Noncovalent interaction mechanism and functional properties of flavonoid glycoside-β-lactoglobulin complexes

), which indicated that glycosylation adversely affected the colloidal complex binding capacity. In this study, the physicochemical properties of the protein-flavonoid colloidal complex were determined. The analysis by circular dichroism spectroscopy demonstrated that flavonoid glycosides made the protein structure looser by inducing the secondary structure of β-LG to transform from the α-helix and β-sheet to random coils. The hydrophobicity of β-LG decreased due to binding with flavonoid glycosides, while functional properties including foaming, emulsification, and antioxidant capacities of β-LG were improved due to the noncovalent interactions. This study presents a part of the insight and guidance on the interactive mechanism of flavonoid glycosides and proteins and is helpful for developing functional protein-based foods.