The Gluten Complex Studied by Urea Denaturation and Red-ox Titration
Gluten surface sites with low affinity for ANS, La low hydrophobicity, were more labile to urea than those with high hydrophobicity and disappeared nearly completely when urea was above 6 M. The surface of the gluten complex was only moderately affected by complete reduction, in which case less hydrophobic regions were more labile.
KeywordsSurface Hydrophobicity Gluten Protein High Hydrophobicity Bread Crumb Flour Dough
Unable to display preview. Download preview PDF.
- American Association Of Cereal Chemists, 1983. Approved Methods of the AACC., 8th ed. Method 38–10, approved April 1961. The Association: St. Paul, MN, USA.Google Scholar
- Cantor C.R., Schimmel P.R., 1980. Ligand interaction at equilibrium. In: V. H. Freeman (Ed.): Biophysical Chemistry, III. The Behaviour of Biological Macromolecules. San Francisco, C.A., USA., 849–886.Google Scholar
- Eckert B., Amend, T., Belitz H. D. Hypothesis on gliadin-glutenin interactions in wheat flour dough. In: Assoc. Cereal Res. (Ed): Gluten Proteins. Detmold, D.Google Scholar
- Eynard L., Guerrieri N., Cerletti P., 1994. Determination of wheat protein in solution by dye binding in flour, dough, and bread crumb. Cereal Chem. 71, 434–438.Google Scholar
- Gao L., Ng P.K.W., Bushuk, W. 1992. Structure of glutenin based on farinograph and electrophoretic results. Cereal Chem. 69, 452–455.Google Scholar
- Guerrieri N., Cerletti P., 1996. The effect of HTST treatment in wheat flour on gluten vitality and structure. Cereal Chem. 73, 375–378.Google Scholar
- Guerrieri N., Alberti E., Lavelli V, Cerletti P., 1996. The use of spectroscopic and fluorescence tecniques to assess heat-induced molecular modifications of gluten. Cereal Chem. 73, 368–374.Google Scholar