Comparative analysis of non-covalent complexation between isomeric polyphenols and soy protein isolate: Focus on interaction mechanisms, interfacial behavior, and emulsion stability
Abstract
This study aimed to investigate the differences in interaction mechanisms between soy protein isolate (SPI) and isomeric polyphenols (quercetin, Que/morin, Mor) at varying concentrations (0-1.6 mM). It also examined the oil/water (O/W) interfacial properties and emulsion stability of the complexes (SQ/SM). Polyphenol binding equivalents (PBE) and SDS-PAGE results showed that SPI formed non-covalent complexes with Que/Mor, with PBE peaking at 0.8 mM (3.08 and 2.72 mmol/mg protein). Multispectral analysis including fourier transform infrared spectra, two-dimensional correlation spectra, ultraviolet and fluorescence spectra revealed that polyphenols bound to SPI through hydrogen bonds and hydrophobic interactions. These induced unfolding of the secondary structure (conversion of β-sheet to disordered structures) and tertiary conformational changes in the protein. Meanwhile, the particle size increased after Que/Mor complexed with SPI, and electrostatic repulsion weakened. The combined molecular docking found that Que exhibited stronger binding affinity to SPI than Mor (7S-Que/Mor, -8.5/-8.1 kcal/mol). The hydrogen bond played a crucial role in the formation of SQ. Furthermore, polyphenol-modified SPI showed a more balanced hydrophilic/hydrophobic (contact angle approaching 90°), reduced interfacial tension, and accelerated interfacial protein adsorption. The complexes stabilize the emulsion system through a networked "bridging" structure. The appropriate amount of Que/Mor…
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