Interaction of soybean protein isolate with hawthorn flavone complex

In view of the possible synergistic effects of the combination of polyphenols and proteins, the present study investigated the mode of interaction between hawthorn flavonoids (HF) and soybean isolated protein (SPI). The FTIR analysis demonstrated that the amino group of the amide in SPI interacted with the hydroxyl group in HF, forming hydrogen bonds. SEM showed that HF changed the microstructure and surface morphology of SPI.XRD diffraction showed that part of the crystal structure of SPI changed to the amorphous structure. Furthermore, molecular docking and molecular dynamics simulations indicate that the binding energy of HF and SPI 7S is predominantly van der Waals energy(−37.66 kcal/mol), and Electrostatic energy is −0.74 kcal/mol. The primary factor governing the binding energy between HF and SPI 11S is the van der Waals energy(−45.11 kcal/mol), The electrostatic energy is −25.6 kcal/mol. Briefly, the binding between HF and SPI in this study is non-covalent.