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Phosphorylation of sarcoplasmic and myofibrillar proteins in three ovine muscles during postmortem ageing

文献类型: 外文期刊

作者: Wang Ying 1 ; Li Xin 3 ; Li Zheng 3 ; Du Man-ting 3 ; Zhu Jie 1 ; Zhang She-qi 1 ; Zhang De-quan 3 ;

作者机构: 1.Northwest A&F Univ, Inst Biophys, Lab Biomech & Engn, Yangling 712100, Shaanxi, Peoples R China

2.Northwest A&F Univ, Coll Sci, Yangling 712100, Shaanxi, Peoples R China

3.Chinese Acad Agr Sci, Minist Agr, Key Lab Agroprod Proc, Inst Food Sci & Technol, Beijing 100193, Peoples R China

关键词: ovine muscle; protein phosphorylation; mu-calpain; myofibril fragmentation index

期刊名称:JOURNAL OF INTEGRATIVE AGRICULTURE ( 影响因子:2.848; 五年影响因子:2.979 )

ISSN: 2095-3119

年卷期: 2019 年 18 卷 7 期

页码:

收录情况: SCI

摘要: This study aimed to examine changes in phosphorylation of sarcoplasmic and myofibrillar proteins from longissimus lumborum, semitendinosus, and psoas major muscles during postmortem ageing for 5 d. These sarcoplasmic and myofibrillar proteins were separated using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and stained with phosphorous and protein specific stains. Myofibril fragmentation index, pH, the content of lactic acid and the relative activity of mu-calpain in three ovine muscles were measured. These results showed that the relative phosphorylation level of sarcoplasmic and myofibrillar proteins of psoas major muscle were lower compared with longissimus lumborum and semitendinosus muscles (P<0.05). The pH of psoas major muscle was the lowest at 0.5 h postmortem, and the highest after 12 h postmortem (P<0.05). In addition, the relative activity of mu-calpain was higher within 5 d postmortem and myofibril fragmentation index was higher after 1 d postmortem in psoas major muscle than those of longissimus lumborum and semitendinosus muscles (P<0.05). The sarcoplasmic protein phosphorylation may regulate the rate of pH decline to influence the mu-calpain activity and then proteolysis of proteins consequently. This study gives a new perspective of the mechanism of postmortem meat tenderization.

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