Influence of caspase3 selective inhibitor on proteolysis of chicken skeletal muscle proteins during post mortem aging

The objective of this study was to investigate the potential contribution of apoptosis related downstream executioner caspase3 to post mortem skeletal muscle proteolysis by use of caspase3 selective inhibitor DEVD–CHO (N-acetyl–Asp–Glu–Val–Asp–CHO). After slaughter, four chicken breast muscles were removed and cut into small pieces, then marinated in treatment solution containing DEVD–CHO, or in control solution, and stored at 4 °C for 1, 3 or 7 d. Meat samples were obtained and used for detecting muscle protein degradation or calpain activity. Results showed that DEVD–CHO had inhibited the degradation of muscle skeletal proteins (titin, nebulin, desmin and troponin-T) significantly, whereas the activity of calpains had not been influenced. Therefore, the degradation of muscle proteins should not been exclusively attributed to the calpain system, and the effector caspase3 may be a new protease involved in meat post mortem tenderization.