研究报告

矢车菊素-3-O-葡萄糖苷与牛血清白蛋白相互作用及对蛋白性质的影响

  • 张会敏 ,
  • 刘国宸 ,
  • 任李宁 ,
  • 宁宁 ,
  • 琚萌萌 ,
  • 孙爱东
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  • (北京林业大学 生物科学与技术学院, 北京, 100091)
第一作者:博士研究生(孙爱东教授为通信作者,E-mail:adsun@bjfu.edu.cn)

收稿日期: 2024-06-11

  修回日期: 2024-08-12

  网络出版日期: 2025-06-19

基金资助

国家自然科学基金项目(32172222,32372370);国家重点研发计划项目(2023YFD2201804)

Interaction of cyanidin-3-O-glucoside with bovine serum albumin and its effect on protein properties

  • ZHANG Huimin ,
  • LIU Guochen ,
  • REN Lining ,
  • NING Ning ,
  • JU Mengmeng ,
  • SUN Aidong
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  • (School of Biological Science and Technology, Beijing Forestry University, Beijing 100091, China)

Received date: 2024-06-11

  Revised date: 2024-08-12

  Online published: 2025-06-19

摘要

蛋白质以可逆或不可逆的方式与多酚相互作用,从而影响食品的感官、质地和营养特性。为探究以矢车菊素-3-O-葡萄糖苷(centaurin-3-O-glucoside,C3G)为代表的花色苷类多酚与牛血清白蛋白(bovine serum albumin,BSA)的非共价作用方式及其对蛋白特性的影响,该研究采用多光谱技术和分子对接手段探究二者的相互作用,并探讨了C3G对BSA蛋白质特性的影响。傅里叶红外光谱显示,C3G与BSA结合后,酰胺I带和A带发生红移且峰强度减弱。圆二色光谱结果表明,C3G使BSA蛋白结构变得松散,BSA二级结构发生改变,α-螺旋含量由31.8%下降到31.1%,β-折叠含量由18.1%增加到18.5%。荧光光谱证实了C3G对BSA的猝灭是形成基态络合物引起的静态猝灭。热力学和分子对接结果显示,BSA和C3G之间的作用力以静电引力和氢键作用为主,C3G可进入BSA内腔结构。对BSA物理特性研究发现,C3G的加入可使BSA结构域扩展,粒径从244.75 nm增加至644.70 nm。同时C3G显著增强了BSA的溶解性、持水性和持油性,并改善了其泡沫性能和乳化性能。该研究为了解C3G对BSA构象和蛋白特性的影响提供了重要的实验和理论基础,为蛋白花色苷复合物的应用提供了理论依据和参考。

本文引用格式

张会敏 , 刘国宸 , 任李宁 , 宁宁 , 琚萌萌 , 孙爱东 . 矢车菊素-3-O-葡萄糖苷与牛血清白蛋白相互作用及对蛋白性质的影响[J]. 食品与发酵工业, 2025 , 51(11) : 199 -207 . DOI: 10.13995/j.cnki.11-1802/ts.040159

Abstract

Proteins and polyphenols can interact in reversible or irreversible ways, thus affect the sensory, texture and nutritional properties of foods.To investigate the types of non-covalent interactions between anthocyanins (centaurin-3-O-glucoside (C3G)) and bovine serum albumin (BSA) and their effects on BSA protein properties, multispectral techniques and molecular docking methods were used.The effects of C3G on the properties of BSA protein were also studied.First, Fourier infrared spectroscopy showed that the amide I and A bands were redshifted and their peak intensities weakened after C3G combined with BSA.The results of circular dichroism spectrum showed that the structure of BSA protein became loose and the secondary structure of BSA was changed in the presence of C3G.The α-helix content decreased from 31.8% to 31.1%, and the β-fold content increased from 18.1% to 18.5%.Next, the fluorescence spectra confirmed that the quenching of BSA by C3G is a static quenching caused by the formation of ground state complex.Thermodynamic and molecular docking results showed that the force between BSA and C3G is mainly contributed by electrostatic attraction and hydrogen bond, and C3G entered the BSA cavity structure.Finally, the study on the physical properties of BSA showed that the addition of C3G could expand the BSA domain and increase the particle size from 244.75 nm to 644.70 nm.Interestingly, C3G significantly enhanced the solubility, water holding capacity and oil holding capacity of BSA, as well as improved foam properties and emulsification properties.This study provides an important experimental and theoretical basis for understanding the effects of C3G on the conformation and protein properties of BSA, and provides a theoretical basis and reference for the application of protein-anthocyanin complexes.

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