Abstract
Four fractions (100-, 50-, 20-K and permeate) from a proteolytic hydrolysate (DH=2.8%) of wheat gluten were separated using size fractionation on ultrafiltration membranes with molecular weight cut-offs of 100, 50 and 20 kDa and their functional properties evaluated. Proteolysis led to a significant ( P<0.05) increase in solubility of gluten fractions at pHs between 2–10 and a shift of the pI value from 6–7 to 5. The solubilities of 100-K, 50-K, 20-K and permeate fractions were significantly ( P<0.05) improved compared with the untreated control and the hydrolysate. The 50-K fraction was superior to other three fractions for emulsion activity index between pH 2 and 10. The most stable foam was given by the 100-K fraction which showed 65.8% of initial foam while the control sample gave only 23% of foam, after 60 min resting. Foam stability decreased as the molecular mass of hydrolysate fractions decreased. Furthermore, after proteolysis, the surface hydrophobicity ( H 0) of gluten increased significantly ( P<0.05) compared with the control except for the permeate fraction. The highest value of H 0 was given by the 100-K fraction, followed by the 50-K, 20-K and permeate fractions. In addition, proteolysis resulted in a decrease in the storage modulus of gels.
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