Revealing the Potential of Theaflavin to Reduce Egg Allergenicity at the Molecular Level: A Study of the Binding Affinity of Theaflavin to Egg White Lysozyme

Tea polyphenols are considered one of the effective means to reduce protein sensitization, and it is necessary to study their binding mechanism. Therefore, this study investigated the major polyphenol theaflavin (TF) in black tea to investigate its interaction mechanism with egg white lysozyme (LYZ) using multispectral techniques and computer simulations. Molecular global docking and local docking showed that the binding sites of TF and LYZ overlapped highly with the sensitizing linear epitopes. Fluorescence spectroscopy experiments showed that TF formed a ground state complex with LYZ mainly through electrostatic forces to quench its endogenous fluorescence and lead to a decrease in surface hydrophobicity, and the binding reaction proceeded spontaneously; circular dichroism spectra indicated that the addition of TF affected the secondary structure of LYZ. In addition, enzymatic activity assays and in vitro antioxidant assays showed that this interaction slightly reduced the activity of LYZ on the one hand and the antioxidant activity of TF on the other. These results reveal the potential of TF to reduce the allergenicity of egg at the molecular level and provide a theoretical basis for applying tea polyphenols.