A comparative analysis of phosphoproteome in ovine muscle at early postmortem in relationship to tenderness

文献类型： 外文期刊

第一作者： Li, Xin

作者： Li, Xin;Chen, Lijuan;He, Fan;Li, Meng;Zhang, Dequan;Shen, Qingwu

作者机构：

关键词： lamb;meat quality;tenderness;phosphoproteome

期刊名称：JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE （ 影响因子：3.638； 五年影响因子：3.802 ）

ISSN： 0022-5142

年卷期： 2017 年 97 卷 13 期

页码：

收录情况： SCI

摘要： BACKGROUND: Tenderness is considered to be the most important quality characteristic of meat as it is the main cause of unacceptability of meat. Post-translational modification regulates protein functions that involve in postmortem changes in muscle and meat quality formation. Specifically, phosphorylation was proved to regulate postmortem glycolytic rates and meat tenderisation. However, the relationship between protein phosphorylation and meat tenderness remains unclear. This study examined the phosphoproteomes found in ovine muscle with different degrees of tenderness over time (at 0.5 h, 4 h, and 24 h postmortem). RESULTS: This study detected five, eight and nine phosphoprotein spots (> two-fold change, P < 0.05) at each respective time point. The different phosphoproteins found included glyceraldehyde-3-phosphate dehydrogenase, tropomyosin alpha-1 chain, pyruvate kinase, myosin binding protein H, glycogen phosphorylase, alpha-actinin-3, and an uncharacterised protein (GN, myosin-binding protein C2, MYBPC2). Most of the different phosphoproteins maintained sarcomeric functions, or were involved in glycometabolism. CONCLUSION: Phosphorylation levels of multiple proteins that are involved in glycolysis, muscle contraction or sarcomeric structure integrity were identified in ovine muscles with different tenderness. The differential phosphorylation of these proteins explains in part the difference in meat tenderness. (C) 2017 Society of Chemical Industry

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