Comparative analysis of muscle phosphoproteome induced by salt curing. (November 2017)

• Record Type: Journal Article
• Authors: Wang, Zhenyu; Zhang, Caixia; Li, Zheng; Shen, Qingwu; Zhang, Dequan
• Is Part Of: Meat science. Volume 133(2017)
• Page Start: 19
• Page End: 25
• Publication Date: 2017-11
• Subjects: Differential phosphorylated proteins -- Salting -- Sodium chloride -- Phosphorylation -- Glycolysis; Meat -- Periodicals; Meat industry and trade -- Periodicals; Viande -- Périodiques; Viande -- Industrie -- Périodiques; Meat; Meat industry and trade; Periodicals; 641.36
• DOI: 10.1016/j.meatsci.2017.05.018
• Languages: English
• ISSNs: 0309-1740

Abstract

Abstract: Phosphorylated proteins in ovine muscle induced by salt curing were well investigated. Ten topside muscles of crossbred sheep were ground, mixed and divided into two groups, which were cured for 16 h with 0% and 3% NaCl, respectively. Muscle proteins of two cured groups were analyzed by two-dimensional electrophoresis coupled with Pro-Q Diamond and SYPRO Ruby staining. The differential phosphorylated proteins were determined using LC-MS/MS and the UniProt database. Ten different phosphoproteins (> 1.5 fold) induced by salting were identified, including triosephosphate isomerase, glycogen phosphorylase, creatine kinase M-type, myoglobin, troponin T fast skeletal muscle type, actin, myosin light chain 1/3, tropomyosin beta chain, etc. Most of the different phosphoproteins were involved in glycometabolism, protein function and protein degradation. It is conclusively that salting may influence meat quality through protein phosphorylation, which regulates glycolysis metabolism, protein function and degradation. Highlights: Muscle phosphoproteome induced by salt curing was analyzed. Glycogen phosphorylase, troponin T and other eight proteins induced (> 1.5 fold) by salting were identified. Phosphorylation regulates glycolysis metabolism, protein function and degradation of muscle in curing. Curing influence meat quality through protein phosphorylation.