title: Boiling peanut Ara h 1 results in the formation of aggregates with reduced allergenicity.
abstract: METHODS
  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.
  
  
  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.
  
  
  CONCLUSIONS
  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.
authors.affiliation: INRA, UR496, Unité d'Immuno-Allergie Alimentaire, Jouy-en-Josas, France.
authors.forename: Fany
authors.initials: F
authors.lastname: Blanc
authors.forename: Yvonne M
authors.initials: YM
authors.lastname: Vissers
authors.forename: Karine
authors.initials: K
authors.lastname: Adel-Patient
authors.forename: Neil M
authors.initials: NM
authors.lastname: Rigby
authors.forename: Alan R
authors.initials: AR
authors.lastname: Mackie
authors.forename: A Patrick
authors.initials: AP
authors.lastname: Gunning
authors.forename: Nikolaus K
authors.initials: NK
authors.lastname: Wellner
authors.forename: Per S
authors.initials: PS
authors.lastname: Skov
authors.forename: Laetitia
authors.initials: L
authors.lastname: Przybylski-Nicaise
authors.forename: Barbara
authors.initials: B
authors.lastname: Ballmer-Weber
authors.forename: Laurian
authors.initials: L
authors.lastname: Zuidmeer-Jongejan
authors.forename: Zsolt
authors.initials: Z
authors.lastname: Szépfalusi
authors.forename: Janneke
authors.initials: J
authors.lastname: Ruinemans-Koerts
authors.forename: Ad P H
authors.initials: AP
authors.lastname: Jansen
authors.forename: Hervé
authors.initials: H
authors.lastname: Bernard
authors.forename: Jean-Michel
authors.initials: JM
authors.lastname: Wal
authors.forename: Huub F J
authors.initials: HF
authors.lastname: Savelkoul
authors.forename: Harry J
authors.initials: HJ
authors.lastname: Wichers
authors.forename: E N Clare
authors.initials: EN
authors.lastname: Mills
mesh_terms: D000485:Allergens / Q000737:chemistry* / Q000276:immunology; D000818:Animals; D052179:Antigens, Plant / Q000276:immunology*; D010367:Arachis / Q000737:chemistry* / Q000276:immunology; D002460:Cell Line; D049109:Cell Proliferation; D005260:Female; D005511:Food Handling / Q000379:methods*; D006023:Glycoproteins / Q000276:immunology*; D006632:Histamine / Q000096:biosynthesis; D006358:Hot Temperature; D006801:Humans; D007073:Immunoglobulin E / Q000378:metabolism; D007963:Leukocytes, Mononuclear / Q000276:immunology / Q000378:metabolism; D008297:Male; D008565:Membrane Proteins; D021183:Peanut Hypersensitivity / Q000276:immunology* / Q000517:prevention & control; D010940:Plant Proteins / Q000276:immunology*; D051381:Rats; D013601:T-Lymphocytes; D055815:Young Adult
chemical_list: D000485:Allergens; D052179:Antigens, Plant; C500889:Ara h 1 protein, Arachis hypogaea; D006023:Glycoproteins; D008565:Membrane Proteins; D010940:Plant Proteins; D007073:Immunoglobulin E; D006632:Histamine