Different interactions driving the binding of soy proteins (7S/11S) and flavonoids (quercetin/rutin): Alterations in the conformational and functional properties of soy proteins. (1st December 2022)

• Record Type: Journal Article
• Authors: Jia, Yijia; Yan, Xinyue; Huang, Yuyang; Zhu, Huaping; Qi, Baokun; Li, Yang
• Is Part Of: Food chemistry. Volume 396(2022)
• Publication Date: 2022-12-01
• Subjects: Rutin (PubChem CID: 5280805) -- Quercetin (PubChem CID: 5280459); Binding interaction -- Soybean -- Fluorescence spectroscopy -- Flavonoid -- In-silico docking; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2022.133685
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Quercetin/rutin quenched 7S/11S statically and 11S showed higher affinity. Rutin showed higher binding affinity to 7S/11S via hydrophobic interactions. Quercetin bonded to 7S/11S via van der Waals and hydrogen bonding interactions. Quercetin/rutin altered secondary structures and surface hydrophobicity of 7S/11S. The flavonoids affected the thermal stability and antioxidant capacity of 7S/11S. 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.