The apparent molar volumes and viscosity of DL-alanine in aqueous solutions of sodium sulfate, Na2SO4, at different molalities and in the temperature range (283 to 308) K at each 5K were determined from density measurements and flow times, using a vibratory tube densimeter Anton Paar DMA 5000 and an automatic viscometer AMVn, respectively. From these data, the: limiting apparent molar volumes and limiting apparent volumes of transfer, hydration numbers, viscosity coefficients of the Jones-Dole equation, and thermodynamic activation parameters of the viscous flow were calculated. The results indicate that the amino acid behaves as a structure-forming solute on the structure of the solvent, followed by an increase in the overall structure of the water. It is concluded that the formation of the transition state is accompanied by the establishment of intermolecular bonds and a more orderly structure of the species in the activated state.