Structure and functional properties of myosin induced by electrostatic fields at different pH values

Abstract

In this study, the effects of electrostatic field on myosin structure and function at different pH values were investigated. The results demonstrated that a higher surface hydrophobicity and lower sulfhydryl group content of the electrostatic field (EF) group compared to Control group (P < 0.05). The particle size, secondary structure, and microstructure investigations revealed that the EF group had decreased protein aggregation and a more stable protein structure. Furthermore, the application of electrostatic field improved the water holding capacity (WHC) of myosin gel by enhancing interaction between water molecules and protein, reducing the loss of free and immobilized water. In addition, the structure of the gel formed by electrostatic field was more stable, showing higher gel hardness and dense microstructure. The study further revealed that the internal mechanism of electrostatic field to maintain the quality of fresh meat may be related to maintaining the structural and functional activity of myosin.