Effect of hydroxyl radical‐induced oxidation on the structure and heat‐induced gel properties of ovalbumin.

Abstract: The present study is aimed to investigate the effect of hydroxyl radical‐induced oxidation on the structure and gel properties of chicken ovalbumin. With the increase in oxidation time and H₂O₂ dose, the carbonyl content in ovalbumin increased, while the free sulfhydryl content decreased. The effect of oxidation on the structure of ovalbumin was examined, and the results indicated that the disorder level increased. Oxidation of ovalbumin lowered the solubility, and the viscosity of the solution decreased significantly. Oxidation weakened the water holding capacity and gel hardness, as well as resulting in significant changes in the microstructure of ovalbumin gels. Hydroxyl radical‐induced oxidation caused destabilization of the ovalbumin structure, thereby affecting the heat‐induced gel properties. Practical applications: The present study demonstrated the effect of hydroxyl radical‐induced oxidation on chicken OVA, concluding that the oxidation might be one of the primary reasons for the degradation of its gel properties. Consequently, avoiding protein oxidation during storage and processing would help maintain the functional properties of the chicken egg white. Therefore, this study provides important information for the research and application of ovalbumin. [ABSTRACT FROM AUTHOR]