Sequential kinetic resolution by two enantioselective enzymes

J.L.L. Rakels, Anders Wolff, A.J.J. Straathof, J.J. Heijnen

Research output: Contribution to journalJournal articleResearchpeer-review

1 Downloads (Pure)

Abstract

Enhancement of the enantioselectivity by simultaneous use of two enzymes in a sequential kinetic resolution process is presented. The model system consisted of carboxylesterase NP catalyzed hydrolysis of racemic methyl 2-chloropropionate, followed by dehalogenation of the enantiomerically enriched 2-chloropropionate by DL-dehalogenase into lactate. Optimal results are shown to be attained when the conversion rates of both faster reacting enantiomers are the same. An optimization parameter D for sequential resolutions is introduced. The kinetics of both reaction steps were investigated separately by progress curve analysis, and the enantioselectivity of the enzymes was determined. From a quantitative kinetic model we could formulate the sequential resolution, which yielded the predicted improvements of product enantiomeric excess.
Original languageEnglish
JournalBiocatalysis
Volume9
Issue number1-4
Pages (from-to)31-47
Publication statusPublished - 1994
Externally publishedYes

Fingerprint Dive into the research topics of 'Sequential kinetic resolution by two enantioselective enzymes'. Together they form a unique fingerprint.

Cite this