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• W2175032009 abstract "Abstract BACKGROUND Peanut is one of the eight major food allergens. Its allergen, Ara h 2, can be recognized by over 90% of serum IgE samples from peanut‐allergic patients. Therefore, reducing the allergenicity of Ara h 2 is especially important. RESULTS In the present study, polyphenol oxidase ( PPO ), a protein cross‐linking reaction catalyst that acts on tyrosine residue, was used to modify Ara h 2. After crosslinking, the microstructure, digestibility, IgG binding capability and IgE binding capability of Ara h 2 were analyzed. Cross‐linking decreased the potential allergenicity of Ara h 2 by masking the allergen epitope, while the antigenicity of Ara h 2 changed slightly. After crosslinking, the apparent diameter of Ara h 2 was altered from 300 to 1700 nm or 220 nm, indicating that polymerization could either be inter‐ or intramolecular. Regarding digestibility, crosslinked Ara h 2 was relatively more easily digested by gastric fluid compared with the untreated Ara h 2, but much more difficult in the intestinal fluid. CONCLUSION The crosslinking reaction catalyzed by PPO , as a non‐thermal process, may be beneficial for avoiding food allergy. The reaction could mask allergen epitopes, decreasing the allergenicity of Ara h 2. © 2015 Society of Chemical Industry" @default.
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• W2175032009 date "2016-01-19" @default.
• W2175032009 modified "2023-10-16" @default.
• W2175032009 title "Crosslinking of peanut allergen Ara h 2 by polyphenol oxidase: digestibility and potential allergenicity assessment" @default.
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• W2175032009 doi "https://doi.org/10.1002/jsfa.7542" @default.
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