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  • Title: Different interactions driving the binding of soy proteins (7S/11S) and flavonoids (quercetin/rutin): Alterations in the conformational and functional properties of soy proteins.
    Author: Jia Y, Yan X, Huang Y, Zhu H, Qi B, Li Y.
    Journal: Food Chem; 2022 Dec 01; 396():133685. PubMed ID: 35843004.
    Abstract:
    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.
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