Thermodynamics of enzyme-catalyzed esterifications: I. Succinic acid esterification with ethanol

Abstract

Succinic acid (SA) was esterified with ethanol using Candida antarctica lipase B immobilized on acrylic resin at 40 and 50 °C. Enzyme activity in the reaction medium was assured prior to reaction experiments. Reaction-equilibrium experiments were performed for varying initial molalities of SA and water in the reaction mixtures. This allowed calculating the molality-based apparent equilibrium constant K _m as function of concentration and temperature. K _m was shown to depend strongly on the molality of water and SA as well as on temperature. It could be concluded that increasing the molality of SA shifted the reaction equilibrium towards the products. Water had a strong effect on the activity of the enzyme and on K _m . The concentration dependence of K _m values was explained by the activity coefficients of the reacting agents. These were predicted with the thermodynamic models Perturbed-Chain Statistical Associating Fluid Theory (PC-SAFT), NRTL, and Universal Quasichemical Functional Group Activity Coefficients (UNIFAC), yielding the ratio of activity coefficients of products and reactants K _γ . All model parameters were taken from literature. The models yielded K _γ values between 25 and 115. Thus, activity coefficients have a huge impact on the consistent determination of the thermodynamic equilibrium constants K _th. Combining K _m and PC-SAFT-predicted K _γ allowed determining K _th and the standard Gibbs energy of reaction as function of temperature. This value was shown to be in very good agreement with results obtained from group contribution methods for Gibbs energy of formation. In contrast, inconsistencies were observed for K _th using K _γ values from the classical g^E-models UNIFAC and NRTL. The importance of activity coefficients opens the door for an optimized reaction setup for enzymatic esterifications.

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