Study of structural changes of gluten proteins during bread dough mixing by Raman spectroscopy.
Bread dough mixing
Disulphide bond conformation
Gluten protein conformation
Raman spectroscopy
Thiol blocking agent
Tris(2-carboxyethyl)phosphine (TCEP) (PubChem CID 119411)
Journal
Food chemistry
ISSN: 1873-7072
Titre abrégé: Food Chem
Pays: England
ID NLM: 7702639
Informations de publication
Date de publication:
01 Oct 2021
01 Oct 2021
Historique:
received:
20
01
2020
revised:
24
03
2021
accepted:
18
04
2021
pubmed:
4
5
2021
medline:
10
6
2021
entrez:
3
5
2021
Statut:
ppublish
Résumé
The aim of the present study was to evaluate Raman spectroscopy in determining changes that occur in the structure of gluten proteins induced during bread dough mixing. Raman spectra were measured directly within the dough. Three particular phases of mixing were studied: under-mixing, optimum mixing and over-mixing. A thiol blocking reagent, Tris(2-carboxyethyl)phosphine (TCEP) was then used to reduce disulphide bonds within proteins to confirm the important role of disulphide bridges in gluten network formation. For the control dough, the most important changes occurred during the optimum mixing phase when an increase in intermolecular disulphide bonds, anti-parallel β-sheet and α-helix structures was observed, combined with the hydrophobic burial of tryptophan and tyrosine residues. The addition of TCEP appeared to effectively reduce the formation of intermolecular disulphide bonds, anti-parallel β-sheet and α-helix structures and lead to a more disordered secondary protein structure.
Identifiants
pubmed: 33940303
pii: S0308-8146(21)00922-5
doi: 10.1016/j.foodchem.2021.129916
pii:
doi:
Substances chimiques
Disulfides
0
Phosphines
0
tris(2-carboxyethyl)phosphine
22OAC2MO2S
Tyrosine
42HK56048U
Glutens
8002-80-0
Tryptophan
8DUH1N11BX
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
129916Informations de copyright
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