Determination and Analysis of Composition, Structure, and Properties of Teff Protein Fractions

Abstract

To develop teff-based food products with acceptable quality, the composition, structure, and properties of teff protein fractions should be better understood. In this study, teff proteins were extracted, and their protein composition, structure, and properties were calculated, analyzed, and compared with those of wheat gliadin and glutenin. Results showed that teff flour contained 9.07% protein, with prolamin as its main protein fraction. The isoelectric points of albumin, globulin, prolamin, and glutelin were at pH 3.6, 3.0, 4.4, and 3.4, respectively. Teff prolamin and glutelin showed a significant difference in amino acids and free energy of hydration compared to wheat gliadins and glutenins. The protein chain length of teff prolamins was smaller than that of wheat gliadins, and teff glutelins lacked high molecular weight glutelin subunits. Teff prolamin had the highest α-helices content (27.08%), whereas no random coils were determined, which is different from wheat gliadin. Teff glutelin had a lower content of β-turn than wheat glutenin, and no α-helices were determined in it. Teff prolamin and glutelin had lower disulfide bond content and surface hydrophobicity. Teff prolamin had significantly higher thermal stability than wheat gliadin, whereas the thermal stability of teff glutelin was significantly lower than that of wheat glutenin.