Dephosphorylation of myosin regulatory light chain modulates actin–myosin interaction adverse to meat tenderness. (June 2017)

• Record Type: Journal Article
• Authors: Gao, Xing; Li, Xin; Li, Zheng; Du, Manting; Zhang, Dequan
• Is Part Of: International journal of food science & technology. Volume 52:Number 6(2017)
• Page Start: 1400
• Page End: 1407
• Publication Date: 2017-06
• Subjects: Actomyosin dissociation -- ATPase activity -- dephosphorylation -- myosin regulation light chain; Food industry and trade -- Periodicals; 664
• DOI: 10.1111/ijfs.13343
• Languages: English
• ISSNs: 0950-5423

Abstract

Summary: The objective of this study was to investigate the relationship between the dephosphorylation of myosin regulatory light chain and actin–myosin interaction after muscle homogenate was treated with alkaline phosphatase and phosphatase inhibitor. The myosin regulatory light chain was significantly dephosphorylated by alkaline phosphatase after incubation. Among different groups, dephosphorylated myosin regulatory light chain to a much greater extent leads to a lower actomyosin dissociation degree, thereby raising the actomyosin ATPase activity, whereas it exhibits a higher actomyosin dissociation degree and a lower actomyosin ATPase activity when the myosin regulatory light chain was in a low dephosphorylated state. The data suggest that the dephosphorylation of myosin regulatory light chain modulates actomyosin dissociation (the number of myosin interact with actin) negatively and has a positive influence on actomyosin ATPase activity (the interacting force between myosin and actin). Abstract : The role of dephosphorylation of myosin regulatory light chain in actin–myosin interaction was determined. Dephosphorylated myosin regulatory light chain to a much greater extent leads to a lower actomyosin dissociation degree, thereby raising the actomyosin ATPase activity.