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.
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