Abstract
Consumers focus on tenderness and flavor when eating goose meat. This study was conducted to determine the mechanism by which goose muscle becomes tender. Changes in reactive oxygen species (ROS) and myofibril proteins (titin, nebulin, desmin, troponin-T, and β-actin) were analyzed, and the main activated proteins' (caspase-3 and caspase-9) expression levels were examined using western blot analysis. Caspase activity was compared and analyzed across different storage times using a substrate method. Significant variations in troponin-T (approximate 35kDa) and β-actin were detected between samples suspended in 10mmol/l hydrogen peroxide (H2O2) and N-acetyl cysteine (NAC) for various time periods. The data demonstrated that as goose muscle matured there were changes in proteins (titin, nebulin, desmin, troponin-T, and β-actin) and the activated fragments of caspase-3 and caspase-9, with their activities showing a significant negative correlation (P<0.05). The mean fluorescence intensity of dichlorofluorescein (DCF) in the control group was lower than the disposed groups treated with 10mmol/l H2O2, and goose meat aged 2days showed higher dihydroethidium (DHE) levels than that shown by the 0d samples.
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