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Solvent effects on biocatalysis in organic systems: Equilibrium position and rates of lipase catalyzed esterification
Author(s) -
Valivety Rao H.,
Johnston Grant A.,
Suckling Colin J.,
Halling Peter J.
Publication year - 1991
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260381004
Subject(s) - chemistry , catalysis , partition coefficient , solvent , organic chemistry , solvation , lipase , biocatalysis , solvent effects , octanol , solubility , activity coefficient , aqueous solution , reaction mechanism , enzyme
Porcine pancreatic lipase immobilized on celite particles has been employed as a catalyst for the esterification of dodecanol and decanoic acid in a predominantly organic system. Solvent influence on the equilibrium position and on the catalyst activity has been studied using 20 solvents, including aliphatic and aromatic hydrocarbons, ethers, ketones, nitro‐ and halogenated hydrocarbons, and esters. The equilibrium constant for esterification correlates well with the solubility of water in the organic solvent, which in turn shows a good relationship with a function of Guttman's donor number and the electron pair acceptance index number of the solvent. This may be rationalized in terms of the requirements for solvation of water and of the reactants. The catalyst activity, measured as the initial rate of the esterification reaction, is best correlated as a function of both n ‐octanol‐water partition coefficient (log P ) and either the electron pair acceptance index or the polarizability.