Size as a parameter for solvent effects on Candida antarctica lipase B enantioselectivity
2002 (English)In: Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, ISSN 0167-4838, Vol. 1594, no 2, 325-334 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
2002. Vol. 1594, no 2, 325-334 p.
enantiomeric ratio; enthalpy; entropy; lipase; resolution
IdentifiersURN: urn:nbn:se:kth:diva-13382DOI: 10.1016/S0167-4838(01)00324-7ISI: 000174690100012OAI: oai:DiVA.org:kth-13382DiVA: diva2:324825
QC 201006162010-06-162010-06-162010-07-22Bibliographically approved