Non-covalent interactions between electroactivated soybean protein isolate and naringin: Structure, functionality and molecular docking.
To broaden the utilization of soybean protein isolate (SPI), electroactivation-treated SPI (EAP) was combined with naringin (NAR) to form protein-polyphenol complexes (EAP-N), and their structural and functional properties were investigated. EA treatment induced SPI unfolding, reduced particle size, and increased absolute zeta potential. After NAR addition, relatively stable EAP-N complexes were formed. At 0.6 mg/mL NAR, the complex showed the highest solubility (77.01%). Compared with SPI, EAP-N complexes also exhibited enhanced antioxidant activity and improved interfacial properties. Molecular forces and Molecular docking revealed that the modified EAP increased the binding sites with NAR, and the interactions between them were manly non-covalent (hydrogen bonds/hydrophobic interactions). These findings indicate that EAP-N complexes have potential as functional protein-polyphenol ingredients for emulsion and foam-based food systems.