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

文献类型： 外文期刊

第一作者： Lei, Dan

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

作者机构：

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

期刊名称：FOOD CHEMISTRY-X （ 影响因子：6.443； 五年影响因子：6.443 ）

ISSN： 2590-1575

年卷期： 2022 年 15 卷

页码：

收录情况： SCI

摘要： 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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