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- Title
香菇素与 β-酪蛋白的相互作用研究.
- Authors
罗晓林; 徐献兵
- Abstract
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/(molꞏK). 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.
- Publication
Journal of Food Safety & Quality, 2022, Vol 13, Issue 15, p4802
- ISSN
2095-0381
- Publication type
Article