volume 560-561 pages 333-337

Kinetic Resolution of Ethyl-2-hydroxy-4-phenylbutyrate with Lipase AK as Catalyst

Zhi Min Ou 1
Ren Wei Li 1
Publication typeJournal Article
Publication date2012-08-24
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ISSN16628985, 10226680
General Engineering
Abstract

Ethyl (R)-2-hydroxy-4-phenylbutyrate was prepared by enzyme resolution of racemic ethyl- 2-hydroxy-4-phenylbutyrate. The optimal resolution conditions were 0.074 mol/L ethyl-2-hydroxy-4-phenylbutyrate, 20 mg lipase AK in 2.0 ml ethenylethanoate, 30 0C, 100 rpm. Enantiomeric excess of ethyl (R)-2-hydroxy-4-phenylbutyrate was up to 99%. Kinetic resolution model of ethyl- 2-hydroxy-4-phenylbutyrate by lipase AK was described by double substrate ping-pong mechanism. Model data agreed well with experimental data.

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Ou Z. M., Li R. W. Kinetic Resolution of Ethyl-2-hydroxy-4-phenylbutyrate with Lipase AK as Catalyst // Advanced Materials Research. 2012. Vol. 560-561. pp. 333-337.
GOST all authors (up to 50) Copy
Ou Z. M., Li R. W. Kinetic Resolution of Ethyl-2-hydroxy-4-phenylbutyrate with Lipase AK as Catalyst // Advanced Materials Research. 2012. Vol. 560-561. pp. 333-337.
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TY - JOUR
DO - 10.4028/www.scientific.net/amr.560-561.333
UR - https://doi.org/10.4028/www.scientific.net/amr.560-561.333
TI - Kinetic Resolution of Ethyl-2-hydroxy-4-phenylbutyrate with Lipase AK as Catalyst
T2 - Advanced Materials Research
AU - Ou, Zhi Min
AU - Li, Ren Wei
PY - 2012
DA - 2012/08/24
PB - Trans Tech Publications
SP - 333-337
VL - 560-561
SN - 1662-8985
SN - 1022-6680
ER -
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@article{2012_Ou,
author = {Zhi Min Ou and Ren Wei Li},
title = {Kinetic Resolution of Ethyl-2-hydroxy-4-phenylbutyrate with Lipase AK as Catalyst},
journal = {Advanced Materials Research},
year = {2012},
volume = {560-561},
publisher = {Trans Tech Publications},
month = {aug},
url = {https://doi.org/10.4028/www.scientific.net/amr.560-561.333},
pages = {333--337},
doi = {10.4028/www.scientific.net/amr.560-561.333}
}