| Project/Area Number |
15208025
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| Research Category |
Grant-in-Aid for Scientific Research (A)
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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, Institution of Science and Technology, Professor, 自然科学系, 教授 (40018792)
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| Co-Investigator(Kenkyū-buntansha) |
NISHIUMI Tadayuki Niigata University, Institution of Science and Technology, Associate Professor, 自然科学系, 助教授 (60228153)
HARA Takashi Niigata University, Institution of Science and Technology, Associate Professor, 自然科学系, 助教授 (20323959)
SUGIYAMA Toshie Niigata University, Institution of Science and Technology, Assistant, 自然科学系, 助手 (10272858)
IKEUCHI Yoshihide Kyushu University, Graduate School of Agriculture, Professor, 大学院・農学研究院, 教授 (90168112)
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| Project Period (FY) |
2003 – 2005
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| Project Status |
Completed (Fiscal Year 2005)
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| Budget Amount *help |
¥27,040,000 (Direct Cost: ¥20,800,000、Indirect Cost: ¥6,240,000)
Fiscal Year 2005: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
Fiscal Year 2004: ¥5,980,000 (Direct Cost: ¥4,600,000、Indirect Cost: ¥1,380,000)
Fiscal Year 2003: ¥18,200,000 (Direct Cost: ¥14,000,000、Indirect Cost: ¥4,200,000)
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| Keywords | high pressure / muscle protein / α-actinin / intramuscular collagen / differential scanning calorimetry / calpain / proteasonme / meat allergy / 食肉の軟化 / イノシン酸 / 牛肉アレルギー / CDスペクトル / 示差走査熱量分析 / トロポニン複合体 / リソソーム膜 / カテプシン系酵素 |
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| Research Abstract |
The regulation of muscle protein by high pressure was investigated to elucidate the mechanism of pressure-induced meat tenderization and acceleration of meat conditioning focussing on the endogenous protease in the muscle. The elimination of meat allergenicity by high pressure and pressure effects on the enzymes producing taste-related components in the muscle were also investigated.
1) Effect on tropomyosin and α-actinin
(1)α-helix content of α-actinin decreased from 60% to 40% with the increase of pressure applied, while tropomyosin was resistive to high pressure.
(2)Structural changes of α-actinin by high pressure seem to be reversible under 300 MPa and not reversible over 300 MPa.
(3)Superprecipitation(SPPT)-inducing activity of α-actinin highly correlates with actin gelation activity, rather than that with ATPase acceleration.
2)Combined effects of high pressure and heat
(1)The combination of high pressure and heat treatments seem to be effective to tenderize tough meat.
(2)The shear for
… More
ce value may have some relationship with deformation of intramuscular connective tissue and myofibrils.
3)Effect on intramuscular connective tissue
(1)Not only muscle fibrils but also connective tissue was tenderized by high-pressure treatment.
(2)Pressure-dependent decrease of thermal stability and structural weakening of intramuscular collagen was observed.
4)Effect on endogenous proteases in muscle
(1)High pressure led to proteasome (one of endogenous proteases in the muscle) activation and irreversible change in the tertiary structure as detected from fluorescent measurement, whereas the change in the secondary structure was slight compared with that by heat treatment. Therefore pressure-induced activation of the proteasome seems to have been due to a small amount of unfolding of the active cites of proteasome.
(2)Changes in the localization of calpain (one of endogenous proteases in the muscle) in conditioned and pressurized bovine skeletal muscles were investigated by immunogold electron microscopy. It was clear that pressure-induced changes in calpain localization were drastic in comparison with those during conditioning.
5)Effect on allergenicity of bovine serum albumin (BSA)
(1)The effect of high pressure treatment on the elimination of BSA was evaluated on the basis of histamine release from human basophilic KU812 F cells sensitized with sera from allergic patients, and the structural changes of BSA responsible for reducing allergenicity was investigated.
(2)The reducing effect on the allergenicity gradually increased with the increase of pressure to BSA.
(3)The pressure-induced elimination of BSA allergenicity seems to be related to the tertiary structural change of BSA.
6)Effect on the enzymes producing taste-related components in the muscle
Inosinic acid (IMP; one of the umami components) was produced in meat even by high pressurization, because the enzymatic properties of the enzymes producing taste-related components in the muscle were retained in pressurized meat. Less
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