White Roman goose (12-wk-old male, N = 30) carcasses were obtained from a local government-inspected slaughter plant at approximately ∼10-min postmortem. Each carcass was individually sealed in a zip-lock bag and chilled immediately in a water bath at 15°C for 1 h. Both sides of Pectoralis major muscles were excised from each carcass and incubated in 30 mM CaCl2 or 30 mM EDTA at 15°C for 5 h. After incubation, calcium-incubated and EDTA-incubated breast muscles were vacuum-packaged individually and stored at 5°C for 72 h. Control samples (without CaCl2 or EDTA incubation) were directly vacuum-packaged and chilled in a water bath at 15°C for 5 h and stored at 5°C for 72 h. Muscle specimens were taken from the left side of breast muscles at 1 h of chilling (∼1-h postmortem) and at 5 h of incubation at 15°C (∼6-h postmortem), as well as 24, 48, and 72 h of aging at 5°C for measuring the activities of calpain-1 and calpain-11 as well as the contents of 80 kDa calpain-1 subunit and desmin. The samples of shear force value and myofibril fragmentation index (MFI) were taken from the right side of breast muscle at 24 h and 72 h of 5°C storage. Our results showed that the decrease of the activities of calpain-1 and calpain-11 and the contents of 80 kDa calpain-1 subunit and desmin was more rapid (P < 0.05) in calcium-incubated samples than in control and EDTA-incubated samples. The shear force was lower, but the MFI was higher in calcium-incubated samples than in control and EDTA-incubated samples (P < 0.05). Therefore, our results suggest that the calpain-mediated proteolysis and tenderization in postmortem goose muscle could be greatly enhanced by combine effects of stepwise chilling with calcium incubation at 15°C and thereafter aging at 5°C. With applying this procedure, commercial slaughter plants may have an alternative way to improve the tenderness of goose meat.
