Thermal properties of corn gluten meal and its proteic components

Citation
L. Di Gioia et al., Thermal properties of corn gluten meal and its proteic components, INT J BIO M, 24(4), 1999, pp. 341-350
Citations number
37
Categorie Soggetti
Biochemistry & Biophysics
Journal title
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
ISSN journal
01418130 → ACNP
Volume
24
Issue
4
Year of publication
1999
Pages
341 - 350
Database
ISI
SICI code
0141-8130(199905)24:4<341:TPOCGM>2.0.ZU;2-#
Abstract
Thermal properties of corn gluten meal (CGM) and of its extracted proteic c omponents (zein and glutelin) at 0% moisture content, is studied by dynamic mechanical thermal analysis (DMTA) and modulated differential scanning cal orimetry (MDSC). The glass transition temperature (T-g) on first heating, i s measured at 176 and 174 degrees C, respectively, for hot-air-dried and na tive CGM. For zein and glutelin isolated fractions, the measured T-g values are 164 and 209 degrees C, respectively. The calculated T-g from using Mat veev's method (Matveev YI. Spec Publ R Soc Chem 1995;156;552) is in good ag reement with experimental data for zein, a well defined protein. MDSC allow s the measurement of change in heat capacity at T-g(Delta Cp) with a single heating scan, avoiding sample alteration, and Delta Cp values are 0.365 J/ g per K for zein and 0.184 J/g per K for glutelin. The differences observed in T-g, relaxation temperatures, Delta Cp and tan delta peak height are re lated to differences in the structure of the proteins, through the cross-li nkages and hydrogen or van der Weals interactions. Experimental data from D MTA and MDSC, and the Couchman-Karasz thermodynamic approach indicate that CGM behaves as a miscible blend of its components, with high non-polar inte ractions between zein and glutelin proteins. (C) 1999 Elsevier Science B.V. All rights reserved.