Mechanism of interactions between soyasaponins and soybean 7S/11S proteins.

In this study, the proteins glycinin (11S) and β-conglycinin (7S) were mixed with soyasaponin (Ssa) Ab/Bb to form a composite system. We used fluorescence and synchronous fluorescence spectra to demonstrate the changes in the surrounding environment and the structure of the proteins. Dynamic interface behavior analysis showed the possible interface behavior induced by the composite system. The interactions between Ssa and the proteins, along with the mode of action, were analyzed by molecular docking. The interactions between Ssa and soy protein increased with the change in concentration. The interactions between the two proteins were mediated by tryptophan (Trp) and primarily involved hydrogen bonds, which changed the microenvironment and loosened the protein structure. These results helped in understanding the mechanism underlying the interactions between Ssa Ab/Bb and 7S/11S. Furthermore, these results highlighted the theoretical fundamentals for the future applications of composite systems as surfactants in the food industry.