Comparative evaluation of gliadins from four extraction protocols using advanced analytical techniques.

Gliadin, a major component of gluten, is known to trigger celiac disease; therefore, its extraction is important to study its properties as well as its presence in gluten-free products. Four gliadin extraction procedures Osborne (1924), Weiss (1993), Wallace (1989) and DuPont (2005), were investigated on six wheat cultivars using advanced analytical techniques such as dynamic light scattering (DLS), X-ray diffraction (XRD), scanning electron microscopy (SEM) and transmission electron microscopy (TEM). Higher zeta potential of extracted gliadin was observed in DuPont (23.53-27), followed by Weiss (16.17-20.80), Osborne (16.17-20.13), and Wallace (14.60-19.47). Particle Z-average size (15.74-184.83 nm) was found to have an inverse relationship with the Polydispersity index (0.17-184.83). The surface morphological structure of TEM studies revealed the compact globular particle arrangement of gliadin, besides rod-shaped arrangement, was also found in DuPont and Wallace extracted gliadin. XRD pattern of gliadin exposed the crystalline domain at 44.1°, 37.8°, and 10.4° diffraction peaks. The d-spacing obtained from XRD and TEM-SAED analysis supports the presence of crystalline domains in gliadin apart from the amorphous domain. The insight obtained from this work will provide a better understanding of morphology and other properties of the same protein extracted with different extraction procedures.