Mitigation of malondialdehyde-induced protein lipoxidation by epicatechin in whey protein isolate

Malondialdehyde (MDA) can induce lipoxidation in whey protein isolate (WPI). The physicochemical changes in this reaction with or without the presence of a phenolic compound epicatechin (EC) were characterized in this study. Results suggested the content of MDA was significantly reduced during co-incubation of MDA and EC. The addition of EC dose-dependently alleviated MDA-induced protein carbonylation, Schiff base formation and loss of tryptophan fluorescence. The interruption of MDA-binding to WPI was directly visualized by immunoblotting analysis. Observation of the surface microstructure of WPI showed that MDA-induced protein aggregation was partially restored by EC. Meanwhile, EC was found to promote loss of both protein sulfhydryls and surface hydrophobicity due to possible phenol-protein interactions. These observations suggested the potential of EC in the relief of MDA-mediated protein lipoxidation. •Decreased content of MDA was observed when incubated with EC•MDA-induced protein physiochemical changes were partially alleviated by EC•The interruption of MDA-binding to proteins was visualized by Western blot analysis•MDA-induced protein lipoxidation was inhibited by EC