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
作者： Huang, Hui 1 ; He, Yanfu 1 ; Li, Laihao 1 ; Yang, Xianqing 1 ;
作者机构： 1.Chinese Acad Fishery Sci, South China Sea Fisheries Res Inst, 231 Xingang Rd, Guangzhou 510300, Guangdong, Peoples R China
2.Nanjing Agr Univ, Wuxi Fisheries Coll, Wuxi, Jiangsu, Peoples R China
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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