%0 Journal Article
%T Evaluating the binding mechanism, structural changes and stability of ternary complexes formed by the interaction of folic acid with whey protein concentrate-80 and L-ascorbyl 6-palmitate.
%A Wang X
%A Wang Z
%A Zhang K
%A Szeto IM
%A Yan Y
%A Liu B
%A Zhang J
%A Evivie SE
%A Li B
%A Duan S
%J Food Chem
%V 457
%N 0
%D 2024 Nov 1
%M 38917563
%F 9.231
%R 10.1016/j.foodchem.2024.139924
%X In the present study, we investigated the mechanisms associated with the stabilizing effects of whey protein concentrate-80 (WPC80) and L-ascorbyl 6-palmitate (LAP) on folic acid (FA). Multispectral techniques show that WPC80 binds to FA and LAP mainly through hydrophobic interactions, and that energy is transferred from WPC80 to FA and LAP in a nonradiative form (FA/LAP); The combination of FA/LAP resulted in a change in the conformation and secondary structure content of WPC80, an increase in the absolute zeta potential of the system, and a shift in the particle size distribution towards smaller sizes. The compound system exhibits strengthened antioxidant properties and favorable binding properties. Besides, WPC80 improves the storage stability of FA under different conditions. These results demonstrated that the ternary complex formed by FA co-binding with WPC80 and LAP is an effective way to improve the stability against of FA.