Conformational modifications of alpha gliadin and globulin proteins upon complex coacervates formation with gum Arabic as studied by Raman microspectroscopy.

As a molecular model of gelatin-free coacervates, complexes of pea globulin and alpha gliadin proteins with gum arabic prepared at different acidic pH values are studied using Raman microspectrometry. Raman spectra confirm higher content of beta-sheets and random coils in pea globulin and dominating alpha-helical structures in alpha gliadin. For protein-gum arabic complexes, Raman data support the existence of specific pH conditions for optimal complex coacervation (pH 2.