Therefore, our results suggest that BM µ-calpain with a faster and more extensive activation and autolysis would play a relatively dominant role in dictating degradation of desmin and troponin-T in postmortem duck muscle.

Our results suggest that the more rapid postmortem proteolysis found in BM than in LM at 5 °C similar with the previous study could be mainly explained by both greater amounts and faster activation and autolysis of µ-calpain in BM.

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Post mortem ageing at 4°C was studied in the breast and leg muscles from broilers, White Leghorn spent hens and Taiwanese Country Chickens (TCC). Purified myofibrils were prepared from muscles after 0, 1, 3, 5, and 7 days of post mortem storage at 4°C. SDS-PAGE was used to examine the changes in myofibrillar proteins of the muscles. Results showed that 30 kDa components appeared earlier in the breast muscles than in the leg muscles and in the order: broiler, TCC, and spent hen. The intensity of 30 kDa band increased with post mortem time. In the breast muscles, a decrease in the intensity of the a-actinin band could be observed at 1 day post mortem in broilers and TCC and at 3 days post mortem in spent hens. This decrease, however, could not be found in the leg samples until 5 or 7 day post mortem. Titin 1 band disappeared within 3 day post mortem in the breast samples but within 5 days in the leg samples. Similar results could be observed in the degradation of nebulin although traces of nebulin remained in the leg muscles of TCC after 7 days post mortem

No abstract