期刊
FOOD CHEMISTRY-X
卷 19, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.fochx.2023.100773
关键词
Tartary buckwheat; Allergenicity; HPLC/MS-MS; Fermentation
Our study demonstrated that fermentation by Pediococcus pentosaceus degrades allergenic proteins in Tartary buckwheat, leading to a reduction in IgE-binding activity. Comparison with unfermented Tartary buckwheat peptides showed that 756 fragments associated with allergenic proteins were upregulated and the expression of 213 fragments was reduced by 71.83% after fermentation. Bioactivity prediction identified six peptide fragments derived from Fagt 1, potentially contributing to the residual allergenicity in the fermented product.
Tartary buckwheat contains more valuable nutrients than common buckwheat, but it also contains allergenic proteins that induce allergic reactions through an IgE-mediated response. Our study demonstrated that fermentation by Pediococcus pentosaceus degrades allergenic proteins in Tartary buckwheat, as confirmed by HPLC-MS/MS analysis of polypeptides. Our results showed significant degradation of the protein after 16 h of Pediococcus pentosaceus fermentation (PP16), leading to a reduction in IgE-binding activity. Comparison with unfermented Tartary buckwheat (UTB) peptides yielded 2042 fragments, of which 756 fragments associated with allergenic proteins were upregulated. Among them, the expression of 213 fragments was reduced by 71.83%. By performing bioactivity prediction on potential allergenic peptide fragments, we identified six peptide fragments derived from Fagt 1, potentially contributing to the residual allergenicity in PP16. These suggest that Pediococcus pentosaceus fermentation can effectively destroy allergen epitopes and mitigate the allergenicity of Tartary buckwheat.
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