Abstract
A protein concentrate (75.2%) was obtained from some Lens culinaris L. seeds. The osmotic, hydrodynamic and surface properties of protein concentrate aqueous solutions were studied with the help of membrane osmometry, dynamic light scattering, ζ-potential and the pendant drop method, in a wide range of protein concentrate concentrations and pH conditions. The second virial coefficient was determined in the range of pH 2–9. Two theta points (pH∼ 5 and pH∼ 8) were found. The change of the hydrodynamic radii as a function of pH and scattering vector was analysed. It was found that the change of the solvent parameters (pH) has a significant influence on the surface tension value. This phenomenon was related to the values of the second virial coefficient and the translational diffusion coefficient. The increase in the value of the diffusion coefficient (smaller hydrodynamic radius) resulted in faster interface formation at the gas–liquid interface.
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