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

    Journal: Food Chem. X, Volume 15, OCT 30

    Authors: Lei, Dan; Li, Junsheng; Zhang, Chao; Li, Shuyi; Zhu, Zhenzhou; Wang, Feifei; Deng, Qianchun; Grimi, Nabil

    Organizations: National youth talent program in food industry of China and Outstanding young and middle-aged science and technology innovation team in Hubei Province [T2020012]

    Keywords: Soybean protein isolate; ?-Glucan; Myricetin; Ternary complex; Interaction mechanism

    The complexation of soybean protein isolate (SPI) with beta-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 beta-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 1.17x106 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 beta-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.
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