Salt effects on the solubility of aromatic and dicarboxylic amino acids in water

The salt effect on the solubility of the amino acids L-aspartic acid, L-glutamic acid, L-tryptophan, and L-tyrosine, seldomly found in the literature, was studied at 298.2 K, in aqueous solutions of KCl and (NH4)(2)SO4, for salt concentrations up to 2.0 mol.kg(-1). In this concentration range, both salts are salting-in agents for glutamic acid and aspartic acid, with a stronger effect induced by (NH4)(2)SO4. Regarding the two aromatic amino acids, a slight increase in the solubility was obtained at low salt concentrations, followed by a stronger salting-out effect, more pronounced by (NH4)(2)SO4 than by KCl. The relative solubility data obtained in this work were compared to literature data for other amino acids in the same electrolyte solutions to establish a relative solubility ranking connected to their structure. Finally, the solubility data were modeled using the electrolyte Perturbed-Chain Statistical Association Theory (ePC-SAFT). The modeling requires parameters for the amino acids and ions as well as melting properties of the amino acids. All these parameters and properties were obtained from previous works. To quantitatively describe the solubility of amino acids upon salt addition, binary interaction parameters (k(ij)) between any amino acid and anions were determined, while between any amino acid and the cations were fixed to k(ij) = 0.08. The k(ij) parameters between amino acid and the inorganic anions show very similar values for amino acids of the same chemical class (e.g. k(ij) between anion and amino acid with apolar side chains), which may be used to systematically reduce the number of adjustable parameters in future work.