Key Laboratory of Food Nutrition and Safety of SDNU, Provincial Key Laboratory of Animal Resistant Biology, College of Life Science, Shandong Normal University, Jinan 250014, PR China.
Key Laboratory of Food Nutrition and Safety of SDNU, Provincial Key Laboratory of Animal Resistant Biology, College of Life Science, Shandong Normal University, Jinan 250014, PR China.
Int J Biol Macromol. 2019 Sep 1;136:804-812. doi: 10.1016/j.ijbiomac.2019.06.053. Epub 2019 Jun 20.
To investigate the interaction mechanism between bovine protein β-lactoglobulin (β-LG) and theaflavin (TA), chlorogenic acid (CA) and delphinidin-3-O-glucoside (D3G), multi-spectrometry analytical methods and molecular modeling were applied. Fluorescence experiments proved that polyphenols strongly quenched the intrinsic fluorescence of β-LG mainly through static quenching and the main interaction force was hydrophobic interaction. Moreover, Fourier transform infrared (FTIR) and circular dichroism (CD) indicated that polyphenols changed β-LG secondary and tertiary structure. Enzyme-linked immunosorbent assay and molecular modeling study manifested that complex of β-LG with polyphenols could significantly reduce the IgE-binding capacity of β-LG due to the polyphenol binding site directly obscures the IgE linear epitopes. In conclusion, polyphenols had impact on the structure and potential functionality of β-LG, which would be valuable in dairy processing industry and food nutrition security.
为了研究牛血清白蛋白（β-LG）与茶黄素（TA）、绿原酸（CA）和矢车菊素-3-O-葡萄糖苷（D3G）之间的相互作用机制，应用了多种光谱分析方法和分子建模。荧光实验证明，多酚强烈猝灭β-LG 的固有荧光，主要通过静态猝灭，主要相互作用力是疏水相互作用。此外，傅里叶变换红外（FTIR）和圆二色性（CD）表明多酚改变了β-LG 的二级和三级结构。酶联免疫吸附试验和分子建模研究表明，由于多酚结合位点直接掩盖了 IgE 线性表位，β-LG 与多酚形成的复合物可显著降低β-LG 的 IgE 结合能力。总之，多酚会影响β-LG 的结构和潜在功能，这在乳制品加工业和食品营养安全方面具有重要意义。
