Lipase-catalyzed hydrolytic resolution of (R,S)-3-hydroxy-3-phenylpropionates in biphasic media

Shu Hhin Cho; Pei Yun Wang; Shau Wei Tsai

doi:10.1016/j.jtice.2010.09.005

Lipase-catalyzed hydrolytic resolution of (R,S)-3-hydroxy-3-phenylpropionates in biphasic media

Shu Hhin Cho, Pei Yun Wang, Shau Wei Tsai^*

^*Corresponding author for this work

Department of Chemical and Materials Engineering

Chang Gung University

Research output: Contribution to journal › Journal Article › peer-review

15 Scopus citations

Abstract

Lipase PS from Pseudomonas cepacia was screened as the best lipase for the hydrolytic resolution of (R,S)-ethyl 3-hydroxy-3-phenylpropionate in biphasic media. The optimal reaction conditions of using isooctane as the organic phase, aqueous pH 6, and methanol as the leaving moiety was then selected for improving the enantioselectivity in terms of V_S/V_R equal to 50.7. By considering the easy enzyme recovery and reduced background hydrolysis, Lipase PS covalently immobilized on Eupergi C 250L but not Sepabeads^@ EC-HA was further selected for giving V_S/V_R=53.6. Moreover, the kinetic analysis for each enzyme preparation was carried out and compared, showing the main effect of enzyme immobilization on decreasing the kinetic constants k_2R and k_2S.

Original language	English
Pages (from-to)	408-412
Number of pages	5
Journal	Journal of the Taiwan Institute of Chemical Engineers
Volume	42
Issue number	3
DOIs	https://doi.org/10.1016/j.jtice.2010.09.005
State	Published - 05 2011

Keywords

(R,S)-3-Hydroxy-3-phenylpropionates
Covalent immobilization
Hydrolytic resolution
Lipase PS

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10.1016/j.jtice.2010.09.005

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title = "Lipase-catalyzed hydrolytic resolution of (R,S)-3-hydroxy-3-phenylpropionates in biphasic media",

abstract = "Lipase PS from Pseudomonas cepacia was screened as the best lipase for the hydrolytic resolution of (R,S)-ethyl 3-hydroxy-3-phenylpropionate in biphasic media. The optimal reaction conditions of using isooctane as the organic phase, aqueous pH 6, and methanol as the leaving moiety was then selected for improving the enantioselectivity in terms of VS/VR equal to 50.7. By considering the easy enzyme recovery and reduced background hydrolysis, Lipase PS covalently immobilized on Eupergi C 250L but not Sepabeads@ EC-HA was further selected for giving VS/VR=53.6. Moreover, the kinetic analysis for each enzyme preparation was carried out and compared, showing the main effect of enzyme immobilization on decreasing the kinetic constants k2R and k2S.",

keywords = "(R,S)-3-Hydroxy-3-phenylpropionates, Covalent immobilization, Hydrolytic resolution, Lipase PS",

author = "Cho, {Shu Hhin} and Wang, {Pei Yun} and Tsai, {Shau Wei}",

year = "2011",

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T1 - Lipase-catalyzed hydrolytic resolution of (R,S)-3-hydroxy-3-phenylpropionates in biphasic media

AU - Cho, Shu Hhin

AU - Wang, Pei Yun

AU - Tsai, Shau Wei

PY - 2011/5

Y1 - 2011/5

N2 - Lipase PS from Pseudomonas cepacia was screened as the best lipase for the hydrolytic resolution of (R,S)-ethyl 3-hydroxy-3-phenylpropionate in biphasic media. The optimal reaction conditions of using isooctane as the organic phase, aqueous pH 6, and methanol as the leaving moiety was then selected for improving the enantioselectivity in terms of VS/VR equal to 50.7. By considering the easy enzyme recovery and reduced background hydrolysis, Lipase PS covalently immobilized on Eupergi C 250L but not Sepabeads@ EC-HA was further selected for giving VS/VR=53.6. Moreover, the kinetic analysis for each enzyme preparation was carried out and compared, showing the main effect of enzyme immobilization on decreasing the kinetic constants k2R and k2S.

AB - Lipase PS from Pseudomonas cepacia was screened as the best lipase for the hydrolytic resolution of (R,S)-ethyl 3-hydroxy-3-phenylpropionate in biphasic media. The optimal reaction conditions of using isooctane as the organic phase, aqueous pH 6, and methanol as the leaving moiety was then selected for improving the enantioselectivity in terms of VS/VR equal to 50.7. By considering the easy enzyme recovery and reduced background hydrolysis, Lipase PS covalently immobilized on Eupergi C 250L but not Sepabeads@ EC-HA was further selected for giving VS/VR=53.6. Moreover, the kinetic analysis for each enzyme preparation was carried out and compared, showing the main effect of enzyme immobilization on decreasing the kinetic constants k2R and k2S.

KW - (R,S)-3-Hydroxy-3-phenylpropionates

KW - Covalent immobilization

KW - Hydrolytic resolution

KW - Lipase PS

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U2 - 10.1016/j.jtice.2010.09.005

DO - 10.1016/j.jtice.2010.09.005

M3 - 文章

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SN - 1876-1070

VL - 42

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JO - Journal of the Taiwan Institute of Chemical Engineers

JF - Journal of the Taiwan Institute of Chemical Engineers

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ER -

Lipase-catalyzed hydrolytic resolution of (R,S)-3-hydroxy-3-phenylpropionates in biphasic media

Abstract

Keywords

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