Effects of temperature on protein phosphorylation in postmortem muscle.

Abstract

Phosphorylation 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. The 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. The 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.