Effect of Three Phosphates on the Phosphorylation of Myofibrillar Proteins from Silver Carp

This study investigated the effects of adding different levels of tetrasodium pyrophosphate (TSPP), sodium tripolyphosphate (STPP) or sodium hexametaphosphate (SHMP) on the structural and functional properties of myofibrillar proteins from silver carp in a low-salt (1 g/100 mL NaCl) environment. The results indicated that under low-salt conditions, the solubility, surface hydrophobicity, and emulsification properties of increased with increasing addition of phosphate. All three phosphates introduced phosphate groups into myofibrillar proteins. The pyrolysis rate of myofibrillar proteins was reduced by the addition of 0.2–0.5 g/100 mL STPP, indicating improved thermal stability. The protein was most significantly phosphorylated by the addition of 0.4 g/100 mL STPP, resulting in binding of a large number of phosphate groups to the protein. TSPP and STPP led to protein aggregation, while proteins phosphorylated by SHMP were more stable. In conclusion, the addition of 0.4 g/100 mL STPP improved the functional properties of myofibrillar proteins to a greater extent under low-salt conditions.