Release and conformational changes in allergenic proteins from wheat gluten induced by high hydrostatic pressure.
Allergen release
Allergenicity
High hydrostatic pressure
Intermolecular forces
Wheat gluten
Journal
Food chemistry
ISSN: 1873-7072
Titre abrégé: Food Chem
Pays: England
ID NLM: 7702639
Informations de publication
Date de publication:
30 Jan 2022
30 Jan 2022
Historique:
received:
04
11
2020
revised:
02
08
2021
accepted:
04
08
2021
pubmed:
18
8
2021
medline:
21
10
2021
entrez:
17
8
2021
Statut:
ppublish
Résumé
The gluten proteins of wheat are major causative agents of harmful immune responses. This study investigated the effects of high hydrostatic pressure (200, 300, 400, and 500 MPa), treatment time (5-25 min) and protein concentration (1%-5% protein weight/volume) on the structures underlying the allergenicity wheat gluten. The results showed that a combination of 400 MPa, 20 min treatment time and 3% protein reduced the wheat gluten allergenicity by 72.2%. Moreover, a Western blotting showed that the allergenicity of 26, 28, 48, 68 kDa and high molecular weight glutenin was sharply reduced. Fourier infrared spectroscopy and surface hydrophobicity indicated that gluten molecules aggregated after HHP treatment. Intermolecular forces indicated that gluten aggregated mainly through hydrophobic interactions and disulfide bonds but not by hydrogen bonds after HHP treatment. These results suggest that structural changes contributed to the reduction of wheat gluten allergenicity and that HHP may enhance safety for susceptible individuals.
Identifiants
pubmed: 34404002
pii: S0308-8146(21)01811-2
doi: 10.1016/j.foodchem.2021.130805
pii:
doi:
Substances chimiques
Allergens
0
Glutens
8002-80-0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
130805Informations de copyright
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