@article{DU2024, 
author = {Manting DU and Mengli GAO and Ziyan YOU and Ke LI and Yanhong BAI},
title = {Effect of Interaction between Protein Phosphorylation and S-Nitrosylation on Mutton Tenderness during Postmortem Storage},
year = {2024},
journal = {Food Science},
volume = {45},
number = {2},
pages = {17-23},
keywords = {tenderness, protein phosphorylation, protein S-nitrosylation, myofibrillar protein degradation},
url = {https://www.sciopen.com/article/10.7506/spkx1002-6630-20230417-162},
doi = {10.7506/spkx1002-6630-20230417-162},
abstract = {Postmortem mutton longissimus dorsi was minced and treated separately with phosphatase inhibitor, kinase inhibitor, S-nitrosoglutathione and nitric oxide synthase (NOS) inhibitor to control the degrees of phosphorylation and S-nitrosylation. The effect of interaction between protein phosphorylation and S-nitrosylation on mutton tenderness during postmortem storage were investigated by analyzing the changes in the phosphorylation level, S-nitrosylation level, pH, myofibrillar fragmentation index (MFI), desmin and troponin-T degradation of the treated mutton samples during storage at 4 ℃. The results indicated that phosphorylation levels were significantly higher (P < 0.05) in the phosphorylation-controlled group than in the phosphorylation and S-nitrosylation-controlled group in the early (0-12 h) and late (48-72 h) stages of storage, suggesting that protein S-nitrosylation inhibited its phosphorylation. When phosphorylation and S-nitrosylation modifications acted simultaneously, phosphorylation modification was dominant in affecting pH and its effect could be further enhanced by S-nitrosylation. On the contrary, S-nitrosylation played a major role in destroying the internal structure of myofibrillar proteins in mutton longissimus dorsi. When they occurred simultaneously, protein phosphorylation inhibited its S-nitrosylation; conversely, protein S-nitrosylation may promote the inhibitory effect of protein phosphorylation on desmin degradation. During postmortem storage, the interaction between protein phosphorylation and S-nitrosylation varied at different reaction periods, but both ultimately resulted in a decrease of troponin-T degradation. In conclusion, the interaction between protein phosphorylation and S-nitrosylation negatively influences the tenderness of mutton during postmortem aging.}
}