Use of lipases for the kinetic resolution of lactic acid esters in heptane or in a solvent free system
peer reviewed tKinetic resolution of d,l-ethyl lactate (d,l-LA-Et) and d,l-butyl lactate (d,l-LA-Bu) was accomplished inthe presence of lipases. Transesterification of the lactate esters with alcohols was shown to be poorlyenantioselective, with a very low preference toward the l enantiomer. However...
Published in: | Journal of Molecular Catalysis B: Enzymatic |
---|---|
Main Authors: | , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Elsevier Science
2013
|
Subjects: | |
Online Access: | https://orbi.uliege.be/handle/2268/157165 https://doi.org/10.1016/j.molcatb.2013.08.015 |
id |
ftorbi:oai:orbi.ulg.ac.be:2268/157165 |
---|---|
record_format |
openpolar |
spelling |
ftorbi:oai:orbi.ulg.ac.be:2268/157165 2024-04-21T07:48:16+00:00 Use of lipases for the kinetic resolution of lactic acid esters in heptane or in a solvent free system Richard, Gaetan Nott, Katherine Nicks, François Paquot, Michel Blecker, Christophe Fauconnier, Marie-Laure 2013-09-05 https://orbi.uliege.be/handle/2268/157165 https://doi.org/10.1016/j.molcatb.2013.08.015 en eng Elsevier Science http://dx.doi.org/10.1016/j.molcatb.2013.08.015 urn:issn:1381-1177 urn:issn:1873-3158 https://orbi.uliege.be/handle/2268/157165 info:hdl:2268/157165 doi:10.1016/j.molcatb.2013.08.015 scopus-id:2-s2.0-84885000416 restricted access http://purl.org/coar/access_right/c_16ec info:eu-repo/semantics/restrictedAccess Journal of Molecular Catalysis B: Enzymatic, 97, 289-296 (2013-09-05) Candida antarctica lipase B Enantioselective acylation Enzyme catalysis Lactate esters Secondary alcohols Life sciences Food science Sciences du vivant Sciences des denrées alimentaires journal article http://purl.org/coar/resource_type/c_6501 info:eu-repo/semantics/article peer reviewed 2013 ftorbi https://doi.org/10.1016/j.molcatb.2013.08.015 2024-03-27T14:56:39Z peer reviewed tKinetic resolution of d,l-ethyl lactate (d,l-LA-Et) and d,l-butyl lactate (d,l-LA-Bu) was accomplished inthe presence of lipases. Transesterification of the lactate esters with alcohols was shown to be poorlyenantioselective, with a very low preference toward the l enantiomer. However, esterification of the freehydroxyl function of the lactate esters was much more enantioselective, with an opposite preferencetoward the d form. Among the 200 combinations screened (substrates and lipases), only two reactionsfulfilled the required criteria for an efficient resolution (fast reaction, enantioselectivity ratio higherthan 100). The best resolution was obtained by esterification of d,l-LA-Bu with butyric anhydride inthe presence of lipase B from Candida antarctica (CAL-B) in heptane (at 30◦C): LA-Bu was resolved in6 h with an initial esterification rate of d-LA-BU of 1.5 g L−1h−1g−1EZ, an enantioselectivity ratio higherthan 100, a l substrate consumption lower than 1%, and a final substrate enantiomeric excess superiorto 99%. After having demonstrated that neither LA-Bu nor BuAn were inhibitors of CAL-B, the reactionwas further improved by carrying it out in a solvent free system, at an elevated temperature (60◦C), andat a higher lipase concentration. LA-Bu was resolved in 6 h with an initial rate of 7.6 g L−1h−1g−1EZ, anenantioselectivity ratio higher than 100, and a final substrate enantiomeric excess of 95%. Article in Journal/Newspaper Antarc* Antarctica University of Liège: ORBi (Open Repository and Bibliography) Journal of Molecular Catalysis B: Enzymatic 97 289 296 |
institution |
Open Polar |
collection |
University of Liège: ORBi (Open Repository and Bibliography) |
op_collection_id |
ftorbi |
language |
English |
topic |
Candida antarctica lipase B Enantioselective acylation Enzyme catalysis Lactate esters Secondary alcohols Life sciences Food science Sciences du vivant Sciences des denrées alimentaires |
spellingShingle |
Candida antarctica lipase B Enantioselective acylation Enzyme catalysis Lactate esters Secondary alcohols Life sciences Food science Sciences du vivant Sciences des denrées alimentaires Richard, Gaetan Nott, Katherine Nicks, François Paquot, Michel Blecker, Christophe Fauconnier, Marie-Laure Use of lipases for the kinetic resolution of lactic acid esters in heptane or in a solvent free system |
topic_facet |
Candida antarctica lipase B Enantioselective acylation Enzyme catalysis Lactate esters Secondary alcohols Life sciences Food science Sciences du vivant Sciences des denrées alimentaires |
description |
peer reviewed tKinetic resolution of d,l-ethyl lactate (d,l-LA-Et) and d,l-butyl lactate (d,l-LA-Bu) was accomplished inthe presence of lipases. Transesterification of the lactate esters with alcohols was shown to be poorlyenantioselective, with a very low preference toward the l enantiomer. However, esterification of the freehydroxyl function of the lactate esters was much more enantioselective, with an opposite preferencetoward the d form. Among the 200 combinations screened (substrates and lipases), only two reactionsfulfilled the required criteria for an efficient resolution (fast reaction, enantioselectivity ratio higherthan 100). The best resolution was obtained by esterification of d,l-LA-Bu with butyric anhydride inthe presence of lipase B from Candida antarctica (CAL-B) in heptane (at 30◦C): LA-Bu was resolved in6 h with an initial esterification rate of d-LA-BU of 1.5 g L−1h−1g−1EZ, an enantioselectivity ratio higherthan 100, a l substrate consumption lower than 1%, and a final substrate enantiomeric excess superiorto 99%. After having demonstrated that neither LA-Bu nor BuAn were inhibitors of CAL-B, the reactionwas further improved by carrying it out in a solvent free system, at an elevated temperature (60◦C), andat a higher lipase concentration. LA-Bu was resolved in 6 h with an initial rate of 7.6 g L−1h−1g−1EZ, anenantioselectivity ratio higher than 100, and a final substrate enantiomeric excess of 95%. |
format |
Article in Journal/Newspaper |
author |
Richard, Gaetan Nott, Katherine Nicks, François Paquot, Michel Blecker, Christophe Fauconnier, Marie-Laure |
author_facet |
Richard, Gaetan Nott, Katherine Nicks, François Paquot, Michel Blecker, Christophe Fauconnier, Marie-Laure |
author_sort |
Richard, Gaetan |
title |
Use of lipases for the kinetic resolution of lactic acid esters in heptane or in a solvent free system |
title_short |
Use of lipases for the kinetic resolution of lactic acid esters in heptane or in a solvent free system |
title_full |
Use of lipases for the kinetic resolution of lactic acid esters in heptane or in a solvent free system |
title_fullStr |
Use of lipases for the kinetic resolution of lactic acid esters in heptane or in a solvent free system |
title_full_unstemmed |
Use of lipases for the kinetic resolution of lactic acid esters in heptane or in a solvent free system |
title_sort |
use of lipases for the kinetic resolution of lactic acid esters in heptane or in a solvent free system |
publisher |
Elsevier Science |
publishDate |
2013 |
url |
https://orbi.uliege.be/handle/2268/157165 https://doi.org/10.1016/j.molcatb.2013.08.015 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Journal of Molecular Catalysis B: Enzymatic, 97, 289-296 (2013-09-05) |
op_relation |
http://dx.doi.org/10.1016/j.molcatb.2013.08.015 urn:issn:1381-1177 urn:issn:1873-3158 https://orbi.uliege.be/handle/2268/157165 info:hdl:2268/157165 doi:10.1016/j.molcatb.2013.08.015 scopus-id:2-s2.0-84885000416 |
op_rights |
restricted access http://purl.org/coar/access_right/c_16ec info:eu-repo/semantics/restrictedAccess |
op_doi |
https://doi.org/10.1016/j.molcatb.2013.08.015 |
container_title |
Journal of Molecular Catalysis B: Enzymatic |
container_volume |
97 |
container_start_page |
289 |
op_container_end_page |
296 |
_version_ |
1796948748514885632 |