Effects of Manipulation of Proteases on Myofibril Protein Degradation of Tilapia Muscle in vitro and in vivo

文献类型： 外文期刊

第一作者： Huang, Hui

作者： Huang, Hui;He, Yanfu;Li, Laihao;Yang, Xianqing;He, Yanfu

作者机构：

关键词： Tilapia muscle; recombinant protease; protease inhibitor; myofibril; degradation

期刊名称：JOURNAL OF AQUATIC FOOD PRODUCT TECHNOLOGY （ 影响因子：1.767； 五年影响因子：1.628 ）

ISSN： 1049-8850

年卷期： 2019 年 28 卷 6 期

页码：

收录情况： SCI

摘要： This study investigated the role of three proteases in myofibril degradation. Tilapia muscle was soaked in MDL-28170, E-64, and AC-DEVD-CHO, specific inhibitors of calpain, cathepsin, and caspase, respectively, for 14 days to determine the in vivo degradation of myofibril. Desmin and troponin T were significantly inhibited after treatment with inhibitors compared to the control (p < .05). For in vitro analyses, myofibril was incubated with recombinant active mu-calpain, cathepsin B, and caspase-3. Desmin was significantly reduced when incubated with recombinant proteases (p < .05). However, troponin T showed significant degradation only in the mu-calpain and cathepsin B treatment groups (p < .05). Our results reveal mu-calpain and cathespin B have similar degradation patterns, while caspase-3 has partly similar degradation for myofibril in vivo and in vitro. This suggests that mu-calpain and cathespin B are the main proteases responsible for post-mortem myofibril degradation, while caspase-3 is minor.

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