Abstract:

Gliadin and glutenin were extracted from highland barley and wheat using the Osbron method, their
physicochemical properties including subunit compositions, secondary structure, surface hydrophobicity, thermal stability,
and active and total sulfydryl groups were measured. The results showed that gliadin content in highland barley protein was
16.96%, lower than that in wheat protein; glutenin content in highland barley protein was 47.83%, higher than that in wheat
protein; however, highland barley contained less high molecular weight glutenin subunit (HMW-GS) bands wheat. The total
sulfydryl and disulfide bond contents of gliadin and glutenin in highland barley were lower than those of wheat, respectively.
The hydrophobicity of gliadin and glutenin from highland barley and wheat showed a similarity. Highland barley glutenin
showed higher thermal stability compared with wheat glutenin. The secondary structure of gliadin and glutenin was studied
by circular dichroism, and β-pleated sheet was dominant in glutenin. The major secondary structures were β-pleated sheet
and β-sheet in gliadin while β-sheet content of highland barley gliadin was lower compared with wheat gliadin.

Key words: highland barley, gliadin, glutenin, gluten