Partial molar volumes of l-serine and l-threonine in aqueous ammonium sulfate solutions at (278.15, 288.15, 298.15, and 308.15) K

In this study, the partial molar volumes of L-serine and L-threonine in aqueous solutions of ammonium sulfate at (0.0, 0.1, 0.3, 0.7, and 1.0) mol.kg(-1) are reported between 278.15 and 308.15 K. Transfer volumes and hydration numbers were obtained, which are larger in L-serine than in L-threonine. Dehydration of the amino acids is observed, rising with the temperature and salt molality. The data suggest that interactions between ions and charged/hydrophilic groups are predominant, and by applying the McMillan and Mayer formalism, it was concluded that they are mainly pair wise. The combination of the data presented in this study with solubility and molecular dynamics data suggests a stronger interaction of the ammonium cation with the zwitterionic centers of the amino acids when compared to the interactions of those centers with the sulfate anion.

Partial molar volumes of glycine and dl-alanine in aqueous ammonium sulfate solutions at 278.15, 288.15, 298.15 and 308.15 K

In this work, the partial molar volumes of glycine and DL-alanine in aqueous solutions of ammonium sulfate at 0.0, 0.1, 0.3, 0.7, and 1.0 mol.kg(-1) are determined between 278.15 and 308.15 K. Transfer volumes were obtained, which are larger for glycine than DL-alanine. On the contrary, the hydration numbers are higher for DL-alanine than glycine, and dehydration of the amino acids is observed with increasing temperature or salt molality. The data suggest that interactions between ion and charged/hydrophilic groups are predominant and, by applying the methodology proposed by Friedman and Krishnan, it was concluded that they are mainly pairwise. A group-contribution scheme has been successfully applied to the pairwise volumetric interaction coefficient. Finally, the dehydration effect on glycine, alanine and serine in the presence of different electrolytes has been rationalized in terms of the charge density and a parameter accounting for the cation's hydration.

Volumetric interactions of a series of α-amino acids in aqueous magnesium chloride solutions at 278.15, 288.15, 298.15, and 308.15 K

In this work, the partial molar volumes of glycine, l-alanine, l-valine, l-serine, and l-threonine in aqueous solutions of magnesium chloride at 0.0, 0.1, 0.3, 0.7, and 1.0 molal are addressed between 278.15 and 308.15 K. Volumes of transfer were obtained, following the rank serine > glycine a parts per thousand threonine > alanine > valine. Differently, the hydration numbers follow the sequence serine > valine > alanine > threonine > glycine, and dehydration of the amino acids is observed, rising the temperature or salt molality. The data suggest that interactions are mainly pairwise, between the ions and charged/hydrophilic groups of the amino acids. Within the Friedman and Krishnan formalism, a group-contribution scheme has been successfully applied to the pairwise volumetric interaction coefficient. Finally, the dehydration effect of MgCl2 on glycine, alanine, and serine has been predicted applying empirical correlations developed before, showing satisfactory results.