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The effect of sarcoplasmic protein phosphorylation on glycolysis in postmortem ovine muscle
Author(s) -
Chen Li,
Li Zheng,
Li Xin,
Chen Jing,
Everaert Nadia,
Zhang Dequan
Publication year - 2018
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.13882
Subject(s) - glycolysis , rigor mortis , phosphorylation , glycogen phosphorylase , phosphofructokinase , pyruvate kinase , sarcoplasm , adenylate kinase , protein phosphorylation , biochemistry , protein kinase a , phosphoglycerate kinase , glycogen , biology , hexokinase , enzyme , endoplasmic reticulum
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.