Noncovalent interaction mechanism and functional properties of flavonoid glycoside-β-lactoglobulin complexes
Min Fu, Lizhi Gao, Qin Geng, Ti Li, Taotao Dai, Chengmei Liu, Jun Chen
Abstract
), 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.