Complexation of soybean protein isolate with β-glucan and myricetin: Different affinity on 7S and 11S globulin by QCM-D and molecular simulation analysis.

The complexation of soybean protein isolate (SPI) with β-glucan (DG) and myricetin (MC) was focused in this study. UV-Vis, circular dichroism and 3D fluorescence analysis jointly proved that interaction with DG and MC altered the structures of SPI, whose β-sheet decreased to 29 % and random coil increased to 35 %, respectively. Moreover, the microenvironment of tryptophan and tyrosine from protein were changed. The ternary complex performed a different molecular weight distribution, showing a larger molecular weight of 1.17×10 g/mol compared with SPI verified by gel permeation chromatography (GPC). And it was further evidenced by Quartz Crystal Microbalance with Dissipation (QCM-D) and molecular docking that glycinin (11S) possessed a better affinity toward DG and MC compared with β-conglycinin (7S), which indicated stronger binding ability through hydrogen bonds. The successful preparation of SPI-DG-MC complex will advance the application of soybean resource as a functional food ingredient.