Journal
FOOD CHEMISTRY
Volume 358, Issue -, Pages -Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2021.129916
Keywords
Raman spectroscopy; Bread dough mixing; Gluten protein conformation; Disulphide bond conformation; Thiol blocking agent
Funding
- ANR project MIXI-LAB [15-LCV30006-01]
- VMI
- ANRT
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The study evaluated the use of Raman spectroscopy in analyzing gluten protein structural changes during mixing, and found that the addition of TCEP reagent can alter the protein structure.
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 I3-sheet and alpha-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 I3-sheet and alpha-helix structures and lead to a more disordered secondary protein structure.
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