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Thermodynamics of the Lipase Catalyzed Esterification of 1-Dodecanoic Acid and 1-Dodecanol in Organic Solvents

Published

Author(s)

Yadu D. Tewari

Abstract

Lipase immobilized on controlled-pore glass beads was used to catalyze the esterification of 1-dodecanol and 1-dodecanoic acid in organic solvents. Equilibrium measurements were performed in hexane, heptane, cyclohexane, 2,2,4-trimethylpentane, and toluene at the temperature T = 298.15 K. The equilibrium constants correlate well with the (octanol + water) partition coefficients and the dielectric constants of the solvents. The saturation molalities and the (2,2,4-trimethylpentane + water) partition coefficients of 1-dodecanol, 1-dodecanoic acid, and dodecanoic dodecanoate have been determined at T = 298.15 K. The equilibrium constant of the esterification reaction in water has also been calculated.
Citation
Journal of Chemical and Engineering Data
Volume
43
Issue
No. 5

Keywords

1-dodecanoic acid, 1-dodecanol, biocatalysis, equilibrium constant, esterification, lipase, n-dodecyldecanoate, organic solvents, thermodynamics

Citation

Tewari, Y. (1998), Thermodynamics of the Lipase Catalyzed Esterification of 1-Dodecanoic Acid and 1-Dodecanol in Organic Solvents, Journal of Chemical and Engineering Data (Accessed June 21, 2024)

Issues

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Created September 1, 1998, Updated February 17, 2017