dc.contributor.author |
Brady, D
|
en_US |
dc.contributor.author |
Steenkamp, Lucia H
|
en_US |
dc.contributor.author |
Skein, E
|
en_US |
dc.contributor.author |
Chaplin, JA
|
en_US |
dc.contributor.author |
Reddy, S
|
en_US |
dc.date.accessioned |
2007-01-11T11:55:30Z |
en_US |
dc.date.accessioned |
2007-06-07T10:04:54Z |
|
dc.date.available |
2007-01-11T11:55:30Z |
en_US |
dc.date.available |
2007-06-07T10:04:54Z |
|
dc.date.issued |
2004-03-04 |
en_US |
dc.identifier.citation |
Brady, D et al. 2004. Optimisation of the enantioselective biocatalytic hydrolysis of naproxen ethyl ester using ChiroCLEC-CR. Enzyme and microbial technology, vol 34, 4 March, pp 283-291 |
en_US |
dc.identifier.issn |
0141-0229 |
en_US |
dc.identifier.uri |
http://hdl.handle.net/10204/1381
|
en_US |
dc.identifier.uri |
http://hdl.handle.net/10204/1381
|
|
dc.description.abstract |
In a biocatalytic reaction the immobilized lipase ChiroCLEC-CR enantioselectively hydrolysed a naproxen ethyl ester racemate, yielding (S)-naproxen with an enantiomeric excess of more than 98%, an enantiomeric ratio (E) of more than 100, and substrate conversion in excess of 40%. Statistically designed experiments were performed to optimise temperature, enzyme to substrate ratio, substrate concentration, agitation, reaction time, pH, buffer concentration and co-solvent addition. Optimisation efforts resulted in more than 20-fold improvement of activity, while the excellent enantioselectivity of the enzymes was maintained. In particular, the addition of PEG 1000 as a co-solvent improved conversion rates 10-fold. The kinetic parameters V-max and K-M were determined to be 0.359_mol/min/mg and 17.6 mM, respectively. The optimised reaction conditions were 10% (m/v) substrate, and enzyme to substrate ratio of 1:50, at 50 degrees C and pH 5 with addition of 41% PEG 1000. In spite of these kinetic improvements, the stability of the biocatalytic activity under these conditions was poor, limiting the number of possible recycles. |
en_US |
dc.format.extent |
185111 bytes |
en_US |
dc.format.mimetype |
application/pdf |
en_US |
dc.language.iso |
en |
en_US |
dc.publisher |
Elsevier Science Inc. |
en_US |
dc.rights |
Copyright: 2004 Elsevier Inc. |
en_US |
dc.subject |
Candida rugosa lipase |
en_US |
dc.subject |
Enantioselectivity |
en_US |
dc.subject |
ChiroCLEC-CR |
en_US |
dc.subject |
Hydrolysis |
en_US |
dc.subject |
Naproxen ester |
en_US |
dc.subject |
S-Naproxen |
en_US |
dc.subject |
Biotechnology |
en_US |
dc.subject |
Applied microbiology |
en_US |
dc.title |
Optimisation of the enantioselective biocatalytic hydrolysis of naproxen ethyl ester using ChiroCLEC-CR |
en_US |
dc.type |
Article |
en_US |
dc.identifier.apacitation |
Brady, D., Steenkamp, L. H., Skein, E., Chaplin, J., & Reddy, S. (2004). Optimisation of the enantioselective biocatalytic hydrolysis of naproxen ethyl ester using ChiroCLEC-CR. http://hdl.handle.net/10204/1381 |
en_ZA |
dc.identifier.chicagocitation |
Brady, D, Lucia H Steenkamp, E Skein, JA Chaplin, and S Reddy "Optimisation of the enantioselective biocatalytic hydrolysis of naproxen ethyl ester using ChiroCLEC-CR." (2004) http://hdl.handle.net/10204/1381 |
en_ZA |
dc.identifier.vancouvercitation |
Brady D, Steenkamp LH, Skein E, Chaplin J, Reddy S. Optimisation of the enantioselective biocatalytic hydrolysis of naproxen ethyl ester using ChiroCLEC-CR. 2004; http://hdl.handle.net/10204/1381. |
en_ZA |
dc.identifier.ris |
TY - Article
AU - Brady, D
AU - Steenkamp, Lucia H
AU - Skein, E
AU - Chaplin, JA
AU - Reddy, S
AB - In a biocatalytic reaction the immobilized lipase ChiroCLEC-CR enantioselectively hydrolysed a naproxen ethyl ester racemate, yielding (S)-naproxen with an enantiomeric excess of more than 98%, an enantiomeric ratio (E) of more than 100, and substrate conversion in excess of 40%. Statistically designed experiments were performed to optimise temperature, enzyme to substrate ratio, substrate concentration, agitation, reaction time, pH, buffer concentration and co-solvent addition. Optimisation efforts resulted in more than 20-fold improvement of activity, while the excellent enantioselectivity of the enzymes was maintained. In particular, the addition of PEG 1000 as a co-solvent improved conversion rates 10-fold. The kinetic parameters V-max and K-M were determined to be 0.359_mol/min/mg and 17.6 mM, respectively. The optimised reaction conditions were 10% (m/v) substrate, and enzyme to substrate ratio of 1:50, at 50 degrees C and pH 5 with addition of 41% PEG 1000. In spite of these kinetic improvements, the stability of the biocatalytic activity under these conditions was poor, limiting the number of possible recycles.
DA - 2004-03-04
DB - ResearchSpace
DP - CSIR
KW - Candida rugosa lipase
KW - Enantioselectivity
KW - ChiroCLEC-CR
KW - Hydrolysis
KW - Naproxen ester
KW - S-Naproxen
KW - Biotechnology
KW - Applied microbiology
LK - https://researchspace.csir.co.za
PY - 2004
SM - 0141-0229
T1 - Optimisation of the enantioselective biocatalytic hydrolysis of naproxen ethyl ester using ChiroCLEC-CR
TI - Optimisation of the enantioselective biocatalytic hydrolysis of naproxen ethyl ester using ChiroCLEC-CR
UR - http://hdl.handle.net/10204/1381
ER -
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en_ZA |