| Project/Area Number |
06453181
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Zootechnical science/Grassland science
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| Research Institution | NIIGATA UNIVERSITY |
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Principal Investigator |
SUZUKI Atsushi Niigata University, Faculty of Agriculture, Professor, 農学部, 教授 (40018792)
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| Co-Investigator(Kenkyū-buntansha) |
IKEUCHI Yoshihide Niigata University, Faculty of Agriculture, Associate Professor, 農学部, 助教授 (90168112)
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| Project Period (FY) |
1994 – 1996
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| Project Status |
Completed (Fiscal Year 1996)
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| Budget Amount *help |
¥7,000,000 (Direct Cost: ¥7,000,000)
Fiscal Year 1996: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1995: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1994: ¥5,100,000 (Direct Cost: ¥5,100,000)
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| Keywords | high pressure treatment / sarcoplasmic reticulum / Ca^<2+>ion / mitchondria / lysosome / meat tenderization / meat conditioning / calpain / 超高圧処理 / カルシウムイオン / プロテアソーム / 食肉の高圧処理 / 食肉の軟化・熟成 / 食肉の呈味物質 |
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| Research Abstract |
High hydrostatic pressure is a new technology for tenderizing meat or accelerating meat conditioning. It has been well established that Ca^<2+> regulated by sarcoplasmic reticulum (SR) or mitochondria (Mt) is important in postmortem conversion from muscle to meat.
To clarify the mechanism for pressure-induced meat tenderization or acceleration of meat conditioning, the pressure-induced morphological and biochemical changes in SR and Mt treated with high pressure were investigated in comparison with those of the SR and Mt from conditioned muscle. The proteolytic system in the muscle was also investigated.
1) The destruction of the membrane structure of the SR and Mt expanded with increase of the pressure applied to the muscle. Significant changes in the ATPase activity, which provides the energy for Ca^<2+> uptake, were not observed in the SR and Mt preparations pressurized at less than 200 MPa.
2) The Ca^<2+> uptaking ability of the SR and Mt preparations decreased with increase of the pressure applied, and reached near zero at 200MPa.
3) Electron microscopic observation revealed that the translocation of Ca^<2+> into myofibrils was induced by high pressure treatment.
4) The cleavage of connectin under high pressure or during conditioning was caused by calpain (Ca^<2+> activated protease) in the muscle.
5) The pressure-induced increase in the amount of protease activity was due to the release of the enzyme from lysosomes. And total activities of calpain in the muscle were increased by pressure treatment.
The pressure-induced weakening of Ca^<2+> regulation and of muscular structure may be main reason for meat tenderization or accelaration of meat conditioning.
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