Stereospecificity of pig liver esterase in the hydrolysis of racemic esters derived from 1,8-cineole

Autores
Loandos, Maria del Huerto; Muro, Ana Carolina; Villecco, Margarita Beatriz; Catalan, Cesar Atilio Nazareno
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The efficient synthesis of biological active compounds, so much natural as not natural, frequently requires chiral syntons. Enzymes as chiral catalysts are widely used for this purpose owing to the fact that it is usually difficult to carry out highly enantioselective transformations using chemical methods. Esterases, such as that of pig liver (PLE), a serine hydrolase, is able to hydrolize a wide range of substrates with high stereoselectivity. This enzyme has been used for the hydrolysis of different esters, mainly meso and prochiral diesters. 1,8-cineole (1) or eucalyptol is a bicyclic monoterpene ether widespread in plant kingdom (Fig. 1). This is the main constituent of a number of essential oils, in particular those produced by several species of the genus Eucaliptus. We selected the racemates of acetates 5a and 6a, and the diacetate 6b with the purpose of studying the specificity of PLE and its utility for preparing pure enantiomers.   Our results indicate that the enzyme is effective for the enantioselective hydrolysis of the racemate of 5a. However, it doesn´t discriminate the racemate of the primary acetate 6a. The results of the hydrolysis of the diacetate 6b analysed after 3 hours incubation gave a 1:1 mixture of the hydroxyacetate 7b and diol 8, remaining approximately 60% of the unaffected diacetate.  On the other hand, this method represents a route of easy access to 7b, which is almost impossible to obtain by acetylation of the corresponding alcohol, and for obtaining pure enantiomers of 3a.
Fil: Loandos, Maria del Huerto. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
Fil: Muro, Ana Carolina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
Fil: Villecco, Margarita Beatriz. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
Fil: Catalan, Cesar Atilio Nazareno. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
Materia
1,8-CINEOLE
BIOLOGICALLY
ESTERASES
ENZYME
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
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CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
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oai:ri.conicet.gov.ar:11336/102935
Acceder
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spelling Stereospecificity of pig liver esterase in the hydrolysis of racemic esters derived from 1,8-cineoleLoandos, Maria del HuertoMuro, Ana CarolinaVillecco, Margarita BeatrizCatalan, Cesar Atilio Nazareno1,8-CINEOLEBIOLOGICALLYESTERASESENZYMEhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The efficient synthesis of biological active compounds, so much natural as not natural, frequently requires chiral syntons. Enzymes as chiral catalysts are widely used for this purpose owing to the fact that it is usually difficult to carry out highly enantioselective transformations using chemical methods. Esterases, such as that of pig liver (PLE), a serine hydrolase, is able to hydrolize a wide range of substrates with high stereoselectivity. This enzyme has been used for the hydrolysis of different esters, mainly meso and prochiral diesters. 1,8-cineole (1) or eucalyptol is a bicyclic monoterpene ether widespread in plant kingdom (Fig. 1). This is the main constituent of a number of essential oils, in particular those produced by several species of the genus Eucaliptus. We selected the racemates of acetates 5a and 6a, and the diacetate 6b with the purpose of studying the specificity of PLE and its utility for preparing pure enantiomers.   Our results indicate that the enzyme is effective for the enantioselective hydrolysis of the racemate of 5a. However, it doesn´t discriminate the racemate of the primary acetate 6a. The results of the hydrolysis of the diacetate 6b analysed after 3 hours incubation gave a 1:1 mixture of the hydroxyacetate 7b and diol 8, remaining approximately 60% of the unaffected diacetate.  On the other hand, this method represents a route of easy access to 7b, which is almost impossible to obtain by acetylation of the corresponding alcohol, and for obtaining pure enantiomers of 3a.Fil: Loandos, Maria del Huerto. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; ArgentinaFil: Muro, Ana Carolina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; ArgentinaFil: Villecco, Margarita Beatriz. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; ArgentinaFil: Catalan, Cesar Atilio Nazareno. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; ArgentinaInstituto de Investigación de las Ciencias Exactas Físicas y Naturales2006-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/102935Loandos, Maria del Huerto; Muro, Ana Carolina; Villecco, Margarita Beatriz; Catalan, Cesar Atilio Nazareno; Stereospecificity of pig liver esterase in the hydrolysis of racemic esters derived from 1,8-cineole; Instituto de Investigación de las Ciencias Exactas Físicas y Naturales; Molecular Medicinal Chemistry; 10; 12-2006; 35-371666-888X1666-888XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.idecefyn.com.ar/mmcv10/11.pdfinfo:eu-repo/semantics/altIdentifier/url/https://www.semanticscholar.org/paper/Stereospecificity-of-pig-liver-esterase-in-the-of-Muro-Villecco/61523fa64e5ec542f5b948f842778a0dbe29231ainfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:01:50Zoai:ri.conicet.gov.ar:11336/102935instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:01:50.892CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Stereospecificity of pig liver esterase in the hydrolysis of racemic esters derived from 1,8-cineole
title Stereospecificity of pig liver esterase in the hydrolysis of racemic esters derived from 1,8-cineole
spellingShingle Stereospecificity of pig liver esterase in the hydrolysis of racemic esters derived from 1,8-cineole
Loandos, Maria del Huerto
1,8-CINEOLE
BIOLOGICALLY
ESTERASES
ENZYME
title_short Stereospecificity of pig liver esterase in the hydrolysis of racemic esters derived from 1,8-cineole
title_full Stereospecificity of pig liver esterase in the hydrolysis of racemic esters derived from 1,8-cineole
title_fullStr Stereospecificity of pig liver esterase in the hydrolysis of racemic esters derived from 1,8-cineole
title_full_unstemmed Stereospecificity of pig liver esterase in the hydrolysis of racemic esters derived from 1,8-cineole
title_sort Stereospecificity of pig liver esterase in the hydrolysis of racemic esters derived from 1,8-cineole
dc.creator.none.fl_str_mv Loandos, Maria del Huerto
Muro, Ana Carolina
Villecco, Margarita Beatriz
Catalan, Cesar Atilio Nazareno
author Loandos, Maria del Huerto
author_facet Loandos, Maria del Huerto
Muro, Ana Carolina
Villecco, Margarita Beatriz
Catalan, Cesar Atilio Nazareno
author_role author
author2 Muro, Ana Carolina
Villecco, Margarita Beatriz
Catalan, Cesar Atilio Nazareno
author2_role author
author
author
dc.subject.none.fl_str_mv 1,8-CINEOLE
BIOLOGICALLY
ESTERASES
ENZYME
topic 1,8-CINEOLE
BIOLOGICALLY
ESTERASES
ENZYME
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The efficient synthesis of biological active compounds, so much natural as not natural, frequently requires chiral syntons. Enzymes as chiral catalysts are widely used for this purpose owing to the fact that it is usually difficult to carry out highly enantioselective transformations using chemical methods. Esterases, such as that of pig liver (PLE), a serine hydrolase, is able to hydrolize a wide range of substrates with high stereoselectivity. This enzyme has been used for the hydrolysis of different esters, mainly meso and prochiral diesters. 1,8-cineole (1) or eucalyptol is a bicyclic monoterpene ether widespread in plant kingdom (Fig. 1). This is the main constituent of a number of essential oils, in particular those produced by several species of the genus Eucaliptus. We selected the racemates of acetates 5a and 6a, and the diacetate 6b with the purpose of studying the specificity of PLE and its utility for preparing pure enantiomers.   Our results indicate that the enzyme is effective for the enantioselective hydrolysis of the racemate of 5a. However, it doesn´t discriminate the racemate of the primary acetate 6a. The results of the hydrolysis of the diacetate 6b analysed after 3 hours incubation gave a 1:1 mixture of the hydroxyacetate 7b and diol 8, remaining approximately 60% of the unaffected diacetate.  On the other hand, this method represents a route of easy access to 7b, which is almost impossible to obtain by acetylation of the corresponding alcohol, and for obtaining pure enantiomers of 3a.
Fil: Loandos, Maria del Huerto. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
Fil: Muro, Ana Carolina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
Fil: Villecco, Margarita Beatriz. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
Fil: Catalan, Cesar Atilio Nazareno. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
description The efficient synthesis of biological active compounds, so much natural as not natural, frequently requires chiral syntons. Enzymes as chiral catalysts are widely used for this purpose owing to the fact that it is usually difficult to carry out highly enantioselective transformations using chemical methods. Esterases, such as that of pig liver (PLE), a serine hydrolase, is able to hydrolize a wide range of substrates with high stereoselectivity. This enzyme has been used for the hydrolysis of different esters, mainly meso and prochiral diesters. 1,8-cineole (1) or eucalyptol is a bicyclic monoterpene ether widespread in plant kingdom (Fig. 1). This is the main constituent of a number of essential oils, in particular those produced by several species of the genus Eucaliptus. We selected the racemates of acetates 5a and 6a, and the diacetate 6b with the purpose of studying the specificity of PLE and its utility for preparing pure enantiomers.   Our results indicate that the enzyme is effective for the enantioselective hydrolysis of the racemate of 5a. However, it doesn´t discriminate the racemate of the primary acetate 6a. The results of the hydrolysis of the diacetate 6b analysed after 3 hours incubation gave a 1:1 mixture of the hydroxyacetate 7b and diol 8, remaining approximately 60% of the unaffected diacetate.  On the other hand, this method represents a route of easy access to 7b, which is almost impossible to obtain by acetylation of the corresponding alcohol, and for obtaining pure enantiomers of 3a.
publishDate 2006
dc.date.none.fl_str_mv 2006-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/102935
Loandos, Maria del Huerto; Muro, Ana Carolina; Villecco, Margarita Beatriz; Catalan, Cesar Atilio Nazareno; Stereospecificity of pig liver esterase in the hydrolysis of racemic esters derived from 1,8-cineole; Instituto de Investigación de las Ciencias Exactas Físicas y Naturales; Molecular Medicinal Chemistry; 10; 12-2006; 35-37
1666-888X
1666-888X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/102935
identifier_str_mv Loandos, Maria del Huerto; Muro, Ana Carolina; Villecco, Margarita Beatriz; Catalan, Cesar Atilio Nazareno; Stereospecificity of pig liver esterase in the hydrolysis of racemic esters derived from 1,8-cineole; Instituto de Investigación de las Ciencias Exactas Físicas y Naturales; Molecular Medicinal Chemistry; 10; 12-2006; 35-37
1666-888X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.idecefyn.com.ar/mmcv10/11.pdf
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dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
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dc.publisher.none.fl_str_mv Instituto de Investigación de las Ciencias Exactas Físicas y Naturales
publisher.none.fl_str_mv Instituto de Investigación de las Ciencias Exactas Físicas y Naturales
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
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reponame_str CONICET Digital (CONICET)
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instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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