The thermodynamic equilibrium of the aminotransferase reaction from L-alanine and 2-oxoglutarate to L-glutamate and pyruvate in aqueous solution was investigated in a temperature range between 25 and 37 degrees C and pH between at 5 and 9. Prior to considering the reaction equilibria, measurements were carried out to ensure the enzyme activity in the aqueous reaction media. After that, equilibrium concentrations of reacting agents were measured by HPLC-analysis. At constant temperature and pH, reaction equilibrium was shown to depend on the absolute molalities (0.005-0130 mol kg(-1)) as well as on the ratio of initial molalities of the reactants. It could be concluded that reaction equilibrium was shifted towards the product site upon increasing reactant molalities, increasing temperature, and increasing pH. Further, yields of pyruvate were increased upon excess initial molality of L-alanine compared to 2-oxoglutarate. The thermodynamic equilibrium constant K-a center dot was determined by extrapolating the ratio of product equilibrium molalites and reactant equilibrium molalites to infinite dilution of all reacting agents. The activity-coefficient ratio of products and reactants in the reaction media was predicted with ePC-SAFT. Combining K-a center dot and the activity-coefficient ratio allowed quantitatively predicting the influence of temperature, pH, and reacting-agent molalities on the reaction equilibrium. (C) 2016 Elsevier B.V. All rights reserved.