Solubility variation of wheat dough proteins: A practical way to track protein behaviors in dough processing.
2-DGE
Gluten proteins
Non-gluten proteins
Protein behavior
SE-HPLC
Journal
Food chemistry
ISSN: 1873-7072
Titre abrégé: Food Chem
Pays: England
ID NLM: 7702639
Informations de publication
Date de publication:
15 May 2020
15 May 2020
Historique:
received:
23
07
2019
revised:
05
11
2019
accepted:
06
12
2019
pubmed:
4
1
2020
medline:
27
3
2020
entrez:
4
1
2020
Statut:
ppublish
Résumé
To understand wheat dough protein behavior under dual mixing and thermal treatment, solubility of Mixolab-dough proteins were investigated using nine extraction buffers of different dissociation capacities. Size exclusion high performance liquid chromatography (SE-HPLC) and two-dimensional gel electrophoresis (2-DGE) demonstrated that overall changes of protein fractions and dynamic responses of specific proteins during dough processing were well reflected by their solubility variations. After starch pasting, the abundance of 0.5 M NaCl extractable proteins were decreased except for six protein groups including α-amylase inhibitors and superoxide dismutase (SOD). The solubility loss of glutenin proteins at C3 (32 min; 80 ℃) was mainly ascribed to the un-extractable HMW-GSs, LMW-GSs, globulin and triticin, while the extract yield of α-, β-, γ-gliadins and avenin-like proteins (ALPs) increased after starch pasting. Differential responses of dough proteins to extraction systems provides the basis for further exploring wheat protein dynamics in processing.
Identifiants
pubmed: 31896458
pii: S0308-8146(19)32183-1
doi: 10.1016/j.foodchem.2019.126038
pii:
doi:
Substances chimiques
Glutens
8002-80-0
Starch
9005-25-8
Gliadin
9007-90-3
glutenin
FX065C7O71
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
126038Informations de copyright
Copyright © 2019 Elsevier Ltd. All rights reserved.