To study the effects of ultrasound, phosphorylation, and ultrasound combined with phosphorylation on the gel properties of egg white protein, considering the order of composite modification, the gel properties of egg white protein before and after modification were determined. The changes in molecular weight, spatial structure, surface hydrophobicity, particle size, and zeta potential of egg white protein before and after modification were analyzed. Results showed that ultrasound and phosphorylation significantly improved the gel hardness and water-holding capacity of egg white protein, while phosphorylation had a negative effect on water-holding capacity. The optimum ultrasonic conditions for improving the hardness of egg white protein gel were 150 W and 5 min, which was 21.22% higher than that of the blank group. The phosphorylation conditions were sodium tripolyphosphate addition of 0.8%, time of 2 h, a temperature of 45 ℃, and pH 9, which was 15.65% higher than that of the blank group. The composite modification of phosphorylation first and then ultrasound was the most significant, 63.19% higher than that of the blank group. The effect of each modification method on the molecular weight of egg white protein was not significant. Ultrasound promoted the depolymerization of protein molecules and smaller particle sizes exposed more hydrophobic groups. As the potential decreased, the solution tended to be unstable, and phosphorylation inhibited this trend to some extent. The composite modification improved the hardness of the egg white protein gel and the stability of the solution to a certain extent. The composite modification provides a reference for improving the gel properties of egg white.
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