Different interactions driving the binding of soy proteins (7S/11S) and flavonoids (quercetin/rutin): Alterations in the conformational and functional properties of soy proteins

The purpose of this research was to comparatively investigate the interactions between bioactive flavonoids (quercetin and rutin) and two predominant soy proteins (β-conglycinin and glycinin), and the structural and functional properties of their complexes. The binding affinities of quercetin/rutin toward 7S/11S were structure-dependent, in that rutin had a higher binding affinity than that of quercetin, and 11S exhibited higher affinity toward quercetin/rutin than that of 7S. The interactions in the 7S/11S-quercetin complexes were driven by van der Waals forces and hydrogen-bonding interactions, whereas the 7S/11S-rutin complexes exhibited hydrophobic interactions. Binding to quercetin or rutin altered the secondary structures (decrease in the α-helix and random coil contents and increase in the β-sheet content), decreased the surface hydrophobicity and thermal stability, and enhanced the antioxidant capacity of 7S and 11S. These findings provide valuable information that can facilitate the design of custom-tailored protein-flavonoid macromolecules.