Temperature-orientation changes in ROS-oxidized egg white protein conformation modulate the thermal aggregation behavior

In this paper, the differences in thermal aggregation behavior of egg white protein (EWP) mediated by reactive oxygen species (ROS) at different heat temperatures were investigated. Results showed that an increase in EWP turbidity and the change in particle size during the heating process depended on the interactions after protein peptide chain unfolding. With the increase in heating temperature, the EWP aggregates changed from indeterminate fiber-like structure to regular network structure. The thermal stability results showed an increase in the thermal stability of EWP after oxidation. The formation of thermally induced aggregates was accompanied by a significant increase in the hydrophobicity of the protein surface from 249.93 to 2748.10. Raman spectroscopy indicated that oxidized EWP exposed hydrophobic groups to inhibit aggregation during heating, and EWP demonstrated significant anti-aggregation properties when heated at 72 °C. This study provides certain theoretical support for improving the thermal processing level of egg products.