Localization and identification of denatured antigenic sites of glycinin A3 subunit after using two processing technologies.
A3 subunit
Allergic site
Amino acid
Antigenic sites
Indirect ELISA
Journal
Food research international (Ottawa, Ont.)
ISSN: 1873-7145
Titre abrégé: Food Res Int
Pays: Canada
ID NLM: 9210143
Informations de publication
Date de publication:
Sep 2023
Sep 2023
Historique:
received:
26
04
2023
revised:
31
05
2023
accepted:
01
06
2023
medline:
19
6
2023
pubmed:
18
6
2023
entrez:
18
6
2023
Statut:
ppublish
Résumé
Glycinin is an important allergen in soybeans. In this study, molecular cloning and recombinant phage construction were performed to explore the antigenic sites of the glycinin A3 subunit that were denatured during processing. Next, the A-1-a fragment was located as the denatured antigenic sites by indirect ELISA. The combined UHP heat treatment showed better denaturation of this subunit than the single heat treatment assay. In addition, identification of the synthetic peptide showed that the A-1-a fragment was an amino acid sequence containing a conformational and linear IgE site, in which the first synthetic peptide (P1) being both an antigenic and allergenic site. The results of alanine-scanning showed that the key amino acids affecting antigenicity and allergenicity of A3 subunit were S
Identifiants
pubmed: 37330838
pii: S0963-9969(23)00627-0
doi: 10.1016/j.foodres.2023.113082
pii:
doi:
Substances chimiques
glycinin
9007-93-6
Soybean Proteins
0
Globulins
0
Allergens
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
113082Informations de copyright
Copyright © 2023. Published by Elsevier Ltd.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.