Characterization of gliadin, secalin and hordein fractions using analytical techniques.

ABSTRACT: Prolamins, alcohol soluble storage proteins of the Triticeae tribe of Gramineae family, are known as gliadin, secalin and hordein in wheat, rye and barley respectively. Prolamins were extracted from fifteen cultivars using DuPont protocol to study their physiochemical, morphological and structural characteristics. SDS-PAGE of prolamins showed well resolved low molecular weight proteins with significant amount of albumin and globulin as cross-contaminant. The β-sheet (32.72-37.41%) and β-turn (30.36-37.91%) were found higher in gliadins, while α-helix (20.32-28.95%) and random coil (9.05-10.28%) in hordeins. The high colloidal stability as depicted by zeta-potential was observed in gliadins (23.5-27.0 mV) followed secalins (11.2-16.6 mV) and hordeins (4.1-7.8 mV). Surface morphology by SEM

SUBMITTER: Rani M 

PROVIDER: S-EPMC8633357 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature