若松純一, 西邑隆徳, 服部昭仁, 山田良司  日本食肉研究会総会提出議案及び大会講演要旨  47th-  (1)  32-36  -163  2006  [Not refereed][Not invited]
  
• 51st International Congress of Meat Science and Technology(第51回国際食肉科学技術会議)に参加して

  坂田亮一, 島田謙一郎, 西海理之, 若松純一  食肉の科学  46-  (2)  191  -214  2005/12  [Not refereed][Not invited]
  
• パルマハム中の亜鉛プロトポルフィリンIX(ZPP)はヘム以外から新たに生成される

  奥井潤, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  105th-  104  2005/08/25  [Not refereed][Not invited]
  
• 筋細胞におけるマトリックスメタロプロテアーゼの局在

  中村主貴, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  105th-  81  2005/08/25  [Not refereed][Not invited]
  
• 冷凍肉の通電解凍に及ぼす電流密度の影響

  しょう土龍, 若松純一, 西邑隆徳, 樋元淳一, 服部昭仁  日本畜産学会大会講演要旨  105th-  102  2005/08/25  [Not refereed][Not invited]
  
• reserve cellにおけるデコリンの局在と発現

  野津健次郎, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  105th-  81  2005/08/25  [Not refereed][Not invited]
  
• 中医学による食肉の分類とエネルギー産生関連物質含量との関連性

  山口公一, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  105th-  105  2005/08/25  [Not refereed][Not invited]
  
• 豚骨格筋における死後硬直時のサルコメア長の違いに関する研究

  中村幸信, 若松純一, 西邑隆徳, 服部昭仁  食肉の科学  46-  (1)  140-142  2005/06  [Not refereed][Not invited]
  
• 食肉の物理化学的特性に及ぼす通電解凍の影響

  蒋士竜, 若松純一, 西邑隆徳, 樋元淳一, 川村周三, 伊藤和彦, 服部昭仁  日本畜産学会大会講演要旨  104th-  166  2005/03/20  [Not refereed][Not invited]
  
• 豚骨格筋I型およびII型筋線維における死後硬直の違いについて

  中村幸信, 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-  167  2005/03/20  [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]
  
• パルマハム中の亜鉛プロトポルフィリンIX(ZPP)形成機構について

  奥井潤, 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-  167  2005/03/20  [Not refereed][Not invited]
  
• コネクチンのパラトロポミオシン結合断片の大腸菌での発現と精製

  山之上脈, 松田直, 若松純一, 服部昭仁  日本畜産学会大会講演要旨  104th-  180  2005/03/20  [Not refereed][Not invited]
  
• デコリンはミオスタチンを捕捉しその活性を制御する

  三浦孝之, RAVI KAMBADUR, 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-  212  2005/03/20  [Not refereed][Not invited]
  
• デコリンはミオスタチンの増殖抑制活性を制御している

  岸岡康博, RAVI KAMBADUR, 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-  212  2005/03/20  [Not refereed][Not invited]
  
• 筋衛星細胞におけるデコリンの発現と局在

  野津健次郎, 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-  211  2005/03/20  [Not refereed][Not invited]
  
• 骨格筋の発達に伴うミオスタチンおよびデコリンの発現と局在

  大山弘平, RAVI KAMBADUR, 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-  212  2005/03/20  [Not refereed][Not invited]
  
• パルマハムにおける亜鉛プロトポルフィリンIX(ZPP)の局在とフェロケラターゼの関与について

  池田有希, 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-  167  2005/03/20  [Not refereed][Not invited]
  
• 豚骨格筋における死後硬直時のサルコメア長の違いに関する研究

  中村幸信, 若松純一, 西邑隆徳, 服部昭仁  日本食肉研究会総会提出議案及び大会講演要旨  46th-  (1)  40-42  -142  2005  [Not refereed][Not invited]
  
• 研究発表 豚骨格筋における死後硬直時のサルコメア長の違いに関する研究 (研究会発表要旨 第46回日本食肉研究会大会発表要旨)

  中村 幸信, 若松 純一, 西邑 隆徳  食肉の科学  46-  (1)  140  -142  2005  [Not refereed][Not invited]
  
• Determination of zinc protoporphyrin IX in a new model system without addition of myoglobin

  51st International Congress of Meat Science and Technology (CD-ROM)  Th24  2005  [Not refereed][Not invited]
  
• Cloning and expression of DNA fragment encoding paratropomyosin binding connectin/titin domains at the A-I junction of a sarcomere

  51st International Congress of Meat Science and Technology (CD-ROM)  Th74  2005  [Not refereed][Not invited]
  
• Localization of zinc protoporphyrin IX (ZPP) in Parma ham

  WAKAMATSU J.  51st International Congress of Meat Science and Technology (ICoMST), Baltimore, Maryland USA, 2005  F26  2005  [Not refereed][Not invited]
  
• Expression and localization of decorin and myostatin during development of rat skeletal muscle

  K Oyama, J Wakamatsu, A Hattori, R Kambadur, M Sharma, T Nishimura  MOLECULAR BIOLOGY OF THE CELL  15-  303A  -303A  2004/11  [Not refereed][Not invited]
  
• Decorin rescues myostatin-induced inhibitory action to myogenic cell growth

  Y Kishioka, T Miura, J Wakamatsu, A Hattori, R Kambadur, M Thomas, M Sharma, T Nishimura  MOLECULAR BIOLOGY OF THE CELL  15-  303A  -303A  2004/11  [Not refereed][Not invited]
  
• Decorin traps myostatin and regulates its activity to myogenic cells in vitro

  T Miura, Y Kishioka, J Wakamatsu, A Hattori, R Kambadur, A Hennebry, M Sharma, T Nishimura  MOLECULAR BIOLOGY OF THE CELL  15-  303A  -303A  2004/11  [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]
  
• 通電解凍した食肉の品質について

  蒋士竜, 若松純一, 西邑隆徳, 樋元淳一, 川村周三, 伊藤和彦, 井上貞仁, 熊林義晃, 服部昭仁  日本畜産学会大会講演要旨  103rd-  187  2004/03/20  [Not refereed][Not invited]
  
• 骨格筋におけるミオスタチンおよびSmall leucine‐rich proteoglycansの局在

  大山弘平, 若松純一, RAVI K, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  103rd-  151  2004/03/20  [Not refereed][Not invited]
  
• 豚肉の熟成が筋線維および筋肉内結合組織の加熱変化に及ぼす影響

  安川淳志, 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-  187  2004/03/20  [Not refereed][Not invited]
  
• 伝統的乾塩漬食肉製品の色素形成機構に関する研究 2.食肉内在酵素の関与とその存在画分について

  池田有希, 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-  164  2004/03/20  [Not refereed][Not invited]
  
• 豚骨格筋における死後硬直時のサルコメア長と筋線維型の関係について

  中村幸信, 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-  151  2004/03/20  [Not refereed][Not invited]
  
• 伝統的乾塩漬食肉製品の色素形成機構に関する研究 1.食肉内在成分の関与について

  奥井潤, 池田有希, 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-  163  2004/03/20  [Not refereed][Not invited]
  
• デコリンは筋管の成熟に関与している

  岸岡康博, 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-  149  2004/03/20  [Not refereed][Not invited]
  
• デコリンは亜鉛イオン存在下でミオスタチンと相互作用する

  三浦孝之, 若松純一, RAVI K, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  103rd-  151  2004/03/20  [Not refereed][Not invited]
  
• パルマハムの鮮赤色は亜鉛プロトポルフィリンIXに起因

  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-  164  2004/03/20  [Not refereed][Not invited]
  
• 骨格筋量制御因子ミオスタチンと細胞外マトリックス成分との相互作用

  三浦孝之, 若松純一, 服部昭仁, KAMBADUR R, 西邑隆徳  マトリックス研究会大会  51st-  53  2004  [Not refereed][Not invited]
  
• Behavior of chicken breast muscle myosin solubilized in neutral and low ionic strength solutions

  50th International Congress of Meat Science and Technology (CD-ROM)  1.23.  2004  [Not refereed][Not invited]
  
• Zinc protoporphyrin IX contributes to the bright red color in Parma ham

  50th International Congress of Meat Science and Technology (CD-ROM)  1.59.  2004  [Not refereed][Not invited]
  
• 中性低イオン強度下のミオシンにおよぼす超音波処理の影響

  伊藤友季子, 土岐真治, 大森丘, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  101st-  226  2003/03/20  [Not refereed][Not invited]
  
• 単離した結合組織と筋線維の加熱変化について

  安川淳志, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  101st-  153  2003/03/20  [Not refereed][Not invited]
  
• ミオスタチンとデコリンの分子間相互作用のついて

  三浦孝之, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  101st-  131  2003/03/20  [Not refereed][Not invited]
  
• 酸可溶化筋原線維タンパク質の調整法とその性質

  土岐真治, 伊藤友季子, 大森丘, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  101st-  226  2003/03/20  [Not refereed][Not invited]
  
• 通電加熱による冷凍食品の解凍法に関する研究

  蒋士竜, 若松純一, 西邑隆徳, 樋元淳一, 川村周三, 伊藤和彦, 服部昭仁  日本畜産学会大会講演要旨  101st-  153  2003/03/20  [Not refereed][Not invited]
  
• ラット筋衛星細胞の増殖に及ぼすミオスタチンの影響

  岸岡康博, 若松純一, 西邑隆徳, 服部昭仁  日本畜産学会大会講演要旨  101st-  131  2003/03/20  [Not refereed][Not invited]
  
• Research of the 47th International Congress of Meat Science and Technology(Poland Krakow) and the European Meat Industry.

  WAKAMATSU JUN'ICHI  食肉に関する助成研究調査成果報告書  20-  306-329  2002/12  [Not refereed][Not invited]
  
• Effect of L-carnitine on Lipid Metabolism and the mRNA Levels in Rats Fed Cholesterol-enriched Diet.

  SHIMADA KEN'ICHIRO, FUKUSHIMA MICHIHIRO, WAKAMATSU JUN'ICHI  食肉に関する助成研究調査成果報告書  20-  255-261  2002/12  [Not refereed][Not invited]
  
• 加熱に伴う食肉の微細構造の変化

  安川淳志, 若松純一, 西邑隆徳, 服部昭仁  北海道畜産学会大会講演要旨  58th-  31  2002/08/20  [Not refereed][Not invited]
  
• アルカリ処理鶏肉を使用した含気食肉製品の開発

  三浦孝之, 若松純一, 沼田正寛, 岩崎智仁, 山本克博, 西邑隆徳, 服部昭仁  北海道畜産学会大会講演要旨  58th-  30  2002/08/20  [Not refereed][Not invited]
  
• 培養筋衛星細胞におけるミオスタチンおよびデコリンの発現

  岸岡康博, 若松純一, 西邑隆徳, 服部昭仁  北海道畜産学会大会講演要旨  58th-  31  2002/08/20  [Not refereed][Not invited]
  
• 新たな食肉製品創出のための食肉タンパク質水可溶化技術の開発

  土岐真治, 伊藤友季子, 大森丘, 井手弘, 若松純一, 西邑隆徳, 服部昭仁  北海道畜産学会大会講演要旨  58th-  30  2002/08/20  [Not refereed][Not invited]
  
• 高脂肪食投与下におけるL‐カルニチンの脂質代謝に及ぼす影響

  島田謙一郎, 今野宗, 渡辺荘子, 福島道広, 関川三男, 中野益男, 三上正幸, 若松純一  日本栄養・食糧学会総会講演要旨集  56th-  253  2002/06/20  [Not refereed][Not invited]
  
• 運動機能を補強する食肉製品の開発について

  野岳一将, 若松純一, 沼田正寛, 中村豊郎  日本食肉研究会総会提出議案及び大会講演要旨  43rd-  17-20  2002/03/29  [Not refereed][Not invited]
  
• 生体内脂質代謝における脂肪酸組成調整飼料の影響

  野岳一将, 若松純一, 沼田正寛  日本畜産学会大会講演要旨  100th-  219  2002/03/20  [Not refereed][Not invited]
  
• 動物骨由来ペプチドのアンギオテンシンI変換酵素阻害効果

  六車三治男, 上島良介, 河原聡, 山内清, 若松純一, 沼田正寛, 中村豊郎  日本畜産学会大会講演要旨  100th-  162  2002/03/20  [Not refereed][Not invited]
  
• 新規食肉加工品素材としてのアルカリ処理鶏肉

  三浦孝之, 永田悠子, 岩崎智仁, 山本克博, 若松純一, 沼田正寛, 中村豊郎  日本畜産学会大会講演要旨  100th-  166  2002/03/20  [Not refereed][Not invited]
  
• L‐カルニチン投与によるラットへの影響

  島田謙一郎, 関川三男, 三上正幸, 福島道広, 中野益男, 若松純一  日本畜産学会大会講演要旨  100th-  163  2002/03/20  [Not refereed][Not invited]
  
• Taste-active Components in Bone Marrow Extracts.

  FUKE SHIN'YA, WAKAMATSU JUN'ICHI, FUJIMAKI MASAO  食肉に関する助成研究調査成果報告書  19-  195-200  2001/12  [Not refereed][Not invited]
  
• Effect of L-carnitine on Utilization of Fatty Acid and ATP Production in Cultured Cardiac Myoblasts.

  NISHIMURA TAKANORI, WAKAMATSU JUN'ICHI, TATSUMI RYUICHI, HATTORI AKIHITO  食肉に関する助成研究調査成果報告書  19-  228-232  2001/12  [Not refereed][Not invited]
  
• Effect of L-carnitine on Lipid Metabolism and the mRNA Levels in Rats.

  FUKUSHIMA MICHIHIRO, SHIMADA KEN'ICHIRO, NAKANO MASUO, WAKAMATSU JUN'ICHI  食肉に関する助成研究調査成果報告書  19-  233-239  2001/12  [Not refereed][Not invited]
  
• 動物骨抽出成分による血圧上昇抑制活性の発現

  六車三治男, 上島良介, 河原聡, 山内清, 若松純一, 沼田正寛, 中村豊郎  日本畜産学会大会講演要旨  98th-  169  2001/03/20  [Not refereed][Not invited]
  
• 家畜・家禽の筋肉における遊離カルニチン量の比較

  島田謙一郎, 関川三男, 三上正幸, 福島道広, 若松純一  日本畜産学会大会講演要旨  98th-  165  2001/03/20  [Not refereed][Not invited]
  
• Relationship Between L-carnitine Content and Myofiber Type in Meat.

  SHIMADA KEN'ICHIRO, FUKUSHIMA MICHIHIRO, MIKAMI MASAYUKI, WAKAMATSU JUN'ICHI  食肉に関する助成研究調査成果報告書  18-  285-289  2000/12  [Not refereed][Not invited]
  
• Studies on L-carnitine Uptake and Proliferation of Myogenic Stem Cells Subjected to Mechanical Stretches.

  NISHIMURA TAKANORI, WAKAMATSU JUN'ICHI, TATSUMI RYUICHI, HATTORI AKIHITO  食肉に関する助成研究調査成果報告書  18-  290-293  2000/12  [Not refereed][Not invited]
  
• 維持透析患者における血清L‐カルニチン濃度と心機能およびQOLの検討 多施設共同研究 第1報

  松上桂子, 石塚史乃, 中村修, 須藤祐司, 永野正史, 斎藤肇, 杉本徳一郎, 正木一伸, 若松純一  日本透析医学会雑誌  33-  (Supplement 1)  850  2000/05/25  [Not refereed][Not invited]
  
• 透析食におけるL‐カルニチン含有量と素材の選択および調理方法の検討

  久保之理子, 萩原純子, 斎藤肇, 永野正史, 若松純一  日本透析医学会雑誌  33-  (Supplement 1)  663  2000/05/25  [Not refereed][Not invited]
  
• New trecd of biologically active substances I. Biologically active substances derived from of animal products and their effect.

  WAKAMATSU JUN'ICHI, HONDA KAZUHISA  ジャパンフードサイエンス  39-  (1)  52-59  -59  2000/01  [Not refereed][Not invited]
  
• エゾシカ肉の熟成に伴う筋原線維の変化について

  島田謙一郎, 関川三男, 三上正幸, 若松純一  北海道畜産学会大会講演要旨  55th-  26  1999/08/18  [Not refereed][Not invited]
  
• Cooking Loss of L-Carnitine from Beef

  Proc. 45th Int. Cogr. Meat Sci. Technol.  2-  738  -739  1999  [Not refereed][Not invited]
  
• The Functimality of L-Carnitine.

  WAKAMATSU JUN'ICHI  食品と開発  33-  (10)  43-46  -46  1998/10  [Not refereed][Not invited]
  
• Diet effect of the beef derivation L - carnitine.

  WAKAMATSU JUN'ICHI  New Food Industry  40-  (9)  1-5  -5  1998/09  [Not refereed][Not invited]
  
• An Outline of Presentation in the 42nd International Congress of Meat Science and Technology.

  OKITANI AKIHIRO, NISHIMURA TAKANORI, NISHIMURA TOSHIHIDE, WAKAMATSU JUN'ICHI, WATANABE AKIRA  食肉に関する助成研究調査成果報告書  15(1996)-  436-463  1997/12  [Not refereed][Not invited]
  
• Studies on Several Characteristics of Chinese Meat Products.

  HAYASHI TETSUHITO, REN H, GOTO SUMIO, WAKAMATSU JUN'ICHI  食肉に関する助成研究調査成果報告書  15(1996)-  285-288  1997/12  [Not refereed][Not invited]
  
• L-カルニチン含有食品素材「カルニッチ」 (特集:今後の活用が期待される食品新素材-2-)

  若松 純一  食品工業  40-  (24)  42  -47  1997/12  [Not refereed][Not invited]
  
• 第42回国際食肉科学技術会議に出席して

  沖谷 明紘, 西邑 隆徳, 西村 敏英, 若松 純一, 渡辺 彰  食肉の科学  38-  (1)  69  -86  1997/06  [Not refereed][Not invited]
  
• 肉・肉製品

  若松 純一  臨床スポーツ医学 = The journal of clinical sports medicine  13-  (0)  351  -352  1996/11  [Not refereed][Not invited]
  
• 牛肉の抗疲労効果について

  若松 純一, 長尾 哲二, 沼田 正寛, 中村 豊郎, 藤巻 正生  食肉の科学  37-  (1)  134  -137  1996/06  [Not refereed][Not invited]
  
• Anti-fatigue effect of beef.

  WAKAMATSU JUN'ICHI  日本食肉研究会総会提出議案及び大会講演要旨  37th-  15-17  1996  [Not refereed][Not invited]
  
• Anti-fatigue Effects of Beef

  Proc. 42nd Int. Cogr. Meat Sci. Technol.  40  -41  1996  [Not refereed][Not invited]
  
• Purification and Characterization of A New Protein, 650 kDa Protein, Being in Skeletal Muscle of Chick Embryo.

  WAKAMATSU JUN'ICHI, KUWAHARA KYOKO, HATTORI AKIHITO  食肉に関する助成研究調査成果報告書  12(1993)-  273-278  1994/12  [Not refereed][Not invited]
  
• 鶏骨格筋に存在する650kDa成分の性質について

  若松純一, 服部昭仁  日本畜産学会大会講演要旨  88th-  253  1994/03  [Not refereed][Not invited]
  
• 鶏骨格筋の発生における650kDa成分の発現について (第3報)

  桑原京子, 若松純一, 服部昭仁  日本畜産学会大会講演要旨  87th-  182  1993/03  [Not refereed][Not invited]
  
• 鶏骨格筋に存在する650kDa成分の単離・精製とその性質

  若松純一, 桑原京子, 服部昭仁  日本畜産学会大会講演要旨  87th-  181  1993/03  [Not refereed][Not invited]
  

Books etc

• 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 (ISBN: 9784874923542)
• 肉の機能と科学

  若松 純一 (Contributor)
  朝倉出版 2015/04 (ISBN: 9784254435504)
• Frontiers of Agricultural Science

  WAKAMATSU Jun-ichi (Contributor)
  Shoukadoh Book Sellers 2015
• 最新 畜産ハンドブック

  若松 純一 (Contributor9.2 食肉の構造・品質と加工品)
  講談社 2014/07 (ISBN: 9784061537392)
• 畜産物利用学

  齋藤 忠夫, 根岸 晴夫, 八田 一 (Contributor)
  文永堂出版 2011 (ISBN: 9784830041211)
• 食肉用語事典

  日本食肉研究会 (Contributor)
  食肉通信社 2010 (ISBN: 9784879881137)
• 栄養・食糧学用語辞典

  日本栄養食糧学会 (Contributor)
  建帛社 2007 (ISBN: 9784767961125)
• 畜産食品の事典

  細野 明義, 沖谷 明紘, 吉川 正明, 八田 一 (Contributor)
  朝倉書店 2007 (ISBN: 9784254431001)
• 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 (Joint work)
  アイ・ケイコーポレーション 2005 (ISBN: 4874922236)
• 畜産食品の事典

  細野 明義, 沖谷 明紘, 吉川 正明, 八田 一 (Contributor)
  朝倉書店 2002 (ISBN: 4254430795)
• 食品機能素材 2

  太田 明一 (Contributor)
  シーエムシー 2001 (ISBN: 488231312X)
• 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 (Contributor)
  伊藤記念財団 2001
• 食品機能素材 4

  太田 明一 
  シーエムシー (ISBN: 9784781301969)
• 食品機能素材 3

  太田 明一 
  シーエムシー (ISBN: 4882315386)

Presentations

• 肉のかたさを科学的に考えてみよう！  [Invited]

  若松 純一

  北海道食文化研究会第7回セミナー  2018/06
• 肉を食べたい！ 微生物の戦いと葛藤  [Invited]

  若松 純一

  北海道食文化研究会第4回セミナー  2017/06
• 体を温める食肉、冷やす食肉  [Invited]

  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～ 」  2017/05
• 肉の発酵と熟成  [Invited]

  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～  2016/08
• 発色剤無添加食肉製品であるパルマハム中の新規色素,亜鉛プロトポルフィリンIXについて  [Not invited]

  若松純一

  日本畜産学会大会講演要旨  2014/03
• 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  [Not invited]

  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

Association Memberships

• 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 Projects

• 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

  日本学術振興会：科学研究費助成事業

  Date (from‐to) : 2022/04 -2025/03 

  Author : 松浦 友紀子, 若松 純一, 中下 留美子, 亀井 利活
• Elucidation of mechanism by which ferrochelatase acts to form zinc protoporphyrin IX in meat and meat products

  The Ito Foundation：研究助成

  Date (from‐to) : 2023/04 -2024/03
• Development of color improvement technique of meat products by using bacteria with high ZnPP-forming ability

  Japan Society for the Promotion of Science：Grants-in-Aid for Scientific Research

  Date (from‐to) : 2020/04 -2023/03 

  Author : 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。
• Studies on ZnPP formation and color-improvement effect of meat products by food-grade Staphylococcus

  The Ito Foundation：研究助成

  Date (from‐to) : 2022/04 -2023/03
• Studies on the formation and the existence form of zinc protoporphyrin IX in dry-cured ham (III)

  The Ito Foundation：研究助成

  Date (from‐to) : 2021/04 -2022/03
• Studies on the formation and the existence form of zinc protoporphyrin IX in dry-cured ham (II)

  The Ito Foundation：研究助成

  Date (from‐to) : 2020/04 -2021/03
• Studies on the formation and the existence form of zinc protoporphyrin IX in dry-cured ham

  The Ito Foundation：研究助成

  Date (from‐to) : 2019/04 -2020/03
• 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）

  公益財団法人伊藤記念財団：平成30年度研究助成

  Date (from‐to) : 2018/04 -2019/03 

  Author : 若松 純一
• Studies on chicken and sheep meat peptides which contribute to activation of brown adipose tissue and raise body temperature after consumption

  Japan Society for the Promotion of Science：Grants-in-Aid for Scientific Research

  Date (from‐to) : 2016/04 -2019/03 

  Author : 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.
• 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

  公益財団法人伊藤記念財団：平成29年度研究助成

  Date (from‐to) : 2017/04 -2018/03 

  Author : 若松 純一
• ZnPP形成能を有する微生物の探索と応用

  伊藤記念財団：平成27年度研究助成

  Date (from‐to) : 2015/06 -2016/03 

  Author : 若松 純一
• 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

  農林水産省：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」

  Date (from‐to) : 2013 -2015 

  Author : 佐々木 啓介
• Improvement of chicken meat production by dietary zinc compounds

  Japan Society for the Promotion of Science：Grants-in-Aid for Scientific Research

  Date (from‐to) : 2012 -2014 

  Author : 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.
• Effect of zinc protoporphyrin IX on the qualities of meat products without nitrite/nitrate

  Japan Society for the Promotion of Science：Grants-in-Aid for Scientific Research

  Date (from‐to) : 2011 -2013 

  Author : 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.
• Studies on mechanism by which zinc protoporphyrin IX is formed in meat product and its applications

  Ministry of Education, Culture, Sports, Science and Technology：Grants-in-Aid for Scientific Research(基盤研究(C))

  Date (from‐to) : 2008 -2010 

  Author : 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...
• Production of additive-free meat products. Investigating into the mechanism leading to good colour dried pork meats without the use of nitrite and nitrate

  Organization for Economic Co-operation and Development (OECD)：The Co-operative Research Programme Fellowship Awards for 2009

  Date (from‐to) : 2009 -2009 

  Author : WAKAMATSU Jun-ichi
• 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

  財団法人伊藤記念財団：平成19年度研究助成

  Date (from‐to) : 2007/04 -2008/03 

  Author : WAKAMATSU Jun-ichi
• 食肉中のエネルギー代謝促進物質の探索と実用化

  独立行政法人科学技術振興機構：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

  Date (from‐to) : 2008 -2008 

  Author : 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。
• 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

  財団法人ソルト・サイエンス研究財団：平成18年度研究助成

  Date (from‐to) : 2006/04 -2007/03 

  Author : 若松 純一
• 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

  ノーステック財団：「研究開発助成事業」若手研究補助金

  Date (from‐to) : 2007 -2007 

  Author : 若松 純一
• 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

  文部科学省：科学研究費補助金(若手研究(B))

  Date (from‐to) : 2004 -2006 

  Author : 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...
• 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

  文部科学省：科学研究費補助金(萌芽研究)

  Date (from‐to) : 2004 -2005 

  Author : 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...
• Moduration of myostatin activity through extracellular matrix

  Ministry of Education, Culture, Sports, Science and Technology：Grants-in-Aid for Scientific Research(基盤研究(B))

  Date (from‐to) : 2002 -2004 

  Author : 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...
• The study on the mechanism of solubilization of myofibrillar proteins in water

  Ministry of Education, Culture, Sports, Science and Technology：Grants-in-Aid for Scientific Research(基盤研究(B))

  Date (from‐to) : 2001 -2003 

  Author : 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...

Industrial Property Rights

• 特許第7190750号:乳酸菌を含有する亜鉛プロトポルフィリンIX形成剤、並びにこれを用いた加工食品の色調改善方法及び製造方法  

  若松 純一, ムド カウサー ウル アラム, 早川 徹, 玖村 朗人  国立大学法人北海道大学  202203008675930669
• 特開2022-028150:乳酸菌を含有する亜鉛プロトポルフィリンIX形成剤、並びにこれを用いた加工食品の色調改善方法及び製造方法  2022/02/16

  若松 純一, ムド カウサー ウル アラム, 早川 徹, 玖村 朗人  国立大学法人北海道大学  202203017700400954
• 特許第4416356号:食肉・食肉加工品退色防止方法  2009/12/04

  三浦 孝之, 山本 克博, 岩崎 智仁, 若松 純一, 賀来 由夏, 沼田 正寛  山本 克博, 伊藤ハム株式会社  200903049166217770
• 特許第3949588号:天然赤色色素及び当該色素を含む食品並びに食品素材  2007/04/27

  沼田 正寛, 若松 純一  伊藤ハム株式会社  200903013836279972
• 特開2006-254818:色調を改善した食肉製品の製造方法  2006/09/28

  若松 純一, 服部 昭仁, 西邑 隆徳  国立大学法人 北海道大学  200903065416657696
• 特許第3856398号:ヘム色素による水溶性の天然着色料及びその製造方法  2006/09/22

  若松 純一, 沼田 正寛  伊藤ハム株式会社  200903031760341582
• 特開2006-056908:天然赤色色素及び当該色素を含む食品並びに食品素材  2006/03/02

  沼田 正寛, 若松 純一  伊藤ハム株式会社  200903013836279972
• 特開2006-028117:オリゴペプチド製造方法及び装置  2006/02/02

  西邑 隆徳, 服部 昭仁, 若松 純一, 竹脇 幸治, 森 徹  石川島播磨重工業株式会社  200903011531181120
• 特開2005-095037:食肉製品の色調改善方法  2005/04/14

  若松 純一, 池田 有希, 奥井 潤, 西邑 隆徳, 服部 昭仁  若松 純一  200903080512679500
• 特許第3608884号:脂質代謝改善剤及びそれを用いた食品  2004/10/22

  若松 純一, 本田 和久, 沼田 正寛  伊藤ハム株式会社  200903072745106273
• 特許第3585062号:含気性食肉製品及びその製造方法  2004/08/13

  若松 純一, 沼田 正寛, 中村 豊郎  伊藤ハム株式会社  200903008073658264
• 特許第3578566号:肥満改善及びダイエット食用素材並びにそれを用いたダイエット用食品  2004/07/23

  若松 純一, 本田 和久, 沼田 正寛  伊藤ハム株式会社  200903033896953282
• 特許第3563892号:体力増強・疲労回復剤及びそれを用いた食品  2004/06/11

  若松 純一, 本田 和久, 沼田 正寛  伊藤ハム株式会社  200903029264353215
• 特開2003-286298:新規ペプチド及びその塩  2003/10/10

  六車 三治男, 上島 良介, 若松 純一, 沼田 正寛, 中村 豊郎  伊藤ハム株式会社  200903018262435409
• 特開2003-135033:抗疲労効果を有する食肉製品  2003/05/13

  沼田 正寛, 若松 純一  伊藤ハム株式会社  200903099683761682
• 特開2003-079342:食肉・食肉加工品の物性改善方法  2003/03/18

  三浦 孝之, 山本 克博, 岩崎 智仁, 若松 純一, 沼田 正寛  山本 克博, 伊藤ハム株式会社  200903002505870482
• 特開2003-018976:食肉・食肉加工品退色防止方法  2003/01/21

  三浦 孝之, 山本 克博, 岩崎 智仁, 若松 純一, 賀来 由夏, 沼田 正寛  山本 克博, 伊藤ハム株式会社  200903049166217770
• 特開2001-057868:脂質代謝改善用素材及びそれを用いた食品  2001/03/06

  若松 純一, 和田 佳子, 沼田 正寛  伊藤ハム株式会社  200903003974535178
• 特開2001-057869:肥満改善及びダイエット食用素材並びにそれを用いたダイエット食品  2001/03/06

  若松 純一, 和田 佳子, 沼田 正寛  伊藤ハム株式会社  200903013986220496
• 特開2001-046021:体力増強・疲労回復用素材及びそれを用いた食品  2001/02/20

  若松 純一, 和田 佳子, 沼田 正寛  伊藤ハム株式会社  200903050553263770
• 特開平10-174564:畜産物由来の組合わせ健康食品  1998/06/30

  若松 純一, 鈴木 美紀, 本田 和久, 沼田 正寛, 中村 豊郎  伊藤ハム株式会社  200903069515351901
• 特開平10-113147:体力増強・疲労回復剤及びそれを用いた食品  1998/05/06

  若松 純一, 本田 和久, 沼田 正寛  伊藤ハム株式会社  200903029264353215
• 特開平10-066542:肥満改善及びダイエット食用素材並びにそれを用いたダイエット用食品  1998/03/10

  若松 純一, 本田 和久, 沼田 正寛  伊藤ハム株式会社  200903033896953282
• 特開平10-066515:脂質代謝改善剤及びそれを用いた食品  1998/03/10

  若松 純一, 本田 和久, 沼田 正寛  伊藤ハム株式会社  200903072745106273
• 特開平9-012912:ヘム色素による水溶性の天然着色料及びその製造方法  1997/01/14

  若松 純一, 沼田 正寛  伊藤ハム株式会社  200903031760341582
• 特開平9-000207:含気性食肉製品及びその製造方法  1997/01/07

  若松 純一, 沼田 正寛, 中村 豊郎  伊藤ハム株式会社  200903008073658264
• 色調を改善した食肉製品の製造方法

  2006-254818
• オリゴペプチド製造方法及び装置

  2006-028117
• 食肉製品の色調改善方法

  2005-095037
• 天然赤色色素及び当該色素を含む食品並びに食品素材

  3949588