Determination of Pepsin-Susceptible and Pepsin-Resistant Epitopes in Native and Heat-Treated Peanut Allergen Ara h 1

E.L. van Boxtel, S.J. Koppelman, L.A.M. van den Broek, H. Gruppen

Research output: Contribution to journalArticleAcademicpeer-review

18 Citations (Scopus)

Abstract

This study was aimed at the determination of the pepsin-susceptible and pepsin-resistant epitopes in native and heat-treated Ara h 1, a major allergen from peanuts. Both the oligomeric structure and the trimeric structure of the allergen were investigated. Under the in vitro conditions applied, oligomeric Ara h 1, either unheated or preheated, was hydrolyzed by pepsin at a lower rate than trimeric Ara h 1. Peptides with relatively high molecular masses were shown to be able to bind IgE, whereas peptides with lower molecular masses (
Original languageEnglish
Pages (from-to)2223-2230
JournalJournal of Agricultural and Food Chemistry
Volume56
Issue number6
DOIs
Publication statusPublished - 2008

Keywords

  • mass-spectrometry
  • in-vitro
  • major allergen
  • food allergens
  • proteins
  • digestion
  • identification
  • vicilin
  • degradation
  • convicilin

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