香菇素与β-酪蛋白的相互作用研究

Study on the interaction between lentinin and β-casein

中文关键词:  香菇素  β-酪蛋白  光谱  相互作用  结构性质

英文关键词:lentinin  β-casein  spectrum  interaction  structural properties

中文摘要:

      目的 研究β-酪蛋白与风味物质香菇素相互作用的具体机制, 阐明相互作用对β-酪蛋白结构及微环境产生的影响。方法 构建香菇素-β-酪蛋白互作模型体系, 经荧光光谱法、紫外-可见分光光度法、圆二色光谱、等温滴定及气相色谱-质谱法、液相色谱-质谱法对香菇素与β-酪蛋白的相互作用进行检测分析。结果 气相色谱-质谱法检测结果表明, β-酪蛋白对香菇素起到显著缓释的作用, 光谱法检测结果及等温滴定结果表明, β-酪蛋白和香菇素的结合主要由疏水相互作用驱动, 热量变化焓值(ΔH)为7.25 kJ/mol, 熵值(ΔS)为113.20 J/(mol·K)。结论 香菇素与β-酪蛋白发生了疏水相互作用。在相互作用过程中, β-酪蛋白发生了静态荧光淬灭, 紫外光谱蓝移以及β-酪蛋白甲基化位点的改变证明了相互作用影响了β-酪蛋白的结构以及微环境极性。

英文摘要:

      Objective To investigate the interaction mechanism between β-casein and flavor substance lentinin, and elucidate the effect of the interaction on the structure and microenvironment of β-casein. Methods A model system of lentinin-β-casein interaction was established, the interaction between lentinin and β-casein was detected and analyzed by fluorescence spectrometry, ultraviolet and visible spectrophotometry, circular dichroism, isothermal titration and gas chromatography-mass spectrometry and liquid chromatography-mass spectrometry. Results The results of gas chromatography-mass spectrometry showed that β-casein played a significant role in slowing down the release of lentinin, the results of spectroscopy and isothermal titration showed that the binding of β-casein and lentinin was mainly driven by hydrophobic interactions, the enthalpy value (ΔH) was 7.25 kJ/mol and the entropy value (ΔS) was 113.20 J/(mol·K). Conclusion Lentinin interacts with β-casein in a hydrophobic manner. During the interaction, static fluorescence quenching of β-casein, blue shift of ultraviolet spectrum and change of β-casein methylation site demonstrate that the interaction have affected the structure and microenvironmental polarity of β-casein.