Effects of protein phosphorylation on color stability of ground meat. (15th March 2017)

• Record Type: Journal Article
• Authors: Li, Meng; Li, Xin; Xin, Jianzeng; Li, Zheng; Li, Guixia; Zhang, Yan; Du, Manting; Shen, Qingwu W.; Zhang, Dequan
• Is Part Of: Food chemistry. Volume 219(2017)
• Page Start: 304
• Page End: 310
• Publication Date: 2017-03-15
• Subjects: Meat color -- Protein phosphorylation -- Myoglobin -- Redox stability -- Glycolysis; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2016.09.151
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: The overall phosphorylation of sarcoplasmic proteins was altered by adding inhibitors. Meat color stability is significantly affected by protein phosphorylation. Protein phosphorylation regulates glycolysis in postmortem muscle. Phosphorylation regulates meat color by regulating glycolysis and the redox state of myoglobin. Abstract: The influence of protein phosphorylation on meat color stability was investigated in this study. Phosphatase and protein kinase inhibitors were added to minced ovine Longissimus thoracis et lumborum (LTL) muscle to manipulate the global phosphorylation of sarcoplasmic proteins. The data obtained show that the rate and extent of pH decline, along with lactate accumulation in postmortem muscle, were related to protein phosphorylation. Analysis of meat color and the relative content of myoglobin redox forms revealed that meat color stability was inversely related to the phosphorylation of sarcoplasmic proteins. Thus, this study suggests that protein phosphorylation may be involved in meat color development by regulating glycolysis and the redox stability of myoglobin.