Effect of Salting Temperature on the Protein Phosphorylation of Mutton
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Abstract:
The effect of different salting temperatures on the phosphorylation level of myofibrillar and sarcoplasmic proteins in mutton was investigated. The topside muscles from both hind legs were removed immediately after slaughter and aged at 4 ℃ for 24 h, and then three salting treatment groups were set up at -1 ℃, 4 ℃, and 25 ℃. Samples from each group were collected at 0 h, 8 h, 16 h, and 24 h, and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) combined with fluorescence staining was employed to analyze phosphorylation levels. The results showed that the global phosphorylation level (P/T) of myofibrillar proteins increased with decreasing salting temperature. After 8 h of salting, the global phosphorylation level of the myofibrillar proteins with freezing temperature treatment was significantly higher than that of the myofibrillar proteins with room temperature treatment (p<0.05), and no significant difference was found between the samples salt-treated for 16 h and those treated for 24 h. The results of the sarcoplasmic protein phosphorylation showed the opposite trend, and the global phosphorylation level of sarcoplasmic proteins decreased with decreasing salting temperature. After 8 h of salting, the global phosphorylation level of the sarcoplasmic proteins with freezing temperature treatment was significantly lower than that of the sarcoplasmic proteins with room temperature treatment (p<0.05), and no significant difference was found between the samples salt-treated for 16 h and those treated for 24 h. The effect of salting temperature on the phosphorylation level of individual protein bands was different. The phosphorylation levels of actin and aldolase increased with increasing salting temperature, while those of myosin and enolase decreased. Therefore, salting temperature can regulate the meat quality by influencing the phosphorylation of muscle proteins.
