Complexation of soybean protein isolate with β-glucan and myricetin: Different affinity on 7S and 11S globulin by QCM-D and molecular simulation analysis (2025)

化学杨梅素石英晶体微天平圆二色性葡聚糖色谱法大豆蛋白生物化学有机化学类黄酮吸附山奈酚抗氧化剂

作者

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

出处

期刊：Food Chemistry: X [Elsevier]
日期：2022-08-10 卷期号：15: 100426-100426 被引量：21

链接

doi.org doaj.org nih.gov nih.govdoi.org

标识

DOI：10.1016/j.fochx.2022.100426

摘要

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 1.17×106 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.

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Complexation of soybean protein isolate with β-glucan and myricetin: Different affinity on 7S and 11S globulin by QCM-D and molecular simulation analysis (2025)

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