Interaction Mechanism of β-lactoglobulin and Phlorizin Under Thermal Processing and the Effect of Immune Attenuation

Abstract

βlactoglobulin (β-LG) is an important whey protein because of its high ability to bind hydrophobic small molecules. Phlorizin is a kind of apple polyphenol. The interaction mechanism between phlorizin and β-lactoglobulin in the milk system and the effect of phlorizin on β-LG after thermal processing are still unclear. Therefore, the interaction mechanism between β-LG and phlorizin and the structural and antigenic changes of the compound under different thermal processing was studied. Firstly, the binding mode of phlorizin and β-LG was simulated by molecular docking, and the binding mechanism of phlorizin and β-LG conformation changes were explored by spectroscopy. Indirect ELISA was used to evaluate the effect of phlorizin on the reduction of β-LG antigen. Phroside interacts with β-LG mainly by static quenching and hydrophobic force. Due to the addition of phlorizin, the hydrophobic groups on the surface of the compound heated at 100℃ were hidden, and the hydrophobic interaction between phlorizin and β-LG was weakened. And the addition of phlorizin after thermal processing changed the secondary structure of β-LG, β-sheet, and random coil were reducing, and α-helix was increasing. Phlorizin reduced the antigenicity of β-LG, but there was no significant difference between thermal processing under 100℃.