Abstract
The effect of enzymatic hydrolysis on structure characteristics (surface aromatic hydrophobicity and molecular size) of both native and modified soy protein isolates was studied. Effects on thermal behavior and functional properties (solubility and foam formation and stabilization at pH 4.5) were also analysed. Hydrolysates were obtained by bromelain digestion at pH 8 of native (N) and of thermally treated isolates at pH 7 (T7) and at pH 1.6 (T1.6). The differential effect of bromelain on the three isolates produced partially hydrolyzed structures, which exhibited an enhancement of their protein solubility ( S TCA and S pH 4.5). Bromelain digestion was more effective on isolate T7 resulting hydrolysates with improved capacity to form foams at pH 4.5. The different functional behavior at pH 4.5 of hydrolysates was explained through the changes in thermal behavior, surface aromatic hydrophobicity and molecular mass distribution.
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