Complexation of soybean protein isolate with β-glucan and myricetin: Different affinity on 7S and 11S globulin by QCM-D and molecular simulation analysis
Dan Lei, Junsheng Li, Chao Zhang, Shuyi Li, Zhenzhou Zhu, Feifei Wang +2 more
Food Chemistry X
Abstract
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<sup>6</sup> 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.
Extracted Claims
3 claims extracted from this paper into the knowledge graph
glycinin (11S) possesses better affinity toward DG and MC
“glycinin (11S) possessed a better affinity toward DG and MC compared with β-conglycinin (7S), which indicated stronger binding ability through hydrogen bonds.”
interaction with DG and MC alters structures of SPI
“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 %,...”
soybean protein isolate (SPI) interacts with β-glucan (DG) and myricetin (MC)
“The complexation of soybean protein isolate (SPI) with β-glucan (DG) and myricetin (MC) was focused in this study.”