Digestibility and allergenicity assessment of enzymatically crosslinked β‐casein

Dragana Stanic, Evanthia Monogioudi, Dilek Ercili Cura, Jelena Radosavljevic, Marina Atanaskovic-Markovic, Olga Vuckovic, Raija Lantto, Maija-Liisa Mattinen, Johanna Buchert, Tanja Cirkovic Velickovic (Corresponding Author)

    Research output: Contribution to journalArticleScientificpeer-review

    69 Citations (Scopus)


    Crosslinking enzymes are frequently used in bioprocessing of dairy products. The aim of this study was to examine the effects of enzymatic crosslinking on IgE binding, allergenicity and digestion stability of β‐casein (CN). β‐CN was crosslinked by transglutaminase, tyrosinase, mushroom tyrosinase/caffeic acid and laccase/caffeic acid. The IgE binding to β‐CN was compared in vitro by CAP inhibition assay, ELISA inhibition as well as ex vivo by basophil activation assay. Crosslinked CNs were digested by simulated gastric fluid for 15 and 60 min and obtained digests analyzed for their ability to inhibit IgE binding by CAP inhibition assay and SDS‐PAGE. The ability of crosslinked CNs to activate basophils was significantly reduced in seven patients in the case of CN crosslinked by laccase and moderately reduced in the case of tyrosinase/caffeic acid crosslinked CN (in two cow's milk allergy patients tested with different allergen concentrations). The response to various crosslinked CNs differed individually among patients' sera tested by ELISA inhibition assay. The presence of caffeic acid hampered digestion by pepsin, and this effect was most pronounced for the tyrosinase/caffeic acid crosslinked CN. The laccase/caffeic acid and mushroom tyrosinase/caffeic acid had the highest potential in mitigating IgE binding and allergenicity of the β‐CN out of all investigated enzymes. The presence of a small phenolic compound also increased digestion stability of β‐CN.
    Original languageEnglish
    Pages (from-to)1273-1284
    Number of pages8
    JournalMolecular Nutrition and Food Research
    Issue number9
    Publication statusPublished - 2010
    MoE publication typeA1 Journal article-refereed


    • Allergen
    • bioprocessing
    • casein
    • crosslinking enzymes
    • digestibility


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