Myricetin suppresses whey protein allergenicity: In vitro and in vivo study.
- 2026-06
- Food chemistry. Molecular sciences 12
- PubMed: 41815264
- DOI: 10.1016/j.fochms.2026.100380
Study Design
- Population
- BALB/c mice with whey protein-induced allergy
- Methods
- Screening of 27 dietary polyphenols, molecular docking, free thiol group determination, and in vivo BALB/c mouse model with dietary administration of whey protein combined with myricetin
- Funding
- Unclear
Reducing the allergenicity of milk-derived proteins is essential for the development of hypoallergenic dairy products. This study was designed to test the hypothesis that myricetin attenuates the allergenicity of whey protein by masking immunoreactive epitopes and modulating immune responses In this study, the effects of myricetin on whey protein allergenicity were evaluated using in vitro and in vivo models. Twenty-seven dietary polyphenols were screened for their ability to inhibit β-lactoglobulin antigenicity using an indirect enzyme-linked immunosorbent assay, and myricetin was identified as the most effective compound. Molecular docking analysis and free thiol group determination suggested that myricetin preferentially interacted with the free thiol group of cysteine 121, suggesting epitope masking as a potential mechanism. In a BALB/c mouse model of whey protein-induced allergy, dietary administration of whey protein combined with myricetin reduced serum mast cell protease-1, antigen-specific immunoglobulin G, and type 2 helper T-cell-associated cytokines, compared with whey protein alone. In addition, myricetin supplementation altered the composition of the intestinal microbiota. These findings support our hypothesis that myricetin can reduce the allergenicity of whey protein, likely through epitope masking and immune-modulatory effects involving the gut microbiota, and highlight its potential application as a natural strategy for producing dairy products with reduced allergenic potential.
Research Insights
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