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 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.
DOI http://dx.doi.org/10.1111/j.1365-2222.2011.03830.x
Department(s) Cell Biology and Immunology
FBR Fresh Supply Chains
Food Chemistry Group
VLAG
WIAS
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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