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 416600
Title Boiling peanut Ara h 1 results in the formation of aggregates with reduced allergenicity
Author(s) Blanc, F.; Vissers, Y.M.; Adel-Patient, K.; Rigby, N.M.; Mackie, A.R.; Gunning, A.P.; Wellner, N.K.; Skov, P.S.; Przybylski-Nicaise, L.; Ballmer-Weber, B.; Zuidmeer-Jongejan, L.; Szépfalusi, Z.; Ruinemans-Koerts, J.; Jansen, A.P.; Bernard, H.; Wal, J.M.; Savelkoul, H.F.J.; Wichers, H.J.; Mills, E.N.C.
Source Molecular Nutrition & Food Research 55 (2011)12. - ISSN 1613-4125 - p. 1887 - 1894.
DOI https://doi.org/10.1002/mnfr.201100251
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) food allergens - ige binding - proteins - ara-h-1
Abstract Scope: Roasting rather than boiling and Maillard modifications may modulate peanut allergenicity. We investigated how these factors affect the allergenic properties of a major peanut allergen, Ara h 1. Methods and results: Ara h 1 was purified from either raw (N-Ara h 1) or roasted (R-Ara h 1) peanuts. Boiling (100°C 15¿min; H-Ara h 1) resulted in a partial loss of Ara h 1 secondary structure and formation of rod-like branched aggregates with reduced IgE-binding capacity and impaired ability to induce mediator release. Glycated Ara h 1 (G-Ara h 1) formed by boiling in the presence of glucose behaved similarly. However, H- and G-Ara h1 retained the T-cell reactivity of N-Ara h 1. R-Ara h 1 was denatured, comprised compact, globular aggregates, and showed no evidence of glycation but retained the IgE-binding capacity of the native protein. Conclusion: Ara h 1 aggregates formed by boiling were morphologically distinct from those formed by roasting and had lower allergenic activity. Glycation had no additional effect on Ara h 1 allergenicity compared with heating alone. Taken together with published data on the loss of Ara h 2/6 from boiled peanuts, this supports the hypothesis that boiling reduces the allergenicity of peanuts
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