Effect of heat shock protein 27 on the invitro degradation of myofibrils by caspase-3 and -calpain

文献类型： 外文期刊

第一作者： Ding, Zhenjiang

作者： Ding, Zhenjiang;Huang, Feng;Zhang, Chunjiang;Zhang, Liang;Sun, Hongxia;Zhang, Hong;Huang, Feng;Zhang, Chunjiang;Zhang, Liang;Zhang, Hong;Huang, Feng;Zhang, Chunjiang;Zhang, Liang;Zhang, Hong

作者机构：

关键词： Caspase-3;heat shock protein 27;myofibrils;tenderisation;-calpain

期刊名称：INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY （ 影响因子：3.713； 五年影响因子：3.408 ）

ISSN： 0950-5423

年卷期： 2018 年 53 卷 1 期

页码：

收录情况： SCI

摘要： This study was designed to investigate the effect of heat shock protein 27 (HSP27) on the invitro degradation of myofibrils induced by caspase-3 or -calpain. Myofibrillar proteins were prepared from at-death beef muscles and incubated with caspase-3 or -calpain with and without HSP27, or with HSP27 alone, at 30 degrees C for 2h, and protein degradation was assessed. Results showed that caspase-3 promoted the degradation of titin, nebulin and troponin-T, and -calpain promoted the degradation of nebulin, desmin and troponin-T, observed during normal PM ageing. Moreover, the addition of HSP27 restricted the degradation of troponin-T in -calpain- and caspase-3-treated myofilaments, and restricted the degradation of desmin in -calpain-treated myofilaments. Therefore, HSP27 may indirectly or directly interact with caspase-3 and -calpain, reducing their activity and mediating PM proteolysis of muscle proteins to affect meat tenderisation.

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