期刊
FOOD CHEMISTRY
卷 314, 期 -, 页码 -出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2020.126203
关键词
Protein S-nitrosylation; Glycolytic enzyme; Muscle metabolism; PSE meat
资金
- National Natural Science Foundation of China [31871827]
- Jiangsu Agriculture Science and Technology Innovation Fund [CX(19)2018]
- Fundamental Research Funds for the Central Universities [KYLH201701, KYDZ201902, CARS-35]
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.
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