食品科学 ›› 0, Vol. ›› Issue (): 0-0.

• 食品化学 •    下一篇

大豆蛋白-黄芩素的结合机制及蛋白构象和功能的变化

闫馨月1,贾亦佳1,孙诗艳1,张东蒙1,耿梦洁1,杨晋杰2,Stanislav Sukhikh3,Olga Babich4,李杨5,齐宝坤5   

  1. 1. 东北农业大学
    2. 渤海大学
    3. 康德波罗的海联邦大学
    4. 康德波罗的海大学
    5. 东北农业大学食品学院
  • 收稿日期:2022-05-20 修回日期:2022-12-19 出版日期:2023-02-25 发布日期:2023-02-25
  • 通讯作者: 李杨 E-mail:yangli@neau.edu.cn
  • 基金资助:
    大豆产业技术体系岗位科学家项目

Exploring the Binding Mechanism of Soybean Protein-Baicalein Including Changes in Protein Conformation and Function

Xin-Yue YAN 2, 2, 2, 2,Jinjie Yang 2,Babich Olga3,li yang 2   

  • Received:2022-05-20 Revised:2022-12-19 Online:2023-02-25 Published:2023-02-25
  • Contact: li yang E-mail:yangli@neau.edu.cn
  • Supported by:
    the Post System Scientist of Ministry of Agriculture

摘要: 探索大豆蛋白组分中β-伴大豆蛋白(7S)/大豆蛋白(11S)与黄芩素的结合机制,考察复合物构象及功能特性的变化。傅里叶变换红外光谱表明黄芩素诱导蛋白的β-折叠转化为α-螺旋和无规卷曲。内源荧光光谱证实了黄芩素的加入使7S、11S结构变得更紧密。黄芩素与蛋白的反应自发进行,并通过静态方式淬灭蛋白荧光。7S、11S蛋白分别通过氢键和疏水相互作用与黄芩素结合。分子对接结果表明,黄芩素对11S的亲和力高于7S。扫描电子显微镜显示了7S、11S与复合物的微观结构差异。此外,与黄芩素结合后,7S、11S的表面疏水性下降,热稳定性及其他功能特性提升。

关键词: β-伴大豆蛋白(7S), 大豆蛋白(11S), 黄芩素, 结合机制, 构象变化, 功能特性

Abstract: To explore the binding mechanism of β-conglycinin (7S)/glycinin (11S) in soybean protein components with baicalein, and to investigate the changes of the conformation and functional properties of the complex. Fourier transform infrared spectroscopy indicated that baicalein induced the transformation of β-sheets into α-helices and random coils. Intrinsic fluorescence spectra confirmed that the addition of baicalein made the 7S、11S structure tighter. The reaction of baicalein with the protein proceeded spontaneously and quenched the protein fluorescence in a static manner. The 7S、11S proteins bound to baicalein by hydrogen bonds and hydrophobic interactions, respectively. The affinity of baicalein to 11S was higher than that of 7S by molecular docking. Scanning electron microscopy showed the microstructure difference between 7S、11S and complex. In addition, the surface hydrophobicity of 7S、11S decreased and the thermal stability and other functional properties of complex were improved after combining with baicalein.

Key words: β-conglycinin (7S), glycinin (11S), baicalein, binding mechanism, conformational change, functional properties

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