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Boiling peanut Ara h 1 results in the formation of aggregates with reduced allergenicity
Authors:Blanc Fany  Vissers Yvonne M  Adel-Patient Karine  Rigby Neil M  Mackie Alan R  Gunning A Patrick  Wellner Nikolaus K  Skov Per S  Przybylski-Nicaise Laetitia  Ballmer-Weber Barbara  Zuidmeer-Jongejan Laurian  Szépfalusi Zsolt  Ruinemans-Koerts Janneke  Jansen Ad P H  Bernard Hervé  Wal Jean-Michel  Savelkoul Huub F J  Wichers Harry J  Mills E N Clare
Affiliation:INRA, UR496, Unité d'Immuno-Allergie Alimentaire, Jouy-en-Josas, France.
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.
Keywords:Allergenicity  Ara h 1  EuroPrevall  IgE  Peanut allergy  Thermal processing
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