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

被引:28
作者
Ding, Zhenjiang [1 ]
Huang, Feng [1 ,2 ,3 ]
Zhang, Chunjiang [1 ,2 ,3 ]
Zhang, Liang [1 ,2 ,3 ]
Sun, Hongxia [1 ]
Zhang, Hong [1 ,2 ,3 ]
机构
[1] Chinese Acad Agr Sci, Minist Agr, Inst Food Sci & Technol, Key Lab Agroprod Proc, Beijing 100193, Peoples R China
[2] Chinese Acad Agr Sci, Acad Food & Nutr Hlth, Hefei 238000, Anhui, Peoples R China
[3] Chinese Acad Agr Sci, Coll Staple Food Technol, Inst Food Sci & Technol, Harbin 151900, Heilongjiang, Peoples R China
基金
中国国家自然科学基金;
关键词
Caspase-3; heat shock protein 27; myofibrils; tenderisation; -calpain; POSTMORTEM STORAGE; MU-CALPAIN; MEAT TENDERNESS; MUSCLE; PROTEOLYSIS; BEEF; APOPTOSIS; QUALITY; HSP27; BIOCHEMISTRY;
D O I
10.1111/ijfs.13565
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
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.
引用
收藏
页码:121 / 128
页数:8
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