Comparison of activity, expression and S-nitrosylation of glycolytic enzymes between pale, soft and exudative and red, firm and non-exudative pork during post-mortem aging. (1st June 2020)

• Record Type: Journal Article
• Authors: Wang, Yingying; Liu, Rui; Hou, Qin; Tian, Xiaona; Fan, Xiaoquan; Zhang, Wangang; Zhou, Guanghong
• Is Part Of: Food chemistry. Volume 314(2020)
• Publication Date: 2020-06-01
• Subjects: Protein S-nitrosylation -- Glycolytic enzyme -- Muscle metabolism -- PSE meat; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2020.126203
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: The method has significant advantage in identifying S-nitrosylated protein. S-nitrosylation of those enzymes for postmortem meat is still unknown. Protein S-nitrosylation may exert effect on glycolysis. It is a new insight to explain PSE meat in postmortem muscle. Abstract: The activity, expression and S-nitrosylation of glycogen phosphorylase (GP), phosphofructokinase (PFK) and pyruvate kinase (PK) was compared between pale, soft and exudative (PSE) and red, firm and non-exudative (RFN) pork. The nitric oxide synthase (NOS) activity of RFN pork was higher than PSE pork (P < 0.05). Glycogen and lactic acid content were significantly different between PSE and RFN samples at 1 h postmortem (P < 0.05). Compared to PSE pork, RFN pork had lower activities and higher S-nitrosylation levels of GP, PFK and PK (P < 0.05). Moreover, GP expression in RFN pork was lower (P < 0.05) while no significant differences of PFK and PK expression were observed between these two groups. These data suggest that protein S-nitrosylation can presumably regulate glycolysis by modulating glycolytic enzymes activities and then regulate the development of PSE pork.