Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
Volume 1594, Issue 2, Pages 325-334Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0167-4838(01)00324-7
Keywords
enantiomeric ratio; enthalpy; entropy; lipase; resolution
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Changes in solvent type were shown to yield significant improvement of enzyme enantioselectivity. The resolution of 3-methyl-2-butanol catalyzed by Candida antarctica lipase B, CALB, was studied in eight liquid organic solvents and supercritical carbon dioxide, SCCO2. Studies of the temperature dependence of the enantiomeric ratio allowed determination of the enthalpic (Delta(R-S)Delta H-double dagger) as well as the entropic (Delta(R-S)Delta S-double dagger) contribution to the overall enantioselectivity (Delta(R-S)Delta G(double dagger) = -RTlnE). A correlation of the enantiomeric ratio, E. to the van der Waals volume of the solvent molecules was observed and suggested as one of the parameters that govern solvent effects on enzyme catalysis. An enthalpy-entropy compensation relationship was indicated between the studied liquid solvents. The enzymatic mechanism must be of a somewhat different nature in SCCO2, as this reaction in this medium did not follow the enthalpy-entropy compensation relation. (C) 2002 Elsevier Science B.V. All rights reserved.
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