Thermoanalytical characterization of high molecular weight glutenin subunits - Water effect on their glass transition

Citation
F. Castelli et al., Thermoanalytical characterization of high molecular weight glutenin subunits - Water effect on their glass transition, THERMOC ACT, 346(1-2), 2000, pp. 153-160
Citations number
25
Categorie Soggetti
Spectroscopy /Instrumentation/Analytical Sciences
Journal title
THERMOCHIMICA ACTA
ISSN journal
00406031 → ACNP
Volume
346
Issue
1-2
Year of publication
2000
Pages
153 - 160
Database
ISI
SICI code
0040-6031(20000329)346:1-2<153:TCOHMW>2.0.ZU;2-H
Abstract
The thermal behaviour of the high M-r, glutenin subunits (a group of storag e proteins in wheat grains) 1Dx5, 1Bx7, 1Dx2, 1Bx20, 1Dy12, 1Bx6 and 1Dy10, was investigated using Differential Scanning Calorimetry and Thermogravime tric Analysis. Also included in these studies, for comparison, was a M-r 58 000 peptide (5 8 K) derived from the repetitive domain of subunit 1Dx5 and expressed in Es cherichia Coli. The plasticizing effect of water on each protein was invest igated. When submitted to the calorimetric analysis, the high M-r glutenin subunits exhibited a glass transition phenomenon that was affected by the water con tent. As expected, the glass transition temperature decreased as the water content was increased. (C) 2000 Elsevier Science B.V. All rights reserved.