Study on the mechanism of non-covalent interaction between rose anthocyanin extracts and whey protein isolate under different pH conditions.

The non-covalent interaction between anthocyanin and dietary protein had an impact on their physicochemical property. The purpose of this study was to study the non-covalent interaction mechanism between rose anthocyanin extract (RAEs) and whey protein isolate (WPI), and further compare the interaction mechanism with pure anthocyanin (PC) and WPI. At pH 3.0 and pH 7.0, RAEs and WPI had non-covalent interactions in the two systems with two types of unequal and mutually influencing binding sites, and the interaction forces were both hydrogen bonds and van der Waals forces. Interestingly, PC and WPI also had non-covalent interactions in both systems, the number of which binding sites was about one type, and the forces were hydrogen bonds and van der Waals forces. In addition, a variety of spectral combination techniques indicated that RAEs and PC caused similar changes in the secondary structure of WPI.