温柔
卡尔帕因
提丁
肌原纤维
肉的嫩度
老化
自溶(生物学)
死后变化
最长肌
蛋白质水解
生物
胸最长肌
蛋白质降解
钙蛋白酶抑制剂
动物科学
男科
生物化学
内分泌学
医学
病理
酶
肌节
遗传学
心肌细胞
作者
Yan XiangLin,Rui Liu,Chaoyang Zhang,Xiaopu Ren,Wangang Zhang,Guanghong Zhou
摘要
Summary This study aimed to investigate the differences in meat tenderisation between two Chinese native sheep breeds, Duolang and Hu. The tenderness of longissimus thoracis (LT) muscle, μ‐calpain autolysis and proteolysis of myofibrillar protein was measured at 1‐ and 7‐days postmortem storage at 4 °C. At 7‐days postmortem ageing, meat from Duolang sheep was more tender compared to that from Hu sheep. The Warner–Bratzler shear force of Duolang and Hu sheep was reduced by 55.20% and 41.51% at 7 days compared with 1 day, respectively. In Duolang LT, a higher proportion of 80‐kDa μ‐calpain was autolyzed than in the Hu samples at 1‐day postmortem ageing, but they did not differ significantly at 7 days. More titin, desmin and troponin‐T were degraded in Duolang sheep compared to Hu sheep. Additionally, pH values at the different ageing time were not significantly different, indicating that pH may be not a determinant factor contributing to the tenderness difference between the two breeds. Our data suggest the earlier activation of μ‐calpain and a larger extent of proteolysis of key structural proteins may contribute to the higher rate of tenderisation of Duolang compared to Hu sheep during postmortem ageing.
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