Dephosphorylation enhances postmortem degradation of myofibrillar proteins.
Protein degradation is primarily responsible for postmortem meat tenderization, which might be affected by phosphorylation. The objective of this study was to investigate the effect of phosphorylation on myofibrillar proteins degradation in muscle during postmortem. Here we modulated the phosphorylation status of protein by protein kinase inhibitor and phosphatase inhibitor, and the effect of these inhibitors on myofibrillar protein degradation was evaluated. Generally, myofibril fragmentation index of samples with lower phosphorylation level was higher. Troponin T and heat shock protein 27 were degraded faster in protein kinase inhibited (low phosphorylation level) muscle, compared with the other two groups, while the degradation of desmin was not affected by inhibitors. Meanwhile, myosin heavy chain, actin and tropomyosin showed limited degradation in postmortem muscle. This study showed that dephosphorylation enhances the degradation of some myofibrillar proteins, indicating that protein phosphorylation may play an important role in postmortem meat tenderization.
['Li|Zheng|Z|', 'Li|Meng|M|', 'Du|Manting|M|', 'Shen|Qingwu W|QW|', 'Zhang|Dequan|D|']
D000199:Actins D000818:Animals D003893:Desmin D055551:HSP27 Heat-Shock Proteins D008460:Meat D009124:Muscle Proteins D018482:Muscle, Skeletal D009210:Myofibrils D018995:Myosin Heavy Chains D010749:Phosphoprotein Phosphatases D010766:Phosphorylation D011180:Postmortem Changes D047428:Protein Kinase Inhibitors D059748:Proteolysis D012756:Sheep D014335:Tropomyosin D020107:Troponin T
Degradation Myofibrillar protein Tenderization Protein phosphorylation