The modifications of gliadins secondary structures during the film-formatio
n process have been studied by Fourier Transform Infrared spectroscopy. The
conformation of proteins in film-forming solutions (in alkaline conditions
) presented two major components : p-turns and Random Coil. In the film sta
te, hydrogen-bonded a-sheets were present. it has been demonstrated that th
e presence of the plasticizer did not influence the protein secondary struc
ture, neither in film-forming solution nor in the film state.
The second part of this work concerned the study of films from highly purif
ied wheat gluten proteins. Though these films presented very different mech
anical properties (depending on the primary structure of each protein), the
secondary structures of the proteins were very similar (same characteristi
c bands in the infrared spectra).