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Comparative studies of interaction of β-lactoglobulin with three polyphenols.

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.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Xu J,Hao M,Sun Q,Tang L

doi

10.1016/j.ijbiomac.2019.06.053

subject

Has Abstract

pub_date

2019-09-01 00:00:00

pages

804-812

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(19)31998-1

journal_volume

136

pub_type

杂志文章

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