Improvement in the gelling properties of myofibrillar protein from the razor clam (Sinonovacula constricta) through phosphorylation and structural characterization of the modified protein

This study investigated the modification of myofibrillar protein (MP) from the razor clam through phosphorylation by using various phosphate salts, namely, sodium tripolyphosphate (STPP), sodium trimetaphosphate (STMP), sodium polyphosphate (STTP) and sodium pyrophosphate (TSPP), and their mechanisms of action for functional and gelling properties. Fourier transform infrared spectrometry (FTIR) showed that MP introduced phosphate groups during phosphorylation; these phosphates changed the secondary structure. Moreover, MP after phosphorylation led to an increase in solubility, which was more evident in the case of TSPP phosphorylation, leading to the improvement of gel properties. Therefore, TSPP was the phosphate with the best gel properties in the modification of MP, showing the highest phosphorus content, which resulted in better gelling properties owing to its relatively shorter chains. These results showed that phosphate was able to improve protein cross-linking through ion interactions and electrostatic interactions, which ultimately improved the gelling properties of the razor clam protein.