Phosphorylation and acetylation of glycolytic enzymes cooperatively regulate their activity and lamb meat quality. (15th December 2022)

• Record Type: Journal Article
• Authors: Ren, Chi; Li, Xin; Bai, Yuqiang; Schroyen, Martine; Zhang, Dequan
• Is Part Of: Food chemistry. Volume 397(2022)
• Publication Date: 2022-12-15
• Subjects: Meat quality -- Enzyme -- Protein phosphorylation -- Protein acetylation -- Glycolysis; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2022.133739
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Slow glycolysis rate group showed lower a*, higher shear force and cooking loss. The activity of HK, PFK and PK decreased in slow glycolysis rate group. Protein phosphorylation and acetylation positively regulated HK activity. Protein phosphorylation and acetylation negatively regulated PFK activity. Phosphorylation and acetylation of PFK were closely related with meat tenderness. Abstract: This study examined cooperative regulation of phosphorylation and acetylation of glycolytic enzymes on their activity and lamb meat quality. Muscle samples were divided into two groups (fast and slow) according to their glycolysis rate as defined by pH decline rate from 1 h to 1 d postmortem. In slow glycolysis rate group, the activity of hexokinase (HK), phosphofructokinase (PFK) and pyruvate kinase (PK) was lower and meat sample showed lower a*, higher shear force and cooking loss. The acetylation and phosphorylation of HK were positively correlated with HK activity. The acetylation and phosphorylation of PFK were correlated with shear force and negatively associated with PFK activity. The acetylation and phosphorylation of PK were significantly correlated with each other but showed insignificant correlations with PK activity. Briefly, the phosphorylation and acetylation of HK, PFK and PK coregulate glycolysis through different crosstalk patterns on their activity and this might affect meat quality.