The effect of sarcoplasmic protein phosphorylation on glycolysis in postmortem ovine muscle

Abstract Protein phosphorylation is a key modulator in glycolysis metabolism and regulates the activity of glycometabolic enzymes. The phosphorylation levels of sarcoplasmic proteins were investigated in relationship to the glycolysis rate in postmortem ovine muscle in the present study. The global phosphorylation levels of sarcoplasmic proteins increased early postmortem and then decreased afterwards in postmortem ovine muscle. Protein bands of different phosphorylation levels were identified as glycometabolism‐related enzymes. The phosphorylation levels of Glycogen phosphorylase and Pyruvate kinase maybe one possible reason for the different glycolytic rates at 0.5 h postmortem. The glycolytic rate attributes were negatively correlated with four bands which were probably phosphofructokinase, enolase and adenylate kinase isoenzyme. In summary, the phosphorylation of sarcoplasmic proteins is related to muscle pH decline early postmortem, influencing the meat rigour mortis and quality development.