Effect of temperature on partial molar volumes and viscosities of aqueous solutions of α-<scp>dl</scp>-Aminobutyric acid,<scp>dl</scp>-Norvaline and<scp>dl</scp>-Norleucine

In this work, we present experimental results for partial molar volumes and viscosities of aqueous solutions of α-dl-aminobutyric acid, dl-norvaline and dl-norleucine at 288.15, 293.15, 298.15 and 303.15 K. The thermodynamic behavior of aqueous amino acid solutions is compared with that reported for glycine and α-alanine in water and is discussed in terms of group additivity and electrostriction. The temperature dependence of the infinite dilution partial molar volumes and the B viscosity coefficients are interpreted in terms of amino acid hydration. According to the usual hydrophobicity criteria, the amino acids considered do not have a hydrophobic character and their behavior is dominated by the polar groups.