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投稿时间:2025-05-16
投稿时间:2025-05-16
中文摘要: 为探究原花青素与组合蛋白的相互作用及对蛋白稳定性的影响,该文采用4种不同聚合度的原花青素为原料,采用浊度、荧光光谱、等温滴定量热等手段表征燕麦-豌豆组合蛋白和不同聚合度原花青素的复合物形成及其相互作用机制。结果表明,4种不同聚合度的原花青素均能和燕麦-豌豆组合蛋白以非共价相互作用自发进行结合,其中燕麦-豌豆组合蛋白和原花青素单体、高聚体的结合过程都以疏水相互作用为主导,而燕麦-豌豆组合蛋白和原花青素低聚体的结合均主要为氢键和范德华力。扫描电子显微镜结果显示,原花青素可以破坏燕麦-豌豆组合蛋白的网络孔状结构,使得蛋白质的骨架和二级结构发生改变,从而提升复合物在温度、盐离子、pH值、乳化性和抗氧化性方面的稳定性。
Abstract:In order to explore the interaction between proanthocyanidins and combined proteins and their influence on protein stability,this paper used four kinds of proanthocyanins with different polymerization degrees as raw materials and employed turbidity,fluorescence spectroscopy,isothermal titration calorimetry,and other means to characterize the complex formation and interaction mechanism of oat-pea combined proteins and proanthocyanins with different polymerization degrees.The results showed that four kinds of procyanidins with different polymerization degrees could bind to oat-pea combined protein spontaneously by non-covalent interaction.Among them,the binding process of oat-pea combined protein with proanthocyanin monomers and high polymer were dominated by hydrophobic interactions,while the binding of oat-pea combined protein and proanthocyanin oligomers was mainly hydrogen bonds and van der Waals forces.Scanning electron microscopy showed that procyanidins destroyed the network pore structure of oat-pea combined protein,which changed the skeleton and secondary structure of protein and improved the stability of the complex in terms of temperature,salt ions,pH value,emulsification,and oxidation resistance.
文章编号:202603001 中图分类号: 文献标志码:
基金项目:国家自然科学基金青年科学基金项目(32101948)
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