Comparative profiling of sarcoplasmic phosphoproteins in ovine muscle with different color stability.

Meng Li, Zheng Li, Xin Li, Jianzeng Xin, Ying Wang, Guixia Li, Liguo Wu, Qingwu W Shen, Dequan Zhang

Food chemistry 2018 Feb 01

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The phosphorylation of sarcoplasmic proteins in postmortem muscles was investigated in relationship to color stability in the present study. Although no difference was observed in the global phosphorylation level of sarcoplasmic proteins, difference was determined in the phosphorylation levels of individual protein bands from muscles with different color stability. Correlation analysis and liquid chromatography - tandem mass spectrometry (LC-MS/MS) identification of phosphoproteins showed that most of the color stability-related proteins were glycolytic enzymes. Interestingly, the phosphorylation level of myoglobin was inversely related to meat color stability. As the phosphorylation of myoglobin increased, color stability based on a∗ value decreased and metMb content increased. In summary, the study revealed that protein phosphorylation might play a role in the regulation of meat color stability probably by regulating glycolysis and the redox stability of myoglobin, which might be affected by the phosphorylation of myoglobin. Copyright © 2017 Elsevier Ltd. All rights reserved.

Citation

Meng Li, Zheng Li, Xin Li, Jianzeng Xin, Ying Wang, Guixia Li, Liguo Wu, Qingwu W Shen, Dequan Zhang. Comparative profiling of sarcoplasmic phosphoproteins in ovine muscle with different color stability. Food chemistry. 2018 Feb 01;240:104-111