Investigating the hydrogen peroxide quenching capacity of proteins in polyphenol-rich foods

Polyphenols are widely regarded as antioxidants, due in large part to their free radical scavenging activities and their ability to disrupt radical chain propagation. However, recent studies have demonstrated that the oxidation of some polyphenolic compounds, such as the tea-derived compound (-)-epigallocatechin-3-gallate (EGCG), results in the generation of reactive oxygen species that can potentially compromise the oxidative stability of food lipids under some conditions. In this present study, the rate of hydrogen peroxide (H(2)O(2)) generation and its stability, resulting from EGCG oxidation in Tween 80- and sodium caseinate-stabilized oil-in-water (O/W) emulsions in the presence of iron (25 μM Fe(3+) from FeCl(3)), were examined. Observed H(2)O(2) levels in protein-stabilized emulsions were significantly lower across all treatments as compared to surfactant-stabilized emulsions. The lower observed H(2)O(2) concentrations seen in the protein system are likely due to the antioxidant effects of the added proteins, which either prevented the generation of or more likely scavenged the peroxide. All protein-stabilized emulsions containing EGCG showed increases in carbonyl concentrations, a marker of protein oxidation, throughout the study. The H(2)O(2) scavenging activity of aqueous phase and interfacial caseinate and whey protein isolate (WPI) was also evaluated. Both proteins showed concentration-dependent scavenging of H(2)O(2) with caseinate displaying significantly higher scavenging abilities at all concentrations. These results suggest that food proteins may play an important role in mitigating the pro-oxidant effects of polyphenols.