Effects of temperature on protein phosphorylation in postmortem muscle
Effects of temperature on protein phosphorylation in postmortem muscle
复制标题
温度对死后肌肉蛋白质磷酸化的影响
DOI：
10.1002/jsfa.10045
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发表时间：
2020
影响因子：
4.1
通讯作者：
Zhang Dequan
中科院分区：
文献类型：
--
作者：
Ren Chi;Hou Chengli;Li Zheng;Li Xin;Bai Yuqiang;Zhang Dequan
背景磷酸化是最重要的翻译后修饰之一。目前，许多肌肉的死后蛋白质磷酸化研究已与肉质（如嫩度和颜色稳定性）相关。然而，不同储存温度（25、15、4 和−1.5°C）对蛋白质磷酸化水平的影响知之甚少。本研究测定了不同储存温度下死后绵羊肌肉蛋白质磷酸化水平的变化。结果数据显示，在-1.5℃条件下，宰后12小时至7天pH下降率受到显着抑制（P<0.05）。 25℃时ATP消耗率高于其他3个温度(P<0.05)。对温度、pH 和 ATP 含量的分析表明，ATP 含量与各个蛋白条带的磷酸化水平有关。磷酸化的肌原纤维和肌浆蛋白，如肌球蛋白结合蛋白C、肌钙蛋白T3、肌球蛋白轻链1、葡萄糖-6-磷酸异构酶和丙酮酸激酶，主要参与糖酵解和肌肉收缩。结论肌肉死后储存温度可影响整体和特异性蛋白质磷酸化水平。蛋白质的磷酸化与糖酵解和肌肉收缩相关。某些磷酸化蛋白质，例如热休克蛋白，需要进一步研究以阐明它们对肉类特性的影响。 © 2019 中国化学工业学会
BACKGROUNDPhosphorylation is one of the most important post‐translational modifications. Currently, many postmortem protein phosphorylation studies in muscle have been related to meat quality such as tenderness and color stability. However, the effects of various storage temperatures (25, 15, 4 and −1.5 °C) on the phosphorylation level of protein are poorly understood. Changes in the protein phosphorylation levels in postmortem ovine muscle at various storage temperatures were determined in this study.RESULTSThe obtained data showed that pH decline rate was significantly inhibited at −1.5 °C from 12 h to 7 days postmortem (P< 0.05). The ATP consumption rate was higher at 25 °C than that at other three temperatures (P< 0.05). Analysis of the temperature, pH and ATP content revealed that the ATP content was related to the phosphorylation levels of individual protein bands. Phosphorylated myofibrillar and sarcoplasmic proteins, such as myosin binding protein C, troponin T3, myosin light chain 1, glucose‐6‐phosphate isomerase and pyruvate kinase, were mainly involved in glycolysis and muscle contraction.CONCLUSIONThe global and specific protein phosphorylation levels can be influenced by the postmortem storage temperature of muscle. Phosphorylation of proteins was correlated with glycolysis and muscle contraction. Certain phosphorylated proteins, such as heat shock proteins, require further study to clarify their effects on meat traits. © 2019 Society of Chemical Industry