Partial molar volumes of some alpha-amino acids in aqueous sodium acetate solutions at 308.15 K

The apparent molar volumes V-2,V-phi have been determined for glycine, DL-a lpha-alanine, DL-alpha-amino-n-butyric acid, DL-valine and DL-leucine in aq ueous solutions of 0.5, 1.0, 1.5 and 2.0 mol kg(-1) sodium acetate by densi ty measurements at 308.15 K. These data have been used to derive the infini te dilution apparent molar volumes V-2,phi(0) for the amino acids in aqueou s sodium acetate solutions and the standard volumes of transfer, Delta(t)V( 0), of the amino acids from water to aqueous sodium acetate solutions. It h as been observed that both V-2,phi(0) and Delta(t)V(0) vary linearly with i ncreasing number of carbon atoms in the alkyl chain of the amino acids. The se linear correlations have been utilized to estimate the contributions of the charged end groups (NH3+,COO-), CH2 group and other alkyl chains of the amino acids to V-2,phi(0) and Delta(t)V(0). The results show that V-2,phi( 0) values for (NH3+, COO-) groups increase with sodium amino acids to V-2,p hi(0) and Delta(t)V(0). The results show that V2,phi 0 values for (NH3+, CO O-) groups increase with sodium acetate concentration, and those for CH2 ar e almost constant over the studied sodium acetate concentration range. The transfer volume increases and the hydration number of the amino acids decre ased with increasing electrolyte concentrations. These facts indicate that strong interactions occur between the ions of sodium acetate and the charge d centers of the amino acids. The volumetric interaction parameters of the amino acids with sodium acetate were calculated in water. The pair interact ion parameters are found to be positive and decreased with increasing alkyl chain length of the amino acids, suggesting that sodium acetate has a stro nger dehydration effect on amino acids which have longer hydrophobic alkyl chains. These phenomena are discussed by means of the cosphere overlap mode l. (C) 1999 Elsevier Science B.V. All rights reserved.