Study of structural changes of gluten proteins during bread dough mixing by Raman spectroscopy
| Autor: | Ali Assaf, Joran Fontaine, Eloïse Lancelot, Gérald Thouand, Joëlle Grua-Priol, Alain Le-Bail |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
Glutens
Phosphines Flour Spectrum Analysis Raman 01 natural sciences Protein Structure Secondary Analytical Chemistry chemistry.chemical_compound symbols.namesake 0404 agricultural biotechnology Disulfides Protein secondary structure Triticum chemistry.chemical_classification 010401 analytical chemistry Intermolecular force Tryptophan Bread 04 agricultural and veterinary sciences General Medicine 040401 food science Gluten 0104 chemical sciences Crystallography chemistry Reagent TCEP symbols Thiol Tyrosine Raman spectroscopy Food Science |
| Zdroj: | Food Chemistry. 358:129916 |
| ISSN: | 0308-8146 |
| DOI: | 10.1016/j.foodchem.2021.129916 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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