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.

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Record number 417191
Title Effect of roasting on the allergenicity of major peanut allergens Ara h 1 and Ara h 2/6: the necessity of degranulation assays
Author(s) Vissers, Y.M.; Iwan, M.; Adel-Patient, K.; Stahl Skov, P.; Rigby, N.M.; Johnson, P.E.; Mandrup Muller, P.; Przybylski-Nicaise, L.; Schaap, M.; Ruinemans-Koerts, J.; Jansen, A.P.H.; Mills, E.N.C.; Savelkoul, H.F.J.; Wichers, H.J.
Source Clinical and Experimental Allergy 41 (2011)11. - ISSN 0954-7894 - p. 1631 - 1642.
Department(s) Cell Biology and Immunology
FBR Fresh Supply Chains
Food Chemistry Group
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) plant food allergens - ige-binding - enzyme immunoassays - maillard reaction - cooking methods - protein - children - ara-h-1 - purification - reactivity
Abstract Background - Peanuts are often consumed after roasting, a process that alters the three-dimensional structure of allergens and leads to Maillard modification. Such changes are likely to affect their allergenicity. Objective - We aimed to establish the effect of thermal treatment mimicking the roasting process on the allergenicity of Ara h 1 and a mix of 2S albumins from peanut (Ara h 2/6). Methods - Ara h 1 and Ara h 2/6 were purified from raw peanuts and heated in a dry form for 20 min at 145 °C in the presence (R+g) or absence (R-g) of glucose, and soluble proteins were then extracted. Sera obtained from 12 well-characterized peanut-allergic patients were used to assess the IgE binding and degranulation capacities of the allergens. Results - Extensive heating at low moisture resulted in the hydrolysis of both Ara h 1 and Ara h 2/6. However, in contrast to Ara h 2/6, soluble R+g Ara h 1 formed large aggregates. Although the IgE-binding capacity of R+g and R-g Ara h 1 was decreased 9000- and 3.6-fold, respectively, compared with native Ara h 1, their capacity to elicit mediator release was increased. Conversely, both the IgE-binding capacity and the degranulation capacity of R-g Ara h 2/6 were 600–700-fold lower compared with the native form, although the presence of glucose during heating significantly moderated these losses. Conclusions - and Clinical Relevance Extensive heating reduced the degranulation capacity of Ara h 2/6 but significantly increased the degranulation capacity of Ara h 1. This observation can have important ramifications for component-resolved approaches for diagnosis and demonstrates the importance of investigating the degranulation capacity in addition to IgE reactivity when assessing the effects of food processing on the allergenicity of proteins.
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