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

15 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

Fingerprint

Pepsin A
pepsin
allergens
epitopes
peanuts
Epitopes
Hot Temperature
Molecular mass
heat
Allergens
peptides
molecular weight
Peptides
Immunoglobulin E
Arachis hypogaea Ara h 1 protein

Keywords

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

Cite this

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title = "Determination of Pepsin-Susceptible and Pepsin-Resistant Epitopes in Native and Heat-Treated Peanut Allergen Ara h 1",
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 (",
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publisher = "American Chemical Society",
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Determination of Pepsin-Susceptible and Pepsin-Resistant Epitopes in Native and Heat-Treated Peanut Allergen Ara h 1. / van Boxtel, E.L.; Koppelman, S.J.; van den Broek, L.A.M.; Gruppen, H.

In: Journal of Agricultural and Food Chemistry, Vol. 56, No. 6, 2008, p. 2223-2230.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Determination of Pepsin-Susceptible and Pepsin-Resistant Epitopes in Native and Heat-Treated Peanut Allergen Ara h 1

AU - van Boxtel, E.L.

AU - Koppelman, S.J.

AU - van den Broek, L.A.M.

AU - Gruppen, H.

PY - 2008

Y1 - 2008

N2 - 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 (

AB - 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 (

KW - mass-spectrometry

KW - in-vitro

KW - major allergen

KW - food allergens

KW - proteins

KW - digestion

KW - identification

KW - vicilin

KW - degradation

KW - convicilin

U2 - 10.1021/jf072907n

DO - 10.1021/jf072907n

M3 - Article

VL - 56

SP - 2223

EP - 2230

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

SN - 0021-8561

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