Conformation and Surface Properties of Deamidated Gluten
- 1 June 1982
- journal article
- research article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 46 (6) , 1583-1586
- https://doi.org/10.1080/00021369.1982.10865285
Abstract
The surface properties of deamidated gluten were investigated with respect to their conformational changes. The helix content of gluten decreased curvilinearly with its decrease of deamidation. The surface tension decreased in proportion to the degree of deamidation. On the other hand, the surface hydrophobicity of gluten increased remarkably in proportion to the degree of deamidation. The emulsifying properties of gluten were improved greatly by deamidation, correlating linearly with the surface hydrophobicity. From these results, the relationships between the conformational changes and functional properties of deamidated gluten are discussed.This publication has 4 references indexed in Scilit:
- Effects of Partial Denaturation on Surface Properties of Ovalbumin and LysozymeAgricultural and Biological Chemistry, 1981
- Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteinsBiochimica et Biophysica Acta (BBA) - Protein Structure, 1980
- Emulsifying properties of proteins: evaluation of a turbidimetric techniqueJournal of Agricultural and Food Chemistry, 1978
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951