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 April 23, 2024)
Official websites use .gov
A .gov website belongs to an official government organization in the United States.
Secure .gov websites use HTTPS
A lock (
) or https:// means you’ve safely connected to the .gov website. Share sensitive information only on official, secure websites.
Thermodynamics of the Lipase Catalyzed Esterification of 1-Dodecanoic Acid and 1-Dodecanol in Organic Solvents
Published
Author(s)
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
Pub Type
Journals
Keywords
1-dodecanoic acid, 1-dodecanol, biocatalysis, equilibrium constant, esterification, lipase, n-dodecyldecanoate, organic solvents, thermodynamics
Citation
Created September 1, 1998, Updated February 17, 2017