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Effect of heat shock protein 27 on the in vitro degradation of myofibrils by caspase‐3 and μ‐calpain
Author(s) -
Ding Zhenjiang,
Huang Feng,
Zhang Chunjiang,
Zhang Liang,
Sun Hongxia,
Zhang Hong
Publication year - 2018
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.13565
Subject(s) - myofibril , calpain , desmin , myofilament , nebulin , titin , protein degradation , proteolysis , heat shock protein , troponin , chemistry , troponin i , microbiology and biotechnology , sarcomere , biochemistry , biology , actin , myocyte , medicine , enzyme , immunology , vimentin , immunohistochemistry , myocardial infarction , gene
Summary This study was designed to investigate the effect of heat shock protein 27 ( HSP 27) on the in vitro degradation of myofibrils induced by caspase‐3 or μ‐calpain. Myofibrillar proteins were prepared from at‐death beef muscles and incubated with caspase‐3 or μ‐calpain with and without HSP 27, or with HSP 27 alone, at 30 °C for 2 h, and protein degradation was assessed. Results showed that caspase‐3 promoted the degradation of titin, nebulin and troponin‐T, and μ‐calpain promoted the degradation of nebulin, desmin and troponin‐T, observed during normal PM ageing. Moreover, the addition of HSP 27 restricted the degradation of troponin‐T in μ‐calpain‐ and caspase‐3‐treated myofilaments, and restricted the degradation of desmin in μ‐calpain‐treated myofilaments. Therefore, HSP 27 may indirectly or directly interact with caspase‐3 and μ‐calpain, reducing their activity and mediating PM proteolysis of muscle proteins to affect meat tenderisation.