1992 Fiscal Year Final Research Report Summary
Mechanism of Postmortem Tenderization of Meat Estimated by Monoclonal Antibody
| Project/Area Number |
02453135
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
畜産化学
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| Research Institution | NIIGATA UNIVERSITY |
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Principal Investigator |
SUZUKI Atsushi Niigata University, Fac. of Agric., Professor, 農学部, 教授 (40018792)
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| Co-Investigator(Kenkyū-buntansha) |
IKEUCHI Yoshihide Niigata University, Faculty of Agric., Associate Professor, 農学部, 助教授 (90168112)
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| Project Period (FY) |
1990 – 1992
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| Keywords | Titin / Connectin / Monoclonal antibody / Meat tenderization / Thaw rigor / Meat conditioning / Myofibrillar protein / High pressure treatment of meat |
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| Research Abstract |
The mechanism of thaw rigor and tenderization of meat was studied by using monoclonal antibody against myofibrillar protein. Following results were obtained.
1. Production of monoclonal antibody against native connection or titn was successful. The identity of connectin and titin in the native state was immunologically suggested on the basis of immuno-blotting and ELISA methods.
2. The factors affecting the conversion of alpha-connectin to beta-connectin induced by pressurization of muscle were investigated over a pressure range from 100 to 400 MPa by using SDS-PAGE and immuno-blot analysis. When muscles were exposed to high pressure, the conversion of alpha-connectin to beta-connectin was markedly accelerated by pressurization at 200 MPa, but further increase of the con-version was not observed in the muscle pressurized at 300 and 400 MPa. The ability of calcium-activated protease ( CAF ) to hydrolyze connectin from alpha to beta was gradually reduced with increasing intensity of pressure. The obtained results indicates that CAF is responsible for the pressure-induced conversion of alpha- to beta-connectin.
3. The immunoelectron microscopic studies using monoclonal antibody against connectin or titin revealed that the antibody-binding stripes between connectin and titin were different. One distinct antibody-binding stripe was recognized at the both side of the H-zone in the center of the A-band in the fiber bundles treated with antibody against connectin, while two stripes were recognized in each half of the A-band in the fiber bundles treated with antibody against titn. The gradual degradation of the stripe recognized at the both side of the H-zone in the fiber bundles treated with antibody against connectin was observed in the muscle stored at 2ﾟC for 7 days. This is one of the evidence that the filament structure consisting of connectin is gradually degraded during postmortem conditioning.
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