Calpain activation and proteolysis in postmortem goose muscles

Area of Science:

• Food Science
• Animal Science
• Biochemistry

Background:

• Meat tenderness is a key consumer-driven quality attribute.
• Endogenous proteases, particularly calpains, enhance meat tenderness during postmortem storage.
• Understanding calpain activity is crucial for optimizing meat processing.

Purpose of the Study:

• To investigate postmortem calpain activation and proteolysis in White Roman goose breast (BM) and leg and thigh (LM) muscles.
• To compare the rate and extent of proteolysis between BM and LM.
• To identify factors influencing postmortem changes in goose meat.

Main Methods:

• Goose carcasses (n=15) were sampled at 0, 1, 3, and 7 days postmortem.
• Muscles (BM and LM) were stored at 5°C.
• Postmortem pH, calpain-1 and -11 activities, calpain-1 80 kDa subunit, and desmin content were analyzed.

Main Results:

• Postmortem pH decline, calpain activity, and desmin degradation were significantly faster in BM compared to LM.
• Proteolysis was more extensive in BM than in LM.
• Greater calpain activation rates and extents were observed in BM.

Conclusions:

• Postmortem proteolysis differs significantly between goose breast and leg/thigh muscles.
• Differences in calpain activation and fiber composition contribute to variations in proteolysis.
• Findings offer insights for optimizing goose meat processing based on muscle type.