SummaryThermodynamic properties of aqueous solutions of both native and modified legumin of broad beans (Viciufuba L.) have been examined. A restricted trypsin-induced proteolysis was used to modify protein structure. Evaluation of protein affinity to ficoll in aqueous solutions showed that modified protein possessed higher hydrophilicity. Thermodynamic properties of diluted solutions were used to predict the phase behaviour in concentrated systems containing protein and ficoll. At specific concentrations of native legumin, the system can separate in two phases, whereas in the case of modified protein the single-phase behaviour of the system was predicted for any concentrations of both components. The experimental data obtained in concentrated systems confirmed predictions of thermodynamic analysis of diluted solutions.
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