不同蔗糖浓度下β-乳球蛋白与花青素结合的分子动力学模拟

doi:10.12441/spyswjs.20240520002

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不同蔗糖浓度下β-乳球蛋白与花青素结合的分子动力学模拟
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                        10.12441/spyswjs.20240520002
                    
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作者单位:1.荆楚理工学院食品与生物学院，湖北 荆门 448000;2.荆楚理工学院特色食品功能挖掘与综合利用团队，湖北 荆门 448000;3.湖北钟祥聚瑞食品有限公司，湖北 荆门 431900
作者简介:
通讯作者:黄业传（1975—），男，博士，教授，硕士研究生导师，主要从事现代食品加工研究。E-mail: huangyc@jcut.edu.cn
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基金项目:湖北省科技计划项目（2022BEC031）。

Molecular Dynamics Simulation of the Binding Between β-Lactoglobulin and Anthocyanins Under Different Sucrose Concentrations

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1.College of Food and Biology, Jingchu University of Technology, Jingmen 448000, China;2.Functional Exploration and Comprehensive Utilization Team for Specialty Foods, Jingchu University of Technology, Jingmen 448000, China;3.Hubei Zhongxiang Jurui Food Co., Ltd., Jingmen 431900, China

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【目的】探究含乳植物饮料中蔗糖的添加对乳蛋白结构与性质、蛋白质与植物中小分子物质结合的影响。【方法】以β-乳球蛋白和花青素为研究对象，采用分子动力学模拟不同蔗糖浓度（0、0.25、0.50、0.75、1.00 mol/L）下两者的结合规律与蛋白质结构变化。【结果】花青素主要结合在β-乳球蛋白的疏水腔。以最优结合构象为起始结构，用GROMACS软件进行150 ns的分子动力学模拟，结果表明，蔗糖环境中β-乳球蛋白的结构更加稳定，氨基酸残基波动也更小；蛋白质的α螺旋数量增加，使蛋白质之间的氢键数量显著增加，同时伴随β折叠数量的减少。与对照组相比，β-乳球蛋白与花青素之间的结合自由能在0.25、0.50 mol/L蔗糖溶液中的变化较小，但在0.75 mol/L蔗糖溶液中显著增加，在1.00 mol/L蔗糖溶液中显著降低，该结合自由能的差异主要是由范德华力和氢键的变化引起的。【结论】蔗糖浓度的变化会造成花青素在 β-乳球蛋白表面的结合位置和结合机理产生差异。

Abstract:

[Objective] This study aims to investigate the effects of adding sucrose to plant-based beverages containing milk on the structure and properties of milk proteins, as well as the binding of proteins to small molecules in plants. [Method]Molecular dynamics simulation was conducted for the binding patterns between β-lactoglobulin and anthocyanins and the protein structure changes under different sucrose concentrations (0, 0.25, 0.50, 0.75, and 1.00 mol/L). [Result] Anthocyanins mainly bound to the hydrophobic cavity of β-lactoglobulin. With the optimal binding conformation as the starting structure, GROMACS was used for the molecular dynamics simulation at 150 ns. The results showed that the structure of β-lactoglobulin in the sucrose solution was more stable, with milder fluctuations of amino acid residues. The increase in the number of α helixes significantly increased the hydrogen bonds between proteins, which was accompanied by the decrease in the number of β folds. The binding free energy between β-lactoglobulin and anthocyanins did not change much in 0.25 and 0.50 mol/L sucrose environments, but significantly increased in the 0.75 mol/L sucrose solution and significantly decreased in the 1.00 mol/L sucrose solution compared with the control group. The differences in binding free energy were mainly caused by changes in van der Waals forces and hydrogen bonding. [Conclusion] The changes in sucrose concentration would cause the differences of the binding position and binding mechanisms of anthocyanins on the β-lactoglobulin surface.

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张喜才,胡霄,黄业传,李蓉,阮军,李硕芳.不同蔗糖浓度下β-乳球蛋白与花青素结合的分子动力学模拟[J].食品与生物技术学报,2025,(3):93-101.

ZHANG Xicai, HU Xiao, HUANG Yechuan, LI Rong, RUAN Jun, LI Shuofang. Molecular Dynamics Simulation of the Binding Between β-Lactoglobulin and Anthocyanins Under Different Sucrose Concentrations[J]. Journal of Food Science and Biotechnology,2025,(3):93-101.

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收稿日期:2024-05-20
最后修改日期:2024-06-24
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在线发布日期: 2025-07-15
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