Details
| Original language | English |
|---|---|
| Pages (from-to) | 87-92 |
| Number of pages | 6 |
| Journal | Journal of biotechnology |
| Volume | 152 |
| Issue number | 3 |
| Early online date | 3 Feb 2011 |
| Publication status | Published - 20 Mar 2011 |
| Externally published | Yes |
Abstract
Benzoylformate decarboxylase (BFD, EC 4.1.1.7) is a homotetrameric thiamine diphosphate (ThDP)-dependent enzyme which catalyzes the synthesis of chiral 2-hydroxyketones accepting a broad range of aldehydes as substrates. In this study the synthesis of 2-hydroxypropiophenone (2-HPP) from benzaldehyde and acetaldehyde was catalyzed by three BFD variants namely BFD F464I, BFD A460I and BFD A460I-F464I. This paper reports the effect of hydrostatic pressure up to 290. MPa when the reactions were carried out at different benzaldehyde concentrations (5-40. mM) as well as at different pH values (7.0-8.5). Acetaldehyde concentration was fixed at 400. mM in all biotransformations. Reactions performed at high benzaldehyde concentrations and at high hydrostatic pressures showed an increase in (R)-2-HPP formation catalyzed by all BFD variants. For BFD A460I-F464I we observed an increase in the ee of (R)-2-HPP up to 80%, whereas at atmospheric conditions this variant synthesizes (R)-2-HPP with an ee of only 50%. Alkaline conditions (up to pH 8.5) and high hydrostatic pressures resulted in an increase of (R)-2-HPP synthesis, especially in the case of BFD A460I and BFD F464I.
Keywords
- Benzoylformate decarboxylase, C-C bond formation, Enantioselectivity, Enzymatic catalysis, High pressure catalysis, PH
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biotechnology
- Chemical Engineering(all)
- Bioengineering
- Immunology and Microbiology(all)
- Applied Microbiology and Biotechnology
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In: Journal of biotechnology, Vol. 152, No. 3, 20.03.2011, p. 87-92.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Influence of reaction conditions on the enantioselectivity of biocatalyzed C-C bond formations under high pressure conditions
AU - Kara, Selin
AU - Long, Wei Sing
AU - Berheide, Marco
AU - Peper, Stephanie
AU - Niemeyer, Bernd
AU - Liese, Andreas
N1 - Funding Information: We thank the Deutsche Forschungsgemeinschaft DFG for the financial support of the project. Special thanks to Prof. Dr. Martina Pohl (Institute of Molecular Enzyme Technology, Heinrich-Heine University of Düsseldorf, Research Center Jülich) for generously providing the wild type BFD and the variants and to Dr. Lutz Hilterhaus (Institute of Technical Biocatalysis, Hamburg University of Technology) for his fruitful discussions and his helpful comments on this manuscript. The skillful technical assistance of Maximilia Kottwitz is gratefully acknowledged.
PY - 2011/3/20
Y1 - 2011/3/20
N2 - Benzoylformate decarboxylase (BFD, EC 4.1.1.7) is a homotetrameric thiamine diphosphate (ThDP)-dependent enzyme which catalyzes the synthesis of chiral 2-hydroxyketones accepting a broad range of aldehydes as substrates. In this study the synthesis of 2-hydroxypropiophenone (2-HPP) from benzaldehyde and acetaldehyde was catalyzed by three BFD variants namely BFD F464I, BFD A460I and BFD A460I-F464I. This paper reports the effect of hydrostatic pressure up to 290. MPa when the reactions were carried out at different benzaldehyde concentrations (5-40. mM) as well as at different pH values (7.0-8.5). Acetaldehyde concentration was fixed at 400. mM in all biotransformations. Reactions performed at high benzaldehyde concentrations and at high hydrostatic pressures showed an increase in (R)-2-HPP formation catalyzed by all BFD variants. For BFD A460I-F464I we observed an increase in the ee of (R)-2-HPP up to 80%, whereas at atmospheric conditions this variant synthesizes (R)-2-HPP with an ee of only 50%. Alkaline conditions (up to pH 8.5) and high hydrostatic pressures resulted in an increase of (R)-2-HPP synthesis, especially in the case of BFD A460I and BFD F464I.
AB - Benzoylformate decarboxylase (BFD, EC 4.1.1.7) is a homotetrameric thiamine diphosphate (ThDP)-dependent enzyme which catalyzes the synthesis of chiral 2-hydroxyketones accepting a broad range of aldehydes as substrates. In this study the synthesis of 2-hydroxypropiophenone (2-HPP) from benzaldehyde and acetaldehyde was catalyzed by three BFD variants namely BFD F464I, BFD A460I and BFD A460I-F464I. This paper reports the effect of hydrostatic pressure up to 290. MPa when the reactions were carried out at different benzaldehyde concentrations (5-40. mM) as well as at different pH values (7.0-8.5). Acetaldehyde concentration was fixed at 400. mM in all biotransformations. Reactions performed at high benzaldehyde concentrations and at high hydrostatic pressures showed an increase in (R)-2-HPP formation catalyzed by all BFD variants. For BFD A460I-F464I we observed an increase in the ee of (R)-2-HPP up to 80%, whereas at atmospheric conditions this variant synthesizes (R)-2-HPP with an ee of only 50%. Alkaline conditions (up to pH 8.5) and high hydrostatic pressures resulted in an increase of (R)-2-HPP synthesis, especially in the case of BFD A460I and BFD F464I.
KW - Benzoylformate decarboxylase
KW - C-C bond formation
KW - Enantioselectivity
KW - Enzymatic catalysis
KW - High pressure catalysis
KW - PH
UR - http://www.scopus.com/inward/record.url?scp=79952899156&partnerID=8YFLogxK
U2 - Fkara10.1016/j.jbiotec.2011.01.020
DO - Fkara10.1016/j.jbiotec.2011.01.020
M3 - Article
C2 - 21295624
AN - SCOPUS:79952899156
VL - 152
SP - 87
EP - 92
JO - Journal of biotechnology
JF - Journal of biotechnology
SN - 0168-1656
IS - 3
ER -