Computational approach to solvent-free synthesis of ethyl oleate using Candida rugosa and Candida antarctica B lipases. I. Interfacial activation and substrate (ethanol, oleic acid...

Autores
Foresti, María Laura; Ferreira, María Luján
Año de publicación
2004
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
This paper presents the results of a MM2 study of the adsorption of oleic acid and ethanol/water in the tunnel and active-site models of lipases from Candida rugosa and Candida antarctica B. The role of an interface polar/no polar in the opening of C rugosa lipase's lid is also addressed, discussed and analyzed at the level of the conformational changes needed to achieve the lipase open form. The adsorption of oleic acid and alcohols considering C. antarctica B, a lipase not interfacially activated, is also presented. In this case, the tunnel is shorter than in case of C. rugosa lipase. Two different pockets can be visualized at the active site-tunnel model of C. antarctica B lipase: one for the acyl group and another for the alcohol. Wrong location of alcohol and oleic acid severely hinders reaction because it hinders the H-transfer to histidine, a key step in the reaction mechanism. Right location of alcohol decreases the possibility of alcohol inhibition. In the case of C. rugosa, no restrictions for ethanol/water location are found. For that lipase, a second adsorption site for oleic acid (outside the tunnel) is presented. This site is the exit tunnel of the ester product when oleic acid is adsorbed in the tunnel. Experimental results of our own that correlate with this study are presented. © 2004 American Chemical Society.
Fil: Foresti, María Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Fil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Materia
Dynamics Simulations
Lipase
Molecular Dynamics
Molecular Modelling
Polyester Synthesis
Rhizomucor Miehei
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/61955
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/61955
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Computational approach to solvent-free synthesis of ethyl oleate using Candida rugosa and Candida antarctica B lipases. I. Interfacial activation and substrate (ethanol, oleic acid) adsorptionForesti, María LauraFerreira, María LujánDynamics SimulationsLipaseMolecular DynamicsMolecular ModellingPolyester SynthesisRhizomucor Mieheihttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2This paper presents the results of a MM2 study of the adsorption of oleic acid and ethanol/water in the tunnel and active-site models of lipases from Candida rugosa and Candida antarctica B. The role of an interface polar/no polar in the opening of C rugosa lipase's lid is also addressed, discussed and analyzed at the level of the conformational changes needed to achieve the lipase open form. The adsorption of oleic acid and alcohols considering C. antarctica B, a lipase not interfacially activated, is also presented. In this case, the tunnel is shorter than in case of C. rugosa lipase. Two different pockets can be visualized at the active site-tunnel model of C. antarctica B lipase: one for the acyl group and another for the alcohol. Wrong location of alcohol and oleic acid severely hinders reaction because it hinders the H-transfer to histidine, a key step in the reaction mechanism. Right location of alcohol decreases the possibility of alcohol inhibition. In the case of C. rugosa, no restrictions for ethanol/water location are found. For that lipase, a second adsorption site for oleic acid (outside the tunnel) is presented. This site is the exit tunnel of the ester product when oleic acid is adsorbed in the tunnel. Experimental results of our own that correlate with this study are presented. © 2004 American Chemical Society.Fil: Foresti, María Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; ArgentinaFil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; ArgentinaAmerican Chemical Society2004-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/61955Foresti, María Laura; Ferreira, María Luján; Computational approach to solvent-free synthesis of ethyl oleate using Candida rugosa and Candida antarctica B lipases. I. Interfacial activation and substrate (ethanol, oleic acid) adsorption; American Chemical Society; Biomacromolecules; 5; 6; 11-2004; 2366-23751525-7797CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1021/bm049688oinfo:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/abs/10.1021/bm049688oinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:05:43Zoai:ri.conicet.gov.ar:11336/61955instacron: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:34982025-10-22 12:05:43.541CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Computational approach to solvent-free synthesis of ethyl oleate using Candida rugosa and Candida antarctica B lipases. I. Interfacial activation and substrate (ethanol, oleic acid) adsorption
title Computational approach to solvent-free synthesis of ethyl oleate using Candida rugosa and Candida antarctica B lipases. I. Interfacial activation and substrate (ethanol, oleic acid) adsorption
spellingShingle Computational approach to solvent-free synthesis of ethyl oleate using Candida rugosa and Candida antarctica B lipases. I. Interfacial activation and substrate (ethanol, oleic acid) adsorption
Foresti, María Laura
Dynamics Simulations
Lipase
Molecular Dynamics
Molecular Modelling
Polyester Synthesis
Rhizomucor Miehei
title_short Computational approach to solvent-free synthesis of ethyl oleate using Candida rugosa and Candida antarctica B lipases. I. Interfacial activation and substrate (ethanol, oleic acid) adsorption
title_full Computational approach to solvent-free synthesis of ethyl oleate using Candida rugosa and Candida antarctica B lipases. I. Interfacial activation and substrate (ethanol, oleic acid) adsorption
title_fullStr Computational approach to solvent-free synthesis of ethyl oleate using Candida rugosa and Candida antarctica B lipases. I. Interfacial activation and substrate (ethanol, oleic acid) adsorption
title_full_unstemmed Computational approach to solvent-free synthesis of ethyl oleate using Candida rugosa and Candida antarctica B lipases. I. Interfacial activation and substrate (ethanol, oleic acid) adsorption
title_sort Computational approach to solvent-free synthesis of ethyl oleate using Candida rugosa and Candida antarctica B lipases. I. Interfacial activation and substrate (ethanol, oleic acid) adsorption
dc.creator.none.fl_str_mv Foresti, María Laura
Ferreira, María Luján
author Foresti, María Laura
author_facet Foresti, María Laura
Ferreira, María Luján
author_role author
author2 Ferreira, María Luján
author2_role author
dc.subject.none.fl_str_mv Dynamics Simulations
Lipase
Molecular Dynamics
Molecular Modelling
Polyester Synthesis
Rhizomucor Miehei
topic Dynamics Simulations
Lipase
Molecular Dynamics
Molecular Modelling
Polyester Synthesis
Rhizomucor Miehei
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv This paper presents the results of a MM2 study of the adsorption of oleic acid and ethanol/water in the tunnel and active-site models of lipases from Candida rugosa and Candida antarctica B. The role of an interface polar/no polar in the opening of C rugosa lipase's lid is also addressed, discussed and analyzed at the level of the conformational changes needed to achieve the lipase open form. The adsorption of oleic acid and alcohols considering C. antarctica B, a lipase not interfacially activated, is also presented. In this case, the tunnel is shorter than in case of C. rugosa lipase. Two different pockets can be visualized at the active site-tunnel model of C. antarctica B lipase: one for the acyl group and another for the alcohol. Wrong location of alcohol and oleic acid severely hinders reaction because it hinders the H-transfer to histidine, a key step in the reaction mechanism. Right location of alcohol decreases the possibility of alcohol inhibition. In the case of C. rugosa, no restrictions for ethanol/water location are found. For that lipase, a second adsorption site for oleic acid (outside the tunnel) is presented. This site is the exit tunnel of the ester product when oleic acid is adsorbed in the tunnel. Experimental results of our own that correlate with this study are presented. © 2004 American Chemical Society.
Fil: Foresti, María Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Fil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
description This paper presents the results of a MM2 study of the adsorption of oleic acid and ethanol/water in the tunnel and active-site models of lipases from Candida rugosa and Candida antarctica B. The role of an interface polar/no polar in the opening of C rugosa lipase's lid is also addressed, discussed and analyzed at the level of the conformational changes needed to achieve the lipase open form. The adsorption of oleic acid and alcohols considering C. antarctica B, a lipase not interfacially activated, is also presented. In this case, the tunnel is shorter than in case of C. rugosa lipase. Two different pockets can be visualized at the active site-tunnel model of C. antarctica B lipase: one for the acyl group and another for the alcohol. Wrong location of alcohol and oleic acid severely hinders reaction because it hinders the H-transfer to histidine, a key step in the reaction mechanism. Right location of alcohol decreases the possibility of alcohol inhibition. In the case of C. rugosa, no restrictions for ethanol/water location are found. For that lipase, a second adsorption site for oleic acid (outside the tunnel) is presented. This site is the exit tunnel of the ester product when oleic acid is adsorbed in the tunnel. Experimental results of our own that correlate with this study are presented. © 2004 American Chemical Society.
publishDate 2004
dc.date.none.fl_str_mv 2004-11
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/11336/61955
Foresti, María Laura; Ferreira, María Luján; Computational approach to solvent-free synthesis of ethyl oleate using Candida rugosa and Candida antarctica B lipases. I. Interfacial activation and substrate (ethanol, oleic acid) adsorption; American Chemical Society; Biomacromolecules; 5; 6; 11-2004; 2366-2375
1525-7797
CONICET Digital
CONICET
url http://hdl.handle.net/11336/61955
identifier_str_mv Foresti, María Laura; Ferreira, María Luján; Computational approach to solvent-free synthesis of ethyl oleate using Candida rugosa and Candida antarctica B lipases. I. Interfacial activation and substrate (ethanol, oleic acid) adsorption; American Chemical Society; Biomacromolecules; 5; 6; 11-2004; 2366-2375
1525-7797
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1021/bm049688o
info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/abs/10.1021/bm049688o
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
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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score 12.982451

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