BACKGROUD: It is generally agreed that calpains are involved in postmortem proteolysis of skeletal muscle and improve meat tenderness. However, little information regarding the postmortem role of calpains in duck skeletal muscle is known. Therefore, the purpose of this study was to examine the role of calpains in Pekin duck postmortem breast muscles (BM) and leg and thigh muscles (LM) muscles at 5 °C.
RESULTS: The postmortem pH was lower (P < 0.05) in BM than in LM. Western blots indicated that postmortem desmin degradation and the 30/32 kDa troponin-T degradation product accumulation were more rapid in BM than in LM. Casein zymograms showed that at-death µ-calpain activity was higher in BM than in LM. As time post mortem increased, µ-calpain was activated and autolyzed more rapidly and extensively in BM than in LM, but µ/m-calpain was activated at a relative slower rate compared with µ-calpain. Correlation results showed that µ-calpain activity, rather than µ/m-calpain activity, in BM samples was highly correlated with the abundance of desmin and the 30/32 kDa troponin-T degradation components across the postmortem period. However, no such correlations were found with LM µ- and µ/m-calpains.
CONCLUSION: 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. Copyright © 2011 Society of Chemical Industry