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- W4283447321 endingPage "111572" @default.
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- W4283447321 abstract "Bee pollen as a plant-derived food is consumed as nutritional/functional supplements by humans. But it might confer foodborne allergenicity in susceptible populations, limiting its extensive application. In this study, five potential allergens including profilin, cystatin, prolamin, expansin, and alcohol dehydrogenase in bee pollen derived from Brassica campestris (BP-Bc), were identified through mass spectrometry-based proteomic analysis. Moreover, different types of enzymes (cellulases, pectases, and papains) serve biological roles in pollen wall breaking and expansion, but also promote allergen release and degradation. Proteomic analysis showed that profilin, cystatin, and alcohol dehydrogenase were significantly reduced in BP-Bc following joint treatment with three enzymes. Metabolomic characterization of potential enzymatic hydrolysates of these significantly-decreased allergens was performed, which showed nine major oligopeptides and six amino acids at significantly higher levels in the enzyme-treated BP-Bc. These findings clarified the culprit responsible for bee pollen allergy and the mechanism of enzymatic desensitization for its further development." @default.
- W4283447321 created "2022-06-26" @default.
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- W4283447321 date "2022-08-01" @default.
- W4283447321 modified "2023-09-28" @default.
- W4283447321 title "Identification of allergens and allergen hydrolysates by proteomics and metabolomics: A comparative study of natural and enzymolytic bee pollen" @default.
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- W4283447321 doi "https://doi.org/10.1016/j.foodres.2022.111572" @default.
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