Role of protein S-nitrosylation in regulating beef tenderness

Food Chem. 2020 Feb 15:306:125616. doi: 10.1016/j.foodchem.2019.125616. Epub 2019 Oct 5.

Abstract

This research aimed to explore the role of protein S-nitrosylation in regulating the tenderness of postmortem beef, from the perspective of μ-calpain autolysis and protein proteolysis. Five bovine semimembranosus muscles were incubated with three treatments including S-nitrosoglutathione (GSNO, nitric oxide donor), normal saline and Nω-nitro-L-arginine methyl ester hydrochloride (L-NAME, nitric oxide synthase inhibitor). The results showed that the level of protein S-nitrosylation was improved by GSNO treatment and reduced by L-NAME treatment (p < 0.05). Compared to the control, GSNO treatment had higher shear force while L-NAME treatment presented lower shear force at 7 d postmortem (p < 0.05). In addition, μ-calpain autolysis, myofibrillar protein and desmin degradation were reduced by GSNO treatment and accelerated by L-NAME treatment (p < 0.05). Therefore, it can be speculated that protein S-nitrosylation could affect beef tenderization by regulating the autolysis of μ-calpain and the degradation of myofibrillar proteins.

Keywords: Protein S-nitrosylation; Protein proteolysis; Tenderness; μ-calpain.

MeSH terms

  • Animals
  • Arginine / analogs & derivatives
  • Arginine / pharmacology
  • Calpain / metabolism
  • Cattle
  • Desmin / metabolism
  • Protein S / chemistry
  • Protein S / metabolism*
  • Proteolysis
  • Red Meat*

Substances

  • Desmin
  • Protein S
  • arginine methyl ester
  • Arginine
  • Calpain
  • mu-calpain