Impact of Maillard Reaction on Immunoreactivity and Allergenicity of the Hazelnut Allergen Cor a 11

M. Iwan, Y.M. Vissers, E. Fiedorowicz, H. Kostyra, H.F.J. Savelkoul, H.J. Wichers

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42 Citations (Scopus)


Few studies exist on the influence of processing methods on structural changes and allergenic potential of hazelnut proteins. This study focused on the effect of glycation (Maillard reaction) on the immunoreactivity and degranulation capacity of the purified hazelnut 7S globulin, Cor a 11. After heating, the extent of the Maillard reaction, sensitivity to proteolysis, binding of human IgE or rabbit IgG, and degranulation capacity were analyzed. Changes in electrophoretic mobility, amount of free amino groups, and contents of bound sugar and fructosamine indicated that glycation of Cor a 11 occurred at all conditions. Glycation at 37 °C did not influence the specific IgG or IgE binding and was decreased after heating at 60 and 145 °C. Heating, with or without glucose, at 145 °C increased basophil degranulation capacity. The results suggest that glycation of Cor a 11 at 60 and 145 °C may decrease the IgE/IgG binding properties but not the degranulation capacity of basophils. This is possibly related to aggregation of the proteins as a result of the Maillard reaction.
Original languageEnglish
Pages (from-to)7163-7171
JournalJournal of Agricultural and Food Chemistry
Issue number13
Publication statusPublished - 2011


  • controlled food challenge
  • ige-binding epitopes
  • corylus-avellana
  • roasted hazelnuts
  • peanut proteins
  • double-blind
  • 2s albumin
  • tree nut
  • denaturation
  • vicilin

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