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Updated: Sep 2, 2025

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
Published on: December 9, 2017
Phosphorylation and acetylation of glycolytic enzymes cooperatively regulate their activity and lamb meat quality
Chi Ren1, Xin Li2, Yuqiang Bai2
1Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs, Beijing 100193, PR China; Precision Livestock and Nutrition Unit, Gembloux Agro-Bio Tech, University of Liège, Passage de Déportés 2, Gembloux, Belgium.
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.
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