Moderate heat enhances gliadin-proanthocyanidin interactions.
Gliadins
Proanthocyanidins
Protein–polyphenol interactions
Quinoproteins
Journal
Food chemistry
ISSN: 1873-7072
Titre abrégé: Food Chem
Pays: England
ID NLM: 7702639
Informations de publication
Date de publication:
01 Nov 2022
01 Nov 2022
Historique:
received:
23
12
2021
revised:
23
05
2022
accepted:
26
05
2022
pubmed:
7
6
2022
medline:
25
6
2022
entrez:
6
6
2022
Statut:
ppublish
Résumé
Understanding wheat gliadin-proanthocyanidin (PA) interactions would be useful to systematically control foams and gels, create novel textures, and reduce inflammatory reactions. This work aimed to determine the effects of heat (50-90 °C) on gliadin-proanthocyanidin (PA) interactions. Gliadin-PA mixtures were heated for 30 min in aqueous ethanol, and resulting morphology, fluorescence, and MW distribution were analyzed. Atomic force microscopy showed that PA greatly increased gliadin particle size, especially with heat. PA significantly quenched gliadin's tryptophan fluorescence. Further fluorescence data analysis indicated that PA interacted with gliadins through static quenching, primarily via hydrophobic interactions, and that 75 °C treatment yielded the greatest gliadin-PA interactions, likely because the proteins unraveled and exposed residues for interaction. PA appeared to interact mostly with ω-gliadins, based on their absence in the SDS-PAGE gel. Though it has been overshadowed in previous studies by non-covalent interactions, staining of quinoproteins indicated that PA covalently cross-linked gliadins at pH ∼ 6.
Identifiants
pubmed: 35661606
pii: S0308-8146(22)01293-6
doi: 10.1016/j.foodchem.2022.133331
pii:
doi:
Substances chimiques
Proanthocyanidins
0
Gliadin
9007-90-3
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
133331Informations de copyright
Copyright © 2022 Elsevier Ltd. All rights reserved.