Comparative profiling of sarcoplasmic phosphoproteins in ovine muscle with different color stability. (1st February 2018)

• Record Type: Journal Article
• Authors: Li, Meng; Li, Zheng; Li, Xin; Xin, Jianzeng; Wang, Ying; Li, Guixia; Wu, Liguo; Shen, Qingwu W.; Zhang, Dequan
• Is Part Of: Food chemistry. Volume 240(2018)
• Page Start: 104
• Page End: 111
• Publication Date: 2018-02-01
• Subjects: Meat color stability -- Protein phosphorylation -- Sarcoplasmic proteins -- Myoglobin -- Glycolytic enzyme; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2017.07.097
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Difference in phosphorylation was observed among muscles of different color stability. Most color-related phosphoprotein were glycolytic enzymes. The phosphorylation of myoglobin was inversely related to meat color stability. The phosphorylation of myoglobin may regulate it' s redox stability. Difference in the phosphorylation of glycolytic enzymes may affect meat color. Abstract: 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.