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

Food Chem. 2020 Jun 1:314:126203. doi: 10.1016/j.foodchem.2020.126203. Epub 2020 Jan 13.

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.

Keywords: Glycolytic enzyme; Muscle metabolism; PSE meat; Protein S-nitrosylation.

Publication types

  • Comparative Study

MeSH terms

  • Animals
  • Color
  • Glycogen / metabolism
  • Glycogen Phosphorylase / metabolism
  • Glycolysis*
  • Muscle, Skeletal / enzymology
  • Muscle, Skeletal / metabolism*
  • Nitric Oxide / metabolism*
  • Nitric Oxide Synthase / metabolism*
  • Phosphofructokinases / metabolism
  • Pork Meat / analysis*
  • Pyruvate Kinase / metabolism
  • Swine

Substances

  • Nitric Oxide
  • Glycogen
  • Nitric Oxide Synthase
  • Glycogen Phosphorylase
  • Phosphofructokinases
  • Pyruvate Kinase