Fabrication of (-)-epigallocatechin-3-gallate carrier based on glycosylated whey protein isolate obtained by ultrasound Maillard reaction.

This study investigated the effect of glycation on the binding of whey protein isolate (WPI) with (-)-epigallocatechin-3-gallate (EGCG), and the physicochemical stability and bioaccessibility of the formed complex. The WPI-gum Acacia (GA) conjugate was prepared by ultrasound-assisted Maillard reaction. Results indicated that conjugated WPI showed stronger binding and entrapping ability to EGCG than that of WPI. The protein aggregation induced by EGCG was partly inhibited by glycosylation, presumably due to the steric hindrance of polysaccharide chains. The greatest protection of EGCG and its antioxidant activity were also obtained by complexing it with WPI-GA conjugate. The in vitro bioaccessibility analysis demonstrated that the bioaccessibility of EGCG cloud be significantly (p < 0.05) enhanced by complexing it with WPI, especially WPI-GA conjugate. These findings are important to design promising and effective EGCG carriers for its wide application in food industry.