Phosphoproteomic profiling of myofibrillar and sarcoplasmic proteins of muscle in response to salting

Abstract

A phosphoproteomic profile of myofibrillar and sarcoplasmic proteins of muscle in response to salting was investigated. Myofibrillar and sarcoplasmic proteins extracted from salted meat with 0, 1, 2, 3, 4, and 5% salt for 0, 2, 4, 6, 8, and 16 h were analyzed by SDS-PAGE electrophoresis and fluorescence staining. The global phosphorylation of myofibrillar proteins in salted meat was lower than that in control muscle at 16 h of salting (p<0.05), and the global phosphorylation of myofibrillar proteins in 3% salt-treated group at 16 h was the lowest. However, salting showed no significant effect on phosphorylation of sarcoplasmic proteins. Four categories of phosphorylated protein were identified by LC-MS/MS, involved in stress response (heat shock protein), glycometabolism (glycogen phosphorylase, glyceraldehyde-3-phosphate dehydrogenase), oxidation or reduction (superoxide dismutase), and others (myoglobin), the phosphorylation of which was affected by salting. Thus, salting may influence meat quality through protein phosphorylation, which regulates protein degradation and glycolysis.