| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10544379 | Food Chemistry | 2005 | 9 Pages |
Abstract
The structural investigation, by analysis of the amide I region of the infrared spectra of gluten samples, solubilised in the presence of additives, showed an increase in the proportion of β-turns and extended structures, accompanied by a decrease in the α-helix proportion. Such results confirm and explain the improvement of wheat gluten solubility by enhancing water-protein bonding and reducing protein-protein interactions. Structural changes result in a better accessibility of more water molecules to the protein and in greater hydration and solubilisation effects.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Mondher Mejri, Barbara Rogé, Abdelfattah BenSouissi, Franck Michels, Mohamed Mathlouthi,