文献类型： 外文期刊

第一作者： Yu, Yihong

作者： Yu, Yihong;Ding, Zhuhong;Ding, Xiaojuan

作者机构：

关键词： Rosa roxburghii Tratt; beta-Glucosidase; Quercetin glycoside; Binding mechanism

期刊名称：LWT-FOOD SCIENCE AND TECHNOLOGY （ 影响因子：6.056； 五年影响因子：6.295 ）

ISSN： 0023-6438

年卷期： 2022 年 165 卷

页码：

收录情况： SCI

摘要： Understanding the molecular mechanisms underlying protein-flavonoid interactions is crucial for the application of protein-flavonoid complexes in food. The purpose of this study was to explore the factors that influence the efficient release of rutin (Rut) and isoquercitrin (Iso) from Lactobacillus acidophilus beta-glucosidase (BGL) and the interaction mechanism among rutin, isoquercitrin and beta-glucosidase. Spectroscopic analysis, atomic force microscopy and molecular docking studies showed that Rut or Iso quenched the intrinsic fluorescence of beta-glucosidase in a static manner through the formation of a flavonoid-beta-glucosidase complex. Atomic force microscopy and circular dichroism measurements confirmed that the conformation of beta-glucosidase changed slightly. Molecular docking further proved that the interaction force of Rut or Iso with beta-glucosidase was hydrogen bonding, hydrophobic interactions and electrostatic interactions, and the binding free energies of the interactions were -180.54 kcal mol(-1) and -119.35 kcal mol(-1), respectively. Substituted groups on the glycosylation of quercetin glycoside compounds are crucial for their binding to beta-glucosidase. This study provides a theoretical basis for the design of natural flavonoid-protein complex functional foods.

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