Mechanistic kinetic model for symmetric carboligations using benzaldehyde lyase
Research output: Contribution to journal › Research article › Contributed › peer-review
Contributors
Abstract
For reactions using thiamine diphosphate (ThDP)-dependent enzymes many empirically-derived kinetic models exist. However, there is a lack of mechanistic kinetic models. This is especially true for the synthesis of symmetric 2-hydroxy ketones from two identical aldehydes, with one substrate acting as the donor and the other as the acceptor. In this contribution, a systematic approach for deriving such a kinetic model for thiamine diphosphate (ThDP)-dependent enzymes is presented. The derived mechanistic kinetic model takes this donor–acceptor principle into account by containing two Km-values even for identical substrate molecules. As example the stereoselective carbon–carbon coupling of two 3,5-dimethoxy-benzaldehyde molecules to (R)-3,30,5,50-tetramethoxy-benzoin using benzaldehyde lyase (EC 4.1.2.38) from Pseudomonas fluorescens is studied. The model is derived using a model-based experimental analysis method which includes parameter estimation, model analysis, optimal experimental design, in silico experiments, sensitivity analysis and model revision. It is shown that this approach leads to a robust kinetic model with accurate parameter estimates and an excellent prediction capability.
Details
Original language | English |
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Pages (from-to) | 27-38 |
Journal | Biotechnology & bioengineering |
Volume | 2008 |
Issue number | 101 |
Publication status | Published - 2008 |
Peer-reviewed | Yes |
Externally published | Yes |
External IDs
Scopus | 50049102673 |
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ORCID | /0000-0002-2912-546X/work/171551986 |
Keywords
Keywords
- Biokatalyse, Benzaldehydlyase, BAL, Modellierung, Kinetik