Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy

J. Radosavljevic, Emilia Nordlund, L. Mihajlovic, M. Krstic, T. Bohn, Johanna Buchert, T.C. Velickovic (Corresponding Author), J. Smit

    Research output: Contribution to journalArticleScientificpeer-review

    29 Citations (Scopus)



    The cross‐linking of proteins by enzymes to form high‐molecular‐weight protein, aggregates can be used to tailor the technological or physiological functionality of food products. Aggregation of dietary proteins by food processing may promote allergic sensitization, but the effects of enzymatic cross‐linking of dietary proteins on the allergenic potential of food are not known. In this study, the bioavailability and the sensitizing or tolerizing potential of peanut proteins (PE) cross‐linked with microbial tyrosinase from Trichoderma reesei and mushroom tyrosinase from Agaricus bisporus, were investigated.

    Methods and results

    The impact of cross‐linking of PE on the in vitro bioavailability of fluorescein isothiocyanate‐labeled peanut proteins was tested in a Caco‐2 cell monolayer and by competitive ELISA. The in vivo allergenicity or capacity to induce oral tolerance in mice were measured by serum levels of PE‐specific antibodies and T cell cytokine production after exposure to PE and cross‐linked PE.


    Enzymatic processing of peanut proteins by the two tyrosinases increased the bioavailability of major peanut allergen Ara h 2, but did not significantly change the allergenic or tolerizing properties of peanut. Enzymatic treatment of peanut proteins yielded cross‐linked proteins with preserved molecular and immunological features of peanut allergens.
    Original languageEnglish
    Pages (from-to)635-646
    Number of pages12
    JournalMolecular Nutrition and Food Research
    Issue number3
    Publication statusPublished - 2014
    MoE publication typeA1 Journal article-refereed


    • allergenicity
    • peanut
    • protein cross-linking
    • tyrosinase


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