Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 408073
Title Impact of Maillard Reaction on Immunoreactivity and Allergenicity of the Hazelnut Allergen Cor a 11
Author(s) Iwan, M.; Vissers, Y.M.; Fiedorowicz, E.; Kostyra, H.; Savelkoul, H.F.J.; Wichers, H.J.
Source Journal of Agricultural and Food Chemistry 59 (2011)13. - ISSN 0021-8561 - p. 7163 - 7171.
DOI http://dx.doi.org/10.1021/jf2007375
Department(s) Cell Biology and Immunology
FBR Fresh Supply Chains
Food Chemistry Group
WIAS
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) controlled food challenge - ige-binding epitopes - corylus-avellana - roasted hazelnuts - peanut proteins - double-blind - 2s albumin - tree nut - denaturation - vicilin
Abstract 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.
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