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Immobilised lipase-catalysed resolution of (R,S)-1-phenylethanol in recirculated packed bed reactor

Six commercial immobolised lipase were screened for the resolution of (R,S)-1-phenylethanol in organic solvent. Among them, lipases for Pseudomonas cepacia (ChiroCLEC-PC) and Candida antartica lipase B (Chirazyme L2, c.-f.,C3, lyo) were used in the kinetics study of the resolution in batch stirred t...

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Main Authors: Chua, Lee Suan, Sarmidi, Mohamad Roji
格式: Article
出版: Elsevier 2004
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T Technology (General)
在線閱讀:http://eprints.utm.my/id/eprint/6305/
http://dx.doi.org/10.1016/j.molcatb.2004.02.004
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spelling my.utm.63052017-03-09T03:42:59Z http://eprints.utm.my/id/eprint/6305/ Immobilised lipase-catalysed resolution of (R,S)-1-phenylethanol in recirculated packed bed reactor Chua, Lee Suan Sarmidi, Mohamad Roji T Technology (General) Six commercial immobolised lipase were screened for the resolution of (R,S)-1-phenylethanol in organic solvent. Among them, lipases for Pseudomonas cepacia (ChiroCLEC-PC) and Candida antartica lipase B (Chirazyme L2, c.-f.,C3, lyo) were used in the kinetics study of the resolution in batch stirred tank reactor (BSTR). Lauric acid was used as acyl donor in the acyl transfer reaction. This enzymatic resolution was carried out at 35C in isooctane. The enzyme activity as well as enantioselectivity was determined by varying substrates concentration from 25mM to 250mM, acyl length of fatty acid from C12 to C18, organic solvents with log P values from 1.4 to 4.5 and reaction temperature from 25 to 50C. An initial reaction velocity approach was used to determine the enzyme activities and a computer software, SELECTIVITY was used to calculate the enzyme enantioselectivity. The activity of ChiroCLEC-PC and Chirazyme L2, c.-f.,C3,lyo are 1.4 kU/g and 1.0 U/g, respectively. The enzymes are highly selective toward (R)-enantiomer of the chiral alcohol with the enantiomeric ratio, E>200. A series of reaction progress curves was used to develop a kinetic model based on the principle of mass action law with steady-state assumption. The reaction follows a Ping-Pong Bi-Bi mechanism with substrate inhibition. The performance of Chirazyme L2,c.-f.,C3,lyo in the resolution was also investigated in recirculated packed bed reactor (RPBR). The enzyme performance in term of initial rate was decreased 19% after 30 min or reaction time. The resolution was also required 350 min longer reaction time in order to achieve equilibrium. A comparable result could be obtained in five-fold scaling up RPBR. Elsevier 2004 Article PeerReviewed Chua, Lee Suan and Sarmidi, Mohamad Roji (2004) Immobilised lipase-catalysed resolution of (R,S)-1-phenylethanol in recirculated packed bed reactor. Journal of Molecular Catalysis B: Enzymatic, 28 . pp. 111-119. ISSN 1381-1177 http://dx.doi.org/10.1016/j.molcatb.2004.02.004
institution Universiti Teknologi Malaysia
building UTM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Teknologi Malaysia
content_source UTM Institutional Repository
url_provider http://eprints.utm.my/
topic T Technology (General)
spellingShingle T Technology (General)
Chua, Lee Suan
Sarmidi, Mohamad Roji
Immobilised lipase-catalysed resolution of (R,S)-1-phenylethanol in recirculated packed bed reactor
description Six commercial immobolised lipase were screened for the resolution of (R,S)-1-phenylethanol in organic solvent. Among them, lipases for Pseudomonas cepacia (ChiroCLEC-PC) and Candida antartica lipase B (Chirazyme L2, c.-f.,C3, lyo) were used in the kinetics study of the resolution in batch stirred tank reactor (BSTR). Lauric acid was used as acyl donor in the acyl transfer reaction. This enzymatic resolution was carried out at 35C in isooctane. The enzyme activity as well as enantioselectivity was determined by varying substrates concentration from 25mM to 250mM, acyl length of fatty acid from C12 to C18, organic solvents with log P values from 1.4 to 4.5 and reaction temperature from 25 to 50C. An initial reaction velocity approach was used to determine the enzyme activities and a computer software, SELECTIVITY was used to calculate the enzyme enantioselectivity. The activity of ChiroCLEC-PC and Chirazyme L2, c.-f.,C3,lyo are 1.4 kU/g and 1.0 U/g, respectively. The enzymes are highly selective toward (R)-enantiomer of the chiral alcohol with the enantiomeric ratio, E>200. A series of reaction progress curves was used to develop a kinetic model based on the principle of mass action law with steady-state assumption. The reaction follows a Ping-Pong Bi-Bi mechanism with substrate inhibition. The performance of Chirazyme L2,c.-f.,C3,lyo in the resolution was also investigated in recirculated packed bed reactor (RPBR). The enzyme performance in term of initial rate was decreased 19% after 30 min or reaction time. The resolution was also required 350 min longer reaction time in order to achieve equilibrium. A comparable result could be obtained in five-fold scaling up RPBR.
format Article
author Chua, Lee Suan
Sarmidi, Mohamad Roji
author_facet Chua, Lee Suan
Sarmidi, Mohamad Roji
author_sort Chua, Lee Suan
title Immobilised lipase-catalysed resolution of (R,S)-1-phenylethanol in recirculated packed bed reactor
title_short Immobilised lipase-catalysed resolution of (R,S)-1-phenylethanol in recirculated packed bed reactor
title_full Immobilised lipase-catalysed resolution of (R,S)-1-phenylethanol in recirculated packed bed reactor
title_fullStr Immobilised lipase-catalysed resolution of (R,S)-1-phenylethanol in recirculated packed bed reactor
title_full_unstemmed Immobilised lipase-catalysed resolution of (R,S)-1-phenylethanol in recirculated packed bed reactor
title_sort immobilised lipase-catalysed resolution of (r,s)-1-phenylethanol in recirculated packed bed reactor
publisher Elsevier
publishDate 2004
url http://eprints.utm.my/id/eprint/6305/
http://dx.doi.org/10.1016/j.molcatb.2004.02.004
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score 13.251813

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