黑木耳多糖与乳清分离蛋白分子间作用力的研究

Study on intermolecular forces between Auricularia auricular polysaccharide and whey protein isolate

中文关键词:  黑木耳多糖  乳清分离蛋白  分子间作用力  分子对接

英文关键词:Auricularia auricular polysaccharide  whey protein isolate  intermolecular forces  molecular docking

中文摘要:

      目的 研究黑木耳多糖与乳清分离蛋白分子间的作用力。方法 本研究利用化学键解离剂处理黑木耳多糖-乳清分离蛋白复合物, 通过可见光吸收光谱、傅里叶红外光谱、荧光光谱技术检测其浊度及二级、三级结构变化, 分析维系该复合物的主要作用力, 并利用离子交换色谱进行单糖组成成分分析, 结合分子对接技术预测其结合位点。结果 浊度结果表明, 氢键和疏水相互作用是维持复合物稳定的主要作用力; 红外光谱、荧光光谱检测发现, 尿素、十二烷基硫酸钠的添加改变了复合物的二级和三级结构, 再次证明复合物间的主要作用力为氢键和疏水相互作用; 黑木耳多糖的单糖成分主要为甘露糖; 分子对接结果显示, 甘露糖主要通过氢键与乳清分离蛋白的组氨酸、谷氨酸、天冬氨酸、色氨酸等氨基酸残基结合。结论 本研究揭示了黑木耳多糖通过氢键及疏水相互作用与乳清分离蛋白结合, 并预测结合位点在组氨酸、谷氨酸、天冬氨酸、色氨酸等氨基酸残基处, 研究结果为黑木耳多糖-乳清分离蛋白复合物在酸性环境中的应用提供了理论基础。

英文摘要:

      Objective To study the intermolecular forces between Auricularia auricular polysaccharide and whey protein isolate. Methods In this study, urea and sodium dodecyl sulfate were used to treat Auricularia auricular polysaccharide-whey protein isolate, and the turbidity and structural changes of the complex were detected to study the intermolecular force between Auricularia auricular polysaccharide and whey protein isolate by visible light absorption spectroscopy and FTIR spectrum, fluorescence spectrum. The monosaccharide composition of Auricularia auricularia polysaccharide was analyzed by ion chromatography, and the binding site was predicted by molecular docking technology. Results The turbidity results showed that hydrogen bond and hydrophobic interaction were the main forces to maintain the stability of the complex. The results of FTIR spectrum and fluorescence spectrum showed that the addition of urea and sodium dodecyl sulfate changed the secondary and tertiary structures of the complex, which again proved that the main force between the complexes was hydrogen bond and hydrophobic interaction. The main monosaccharide component of Auricularia auricularia polysaccharide was mannose. The molecular docking results predicted that mannose mainly binds to amino acid residues such as His, Glu, Asp and Trp of whey protein isolate through hydrogen bonds. Conclusion This study revealed that Auricularia auricularia polysaccharide binds to whey protein isolate through hydrogen bond and hydrophobic interaction, and predicted that the binding site may be at the amino acid residues such as His, Glu, Asp, Trp, etc., which provides a theoretical basis for the subsequent application of the complex in acidic environment.