Epoxide hydrolase activity of Chryseomonas luteola for the asymmetric hydrolysis of aliphatic mono-substituted epoxides
Asymmetric hydrolysis of a homologous range of straight chain 1,2-epoxyalkanes was achieved using whole cells of Chryseomonas luteola. Depending on the chain length, hydrolyses of the racemic epoxides afforded optically active epoxides and diols with varying degrees of optical purity. In the case of...
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| Veröffentlicht in: | Biotechnology letters 1998-04, Vol.20 (4), p.427-430 |
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| container_title | Biotechnology letters |
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| creator | BOTES, A. L STEENKAMP, J. A LETLOENYANE, M. Z VAN DYK, M. S |
| description | Asymmetric hydrolysis of a homologous range of straight chain 1,2-epoxyalkanes was achieved using whole cells of Chryseomonas luteola. Depending on the chain length, hydrolyses of the racemic epoxides afforded optically active epoxides and diols with varying degrees of optical purity. In the case of 1,2-epoxyoctane, the enantiomeric excess of the remaining (S)-epoxide and formed (R)-diol was excellent (ees > 98% and eep = 86%). This is the first report of a bacterial epoxide hydrolase with such unusual enantioselectivity for terminal mono-substituted epoxides bearing no directing group on the chiral C-2 carbon. Benzyl glycidyl ether and the 2,2-disubstituted epoxide, 2-methyl-1,2-epoxyheptane, were hydrolysed, but no enantioselectivity was observed. © Rapid Science Ltd. 1998[PUBLICATION ABSTRACT] |
| doi_str_mv | 10.1023/A:1005347901809 |
| format | Article |
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L ; STEENKAMP, J. A ; LETLOENYANE, M. Z ; VAN DYK, M. S</creator><creatorcontrib>BOTES, A. L ; STEENKAMP, J. A ; LETLOENYANE, M. Z ; VAN DYK, M. S</creatorcontrib><description>Asymmetric hydrolysis of a homologous range of straight chain 1,2-epoxyalkanes was achieved using whole cells of Chryseomonas luteola. Depending on the chain length, hydrolyses of the racemic epoxides afforded optically active epoxides and diols with varying degrees of optical purity. In the case of 1,2-epoxyoctane, the enantiomeric excess of the remaining (S)-epoxide and formed (R)-diol was excellent (ees > 98% and eep = 86%). This is the first report of a bacterial epoxide hydrolase with such unusual enantioselectivity for terminal mono-substituted epoxides bearing no directing group on the chiral C-2 carbon. 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| ispartof | Biotechnology letters, 1998-04, Vol.20 (4), p.427-430 |
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| source | SpringerNature Journals |
| subjects | Bioconversions. Hemisynthesis Biological and medical sciences Biotechnology Chryseomonas luteola Enzymes Fundamental and applied biological sciences. Psychology Hydrolysis Methods. Procedures. Technologies |
| title | Epoxide hydrolase activity of Chryseomonas luteola for the asymmetric hydrolysis of aliphatic mono-substituted epoxides |
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