Modulation mechanism of dextran-mediated glycation on soy protein isolate-quercetin interaction: a spectroscopic and...

This study systematically investigated the interaction mechanisms between glycated soybean protein isolate (GSPI) formed from soy protein isolate (SPI) and dextran (DEX) via Maillard reaction, and quercetin (Que), employing multi-spectroscopic analysis and molecular docking simulation. The results indicated that hydrogen bonding and van der Waals forces dominated the non-covalent binding between GSPI and Que, with the Maillard reaction further enhancing hydrogen bonding interaction. This enhancement was substantiated through molecular docking simulations, which revealed short hydrogen bonds (< 3.0 Å) within GSPI-Que complex. After 4 h of Maillard reaction, GSPI-Que complex exhibited a 3.5 % increase in ordered secondary structures (α-helix and β-sheet), concomitant with significantly enhanced antioxidant capacity: DPPH radical scavenging, ABTS radical scavenging, and reducing power increased by 26.29 %, 12.60 %, and 14.06 %, respectively. These findings provide theoretical reference for designing emulsions utilizing Maillard reaction-glycated proteins in the food industry.