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Updated: Dec 18, 2025

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
Published on: December 9, 2017
Acetylation and Phosphorylation of Proteins Affect Energy Metabolism and Pork Quality
Bo Zou1, Di Zhao1, Guangjie He1
1Key Laboratory of Meat Processing and Quality Control, MOE; Key Laboratory of Meat Processing, MARA; Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, College of Food Science and Technology, Nanjing Agricultural University, 210095 Nanjing, China.
Abstract:
Preslaughter handling has been shown to significantly affect meat quality, but the mechanisms are not fully understood. In this study, we investigated protein phosphorylation and acetylation in pig muscles at early postmortem time and their associations with meat quality attributes. Thirty pigs were randomly assigned to traditional (TH, n = 15) or mild handling (MH, n = 15). Compared with TH, MH reduced the incidence of pale, soft, and exudative (PSE) or dark, firm, and dry (DFD) pork. MH induced 65 and 20 peptides that match with 39 and 12 proteins to be more highly phosphorylated and acetylated, respectively. Creatine kinase, β-enolase, α-1,4-glucan phosphorylase, tropomyosin, and myosin heavy chain isoforms 1, 4, and 7 were found to be simultaneously phosphorylated and acetylated, which may involve glycolysis, tight junctions, and muscle contraction. The phosphorylation and acetylation levels of differential proteins showed significant correlations with meat quality traits. These findings indicate that preslaughter MH can improve meat quality by regulating protein phosphorylation and acetylation involving energy metabolism in muscle.
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