earticle

영어

Barley proteins are expected to have unique functional properties due to their high content of alcohol solubleprotein, hordein. Since the barley proteins obtained by conventional isoelectric precipitation method cannot represent hordeinfraction, barley proteins were fractionated to albumin, globulin, glutelin, and hordein with respect to extraction solvents.Functional properties and film-forming properties of solubility-fractionated barley proteins were investigated to explore theirpotential for human food ingredient and industrial usage. The 100g of total barley protein comprised 5g albumin, 23gglobulin, 45g glutelin, and 27g hordein. Water-binding capacities of barley protein isolates ranged from 140-183mL water/100g solid. Hordein showed the highest oil absorption capacity (136mL oil/100g), and glutelin showed the highest gelationproperty among the fractionated proteins. In general, the barley protein fractions formed brittle and weak films as indicated bylow tensile strength (TS) and percent elongation at break (E) values. The salt-soluble globulin fraction produced film with thelowest TS value. Although films made from glutelin and hordein were dark-colored and had lower E values, they could beused as excellent barriers against water transmission.