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Interaction mechanism of okra (Abelmoschus esculentus L.) seed protein and flavonoids: Fluorescent and 3D-QSAR studies

文献类型： 外文期刊

作者： He, Chengyun 1 ; Bai, Lu 1 ; Liu, Daqun 2 ; Liu, Benguo 1 ;

作者机构： 1.Henan Inst Sci & Technol, Sch Food Sci, Xinxiang 453003, Peoples R China

2.Zhejiang Acad Agr Sci, Food Sci Inst, Hangzhou 310021, Peoples R China

关键词： Okra seed protein; Flavonoids; 3D-QSAR; Interaction; Fluorescence

期刊名称：FOOD CHEMISTRY-X （ 影响因子：6.1； 五年影响因子：6.4 ）

ISSN： 2590-1575

年卷期： 2023 年 20 卷

页码：

收录情况： SCI

摘要： The binding capacity of 10 flavonoids with okra seed protein (OSP) was studied by fluorescence spectroscopy. The structure of flavonoids had an obvious impact on binding performance. The binding ability of flavanone was lower than that of flavone, isoflavone and dihydrochalcone. The binding capacity of flavonoid glycoside was superior to that of the corresponding flavonoid aglycone. The binding ability was positively correlated with the number of phenolic hydroxyl groups on the B ring. The steric field and electrostatic field model constructed by 3D-QSAR method could well explain the above interaction behavior. Thermodynamic analysis suggested that the quenching mechanism of OSP caused by flavonoids was static quenching, and the binding-site number was 1. In addition, hydrogen bonding and van der Waals force dominated this interaction. The 3D and synchronous fluorescence spectra showed that there was no significant change in the polarity of the environment around tryptophan and tyrosine residues during binding.

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