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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

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Abstract

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.

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The data that support the findings of this study are available on request from the corresponding author. The data are not publicly available due to privacy restrictions.

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Acknowledgements

We would also like to thank the School of Chemical Engineering of Sichuan University for their assistance in the computer simulation experiment.

Funding

This work was support by the National Key Research and Development Program of China (2022YFD2101001) and the National Natural Science Foundation of China (3236064).

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Authors and Affiliations

  1. Meat Processing Key Laboratory of Sichuan Province, School of Food and Biological Engineering, Chengdu University, No. 2025 Chengluo Avenue, Chengdu, 610106, China

    Yuanqiao Li, Mohan Li, Qinhong Li, Fang Geng, Na Gan & Di Wu

  2. Engineering Research Center of Bio-Process (Ministry of Education), Key Laboratory for Agricultural Products Processing of Anhui Province, School of Food and Biological Engineering, Hefei University of Technology, No. 420 Jade Road, Hefei, 230601, China

    Shugang Li

  3. Food College, Shihezi University, Shihezi, Xinjiang Autonomus Region, 832061, China

    Qingling Wang

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  1. Yuanqiao Li
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  2. Mohan Li
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Contributions

Yuanqiao Li: investigation, data curation, and writing—original draft preparation. Mohan Li: visualization. Qinhong Li: software. Fang Geng: resources. Qingling Wang: supervision. Na Gan: software. Shugang Li: resources. Di Wu: conceptualization, methodology, writing—reviewing and editing, and project administration.

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Correspondence to Di Wu.

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Li, Y., Li, M., Li, Q. et al. 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. Food Bioprocess Technol (2023). https://doi.org/10.1007/s11947-023-03298-5

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