Dephosphorylation enhances postmortem degradation of myofibrillar proteins. (15th April 2018)

• Record Type: Journal Article
• Authors: Li, Zheng; Li, Meng; Du, Manting; Shen, Qingwu W.; Zhang, Dequan
• Is Part Of: Food chemistry. Volume 245(2018)
• Page Start: 233
• Page End: 239
• Publication Date: 2018-04-15
• Subjects: Protein phosphorylation -- Myofibrillar protein -- Degradation -- Tenderization; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2017.09.108
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Phosphorylation was modulated by protein kinase and phosphatase inhibitor. Myosin, actin, desmin, troponin T, tropomyosin and HSP27 were analyzed. Dephosphorylation enhances degradation of some proteins during postmortem. The effect of phosphorylation depended on the degradation level. Abstract: 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.