温柔
卡尔帕因
肌原纤维
组织蛋白酶B
死后变化
组织蛋白酶
化学
酶
组织蛋白酶L
肉的嫩度
ATP酶
组织蛋白酶D
细胞凋亡
钙蛋白酶抑制剂
内科学
内分泌学
生物化学
生物
病理
医学
食品科学
作者
Jun He,Fang Deng,Daodong Pan,Xiaoqun Zeng
出处
期刊:Poultry Science
[Elsevier]
日期:2019-06-14
卷期号:98 (11): 6125-6130
被引量:10
摘要
Postmortem tenderization is induced by the cooperation of various related enzymes. In this study, CaCl2 and MDL-28170 (Cbz-Val-Phe-H, a calpain inhibitor) were used to regulate the postmortem tenderization process of duck breast muscle. Then the relationship between muscle tenderness change and different enzymes was investigated. At day 0, day 1, and day 4 of the postmortem ageing, the shear force, myofibril fragmentation index (MFI), enzymatic activities of calpains, cathepsin-B, caspase-3, Na+/K+-ATPase, and Ca2+-ATPase were respectively determined. The results showed that duck muscle tenderness could be significantly raised by CaCl2 and reduced by MDL-28170, respectively (P < 0.05). The CaCl2 treatment did not promote the calpains activity as predicted (P > 0.05), but significantly up-regulated the activity of cathepsin-B (P < 0.05). The MDL-28170 significantly inhibited the activity of the calpain system at day 1 (P < 0.05) and raised the activities of the selected 3 apoptosis-related enzymes, including caspase-3, Na+/K+-ATPase, and Ca2+-ATPase, at both day 1 and day 4 (P < 0.05). These data indicated that in duck, the calpain system could be well activated after death, and cathepsin-B might also play an important role in postmortem muscle tenderization. The caspase-3, Na+/K+-ATPase, and Ca2+-ATPase probably have no significant effects on duck muscle tenderness. It might provide useful information for duck production and further research on postmortem muscle tenderization.
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