Abstract
The effects of two different modification methods (deamidation and succinylation) on the functional properties (solubility, water- and oil-binding capacity, foaming capacity and stability, emulsion activity and stability) of oat protein isolates were evaluated. Protein isolates extracted from defatted oat flour at alkaline pH were acylated by 0.20 g/g of succinic anhydride. The protein isolate was also modified using a mild acidic treatment (HCl, 0.5 N). Succinylation and deamidation improved solubility and emulsifying activity of the native protein isolate. Foaming capacity of oat protein isolate increased after deamidation, whereas succinylation decreased it. The deamidated and succinylated proteins had lower foam and emulsion stabilities than had their native counterpart. Water- and oil-binding capacity, in both modified oat proteins, was higher than those of the native oat protein isolate.
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