2. Academic Validation
  3. Comparative studies of interaction of β-lactoglobulin with three polyphenols

Comparative studies of interaction of β-lactoglobulin with three polyphenols

  • Int J Biol Macromol. 2019 Sep 1;136:804-812. doi: 10.1016/j.ijbiomac.2019.06.053.
Jinhui Xu 1,  Minghao Hao 1,  Qifan Sun 1,  Lin Tang 2
Affiliations

Affiliations

  • 1 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.
  • 2 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. Electronic address: tanglin@sdnu.edu.cn.
PMID: 31228500 DOI: 10.1016/j.ijbiomac.2019.06.053
Abstract

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.

Keywords

Allergenicity; Binding; Multi-spectrometry; Polyphenol; β-Lactoglobulin.

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