Investigation on the interaction mechanisms for stability of preheated whey protein isolate with anthocyanins from...

Proteins and anthocyanins coexist in complex food systems. This research mainly studied the steady-state protective design and mechanism of the preheated protein against anthocyanins. Multispectral and molecular dynamics are utilized to illustrate the interaction mechanism between preheated whey protein isolate (pre-WPI) and anthocyanins. The pre-WPI could effectively protect the stability of anthocyanins, and the effect was better than that of the natural whey protein isolate (NW). Among them, NW after preheating treatment at 55 °C showed better protection against anthocyanin stability. Fluorescence studies indicated that pre-WPI there existed a solid binding affinity and static quenching for malvidin-3-galactoside (M3G). Multispectral data showed a significant variation in the secondary structure of pre-WPI. Furthermore, molecular dynamics simulation selects AMBER18 as the protein force field, and the results showed that hydrogen bonding participated as an applied force. Compared with NW, pre-WPI could better wrap anthocyanins and avoid damage to the external environment due to tightening of the pockets. Protein protects anthocyanins from degradation, and this protective effect is influenced by the preheating temperature of protein and the structure of protein. On the basis of the above results, it is possible to pinpoint the interaction mechanism between preheated proteins and anthocyanins.