| Kinetic analysis of enzymatic chiral resolution by progress curve evaluation. | |
| | |
MedLine Citation:
|
PMID: 18615724 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
|
The present study deals with kinetic modeling of enzyme-catalyzed reactions by integral progress curve analysis, and shows how to apply this technique to kinetic resolution of enantiomers. It is shown that kinetic parameters for both enantiomers and the enantioselectivity of the enzyme may be obtained from the progress curve measurement of a racemate only.A parameter estimation procedure has been established and it is shown that the covariance matrix of the obtained parameters is a useful statistical tool in the selection and verification of the model structure. Standard deviations calculated from this matrix have shown that progress curve analysis yields parameter values with high accuracies.Potential sources of systematic errors in (multiple) progress curve analysis are addressed in this article. Amongst these, the following needed to be dealt with: (1) the true initial substrate concentrations were obtained from the final amount of product experimentally measured (mass balancing); (2) systematic errors in the initial enzyme concentration were corrected by incorporating this variable in the fitting procedure as an extra parameter per curve; and (3) enzyme inactivation is included in the model and a first-order inactivation constant is determined.Experimental verification was carried out by continuous monitoring of the hydrolysis of ethyl 2-chloropropionate by carboxylesterase NP and the alpha-chymotrypsin-catalyzed hydrolysis of benzoylalanine mathyl ester in a pH-stat system. Kinetic parameter values were obtained with high accuracies and model predictions were in good agreement with independent measurements of enantiomeric excess values or literature data. (c) 1994 John Wiley & Sons, Inc. |
| | |
Authors:
|
J L Rakels; B Romein; A J Straathof; J J Heijnen |
Related Documents
:
|
16214864 - Simulation study of the contribution of oligomer/oligomer binding to capsid assembly ki... 21310854 - Eliciting benefit-risk preferences and probability-weighted utility using choice-format... 18486964 - Efficient removal of triphenylmethane dyes from aqueous medium by in situ electrogenera... 21171784 - Assessing the basic traits associated with psychopathy: development and validation of t... 8269294 - Complexities of junctional tachycardias. 16492094 - Stress exposure and stress generation in child and adolescent depression: a latent trai... |
Publication Detail:
|
Type: Journal Article |
Journal Detail:
|
Title: Biotechnology and bioengineering Volume: 43 ISSN: 0006-3592 ISO Abbreviation: Biotechnol. Bioeng. Publication Date: 1994 Mar |
Date Detail:
|
Created Date: 2008-07-10 Completed Date: - Revised Date: - |
Medline Journal Info:
|
Nlm Unique ID: 7502021 Medline TA: Biotechnol Bioeng Country: United States |
Other Details:
|
Languages: eng Pagination: 411-22 Citation Subset: - |
Affiliation:
|
Department of Biochemical Engineering, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
|
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Structured model of genetic control via the lac promoter in Escherichia coli.
Next Document: Glycosidase activities of the 293 and NS0 cell lines, and of an antibody-producing hybridoma cell li...