Role of protein S-nitrosylation in regulating beef tenderness

•Beef S-nitrosylation level was up-regulated by GSNO and down-regulated by L-NAME.•Beef tenderness was decreased by GSNO while enhanced by L-NAME treatment.•The modulation of μ-calpain activation by S-nitrosylation influenced tenderness.•The regulation of desmin degradation by S-nitrosylation affect...

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Bibliographic Details
Published in:Food chemistry 2020-02, Vol.306, p.125616-125616, Article 125616
Main Authors: Hou, Qin, Zhang, Chao-yang, Zhang, Wan-gang, Liu, Rui, Tang, Hanqi, Zhou, Guang-hong
Format: Article
Language:English
Subjects:
Animals
Arginine - analogs & derivatives
Arginine - pharmacology
Calpain - metabolism
Cattle
Desmin - metabolism
Protein proteolysis
Protein S - chemistry
Protein S - metabolism
Protein S-nitrosylation
Proteolysis
Red Meat
Tenderness
μ-calpain
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Summary:•Beef S-nitrosylation level was up-regulated by GSNO and down-regulated by L-NAME.•Beef tenderness was decreased by GSNO while enhanced by L-NAME treatment.•The modulation of μ-calpain activation by S-nitrosylation influenced tenderness.•The regulation of desmin degradation by S-nitrosylation affected tenderness. 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 
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2019.125616