摘要
探究黄豆黄素(Glycitein,Gly)和大豆球蛋白(Glycinin,11S)的相互作用机制及其对蛋白结构的影响。以黄豆黄素与大豆球蛋白为研究对象,采用荧光猝灭光谱、同步荧光光谱和分子对接技术研究Gly与11S之间的结合特性和作用机制,并利用紫外-可见光谱与圆二色光谱对Gly与11S蛋白结合后复合物的结构进行表征。结果表明,Gly与11S蛋白之间的猝灭机制为静态猝灭,两者结合位点数为1,主要通过氢键和范德华力形成复合物,使得Gly稳定地结合于11S表面的疏水性空腔中。进一步研究表明,与Gly作用后,11S蛋白的二、三结构发生显著变化,蛋白表面疏水性降低,促使肽链更加伸展,结构更加松散。本研究有助于我们在分子水平上理解黄豆黄素与大豆球蛋白之间的相互作用机制,对于未来在食品工业中有效利用这两种成分具有重要的指导意义。
In this study,the interaction mechanism of glycitein(Gly)and glycinin(11S)and its effect on the structure of the protein were investigated.The interaction mechanism between glycitein and glycinin was investigated by fluorescence quenching spectroscopy,synchronous fluorescence spectroscopy,and molecular docking,and the structures of the complexes were characterized by UV-visible and circular dichroism spectroscopy.The results showed that the mechanism of quenching between Gly and 11S protein was static quenching,and the binding site number was 1.The complex formed mainly through hydrogen bonding and van der Waals forces,which made Gly stably bound to the hydrophobic cavity on the surface of 11S.Further studies showed that the secondary and tertiary structures of 11S protein were significantly changed after interaction with Gly,and the hydrophobicity of the protein surface was reduced,which led to the stretching of the protein peptide chain and a more loosely packed structure.The present study helps us to understand the interaction mechanism between Gly and 11S at the molecular level,and has important guiding significance for the effective utilization of these two components in the food industry in the future.
作者
邓雯
杨安树
陈红兵
DENG Wen;YANG Anshu;CHEN Hongbing(State Key Laboratory of Food Science and Resources Nanchang University,Nanchang 330047,China;Sino-German Joint Research Institute,Nanchang University,Nanchang 330047,China)
出处
《南昌大学学报(理科版)》
2025年第4期373-379,共7页
Journal of Nanchang University(Natural Science)
基金
国家自然科学基金资助项目(31972186,32260595)
江西省主要学科学术和技术带头人培养计划-领军人才项目(20225BCJ22022)。
