Molecular recognition of an acyl–enzyme intermediate on the lipase B from <i>Candida antarctica</i>

Autores
Toledo, María Victoria; Llerena Suster, Carlos Rafael; Ferreira, María L.; Collins, Sebastián E.; Briand, Laura Estefanía
Año de publicación
2017
Idioma
español castellano
Tipo de recurso
artículo
Estado
versión publicada
Descripción
This investigation provides evidence of the acyl enzyme species involved in the interaction of R/Sketoprofen with the lipase B from Candida antarctica. The interaction between the profen and the enzyme was studied by in situ time-resolved ATR-FTIR under both static and transient conditions. Particularly, modulation excitation spectroscopy (MES) with phase sensitive detection (PSD) allowed us to univocally distinguish the signals belonging to the interaction between ketoprofen and the enzyme from the strong background signals. These experimental tools coupled with theoretical DFT analysis allowed us to propose various species derived from the interaction of ketoprofen with serine through H bonding (without reaction) and the acyl enzyme species (ester bond formation) which are the intermediates in the biocatalytic assisted esterification and hydrolysis using lipases.
Centro de Investigación y Desarrollo en Ciencias Aplicadas
Facultad de Ciencias Exactas
Materia
Ciencias Exactas
Candida antarctica
acyl enzyme species
ketoprofen
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/105708
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/105708
network_acronym_str SEDICI
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network_name_str SEDICI (UNLP)
spelling Molecular recognition of an acyl–enzyme intermediate on the lipase B from <i>Candida antarctica</i>Toledo, María VictoriaLlerena Suster, Carlos RafaelFerreira, María L.Collins, Sebastián E.Briand, Laura EstefaníaCiencias ExactasCandida antarcticaacyl enzyme speciesketoprofenThis investigation provides evidence of the acyl enzyme species involved in the interaction of <i>R/S</i>ketoprofen with the lipase B from <i>Candida antarctica</i>. The interaction between the profen and the enzyme was studied by <i>in situ</i> time-resolved ATR-FTIR under both static and transient conditions. Particularly, modulation excitation spectroscopy (MES) with phase sensitive detection (PSD) allowed us to univocally distinguish the signals belonging to the interaction between ketoprofen and the enzyme from the strong background signals. These experimental tools coupled with theoretical DFT analysis allowed us to propose various species derived from the interaction of ketoprofen with serine through H bonding (without reaction) and the acyl enzyme species (ester bond formation) which are the intermediates in the biocatalytic assisted esterification and hydrolysis using lipases.Centro de Investigación y Desarrollo en Ciencias AplicadasFacultad de Ciencias Exactas2017info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf1953-1964http://sedici.unlp.edu.ar/handle/10915/105708spainfo:eu-repo/semantics/altIdentifier/url/https://pubs.rsc.org/en/content/articlelanding/2017/CY/C7CY00245Ainfo:eu-repo/semantics/altIdentifier/issn/2044-4761info:eu-repo/semantics/altIdentifier/doi/10.1039/c7cy00245ainfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:23:32Zoai:sedici.unlp.edu.ar:10915/105708Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:23:32.296SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Molecular recognition of an acyl–enzyme intermediate on the lipase B from <i>Candida antarctica</i>
title Molecular recognition of an acyl–enzyme intermediate on the lipase B from <i>Candida antarctica</i>
spellingShingle Molecular recognition of an acyl–enzyme intermediate on the lipase B from <i>Candida antarctica</i>
Toledo, María Victoria
Ciencias Exactas
Candida antarctica
acyl enzyme species
ketoprofen
title_short Molecular recognition of an acyl–enzyme intermediate on the lipase B from <i>Candida antarctica</i>
title_full Molecular recognition of an acyl–enzyme intermediate on the lipase B from <i>Candida antarctica</i>
title_fullStr Molecular recognition of an acyl–enzyme intermediate on the lipase B from <i>Candida antarctica</i>
title_full_unstemmed Molecular recognition of an acyl–enzyme intermediate on the lipase B from <i>Candida antarctica</i>
title_sort Molecular recognition of an acyl–enzyme intermediate on the lipase B from <i>Candida antarctica</i>
dc.creator.none.fl_str_mv Toledo, María Victoria
Llerena Suster, Carlos Rafael
Ferreira, María L.
Collins, Sebastián E.
Briand, Laura Estefanía
author Toledo, María Victoria
author_facet Toledo, María Victoria
Llerena Suster, Carlos Rafael
Ferreira, María L.
Collins, Sebastián E.
Briand, Laura Estefanía
author_role author
author2 Llerena Suster, Carlos Rafael
Ferreira, María L.
Collins, Sebastián E.
Briand, Laura Estefanía
author2_role author
author
author
author
dc.subject.none.fl_str_mv Ciencias Exactas
Candida antarctica
acyl enzyme species
ketoprofen
topic Ciencias Exactas
Candida antarctica
acyl enzyme species
ketoprofen
dc.description.none.fl_txt_mv This investigation provides evidence of the acyl enzyme species involved in the interaction of <i>R/S</i>ketoprofen with the lipase B from <i>Candida antarctica</i>. The interaction between the profen and the enzyme was studied by <i>in situ</i> time-resolved ATR-FTIR under both static and transient conditions. Particularly, modulation excitation spectroscopy (MES) with phase sensitive detection (PSD) allowed us to univocally distinguish the signals belonging to the interaction between ketoprofen and the enzyme from the strong background signals. These experimental tools coupled with theoretical DFT analysis allowed us to propose various species derived from the interaction of ketoprofen with serine through H bonding (without reaction) and the acyl enzyme species (ester bond formation) which are the intermediates in the biocatalytic assisted esterification and hydrolysis using lipases.
Centro de Investigación y Desarrollo en Ciencias Aplicadas
Facultad de Ciencias Exactas
description This investigation provides evidence of the acyl enzyme species involved in the interaction of <i>R/S</i>ketoprofen with the lipase B from <i>Candida antarctica</i>. The interaction between the profen and the enzyme was studied by <i>in situ</i> time-resolved ATR-FTIR under both static and transient conditions. Particularly, modulation excitation spectroscopy (MES) with phase sensitive detection (PSD) allowed us to univocally distinguish the signals belonging to the interaction between ketoprofen and the enzyme from the strong background signals. These experimental tools coupled with theoretical DFT analysis allowed us to propose various species derived from the interaction of ketoprofen with serine through H bonding (without reaction) and the acyl enzyme species (ester bond formation) which are the intermediates in the biocatalytic assisted esterification and hydrolysis using lipases.
publishDate 2017
dc.date.none.fl_str_mv 2017
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/105708
url http://sedici.unlp.edu.ar/handle/10915/105708
dc.language.none.fl_str_mv spa
language spa
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://pubs.rsc.org/en/content/articlelanding/2017/CY/C7CY00245A
info:eu-repo/semantics/altIdentifier/issn/2044-4761
info:eu-repo/semantics/altIdentifier/doi/10.1039/c7cy00245a
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
1953-1964
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.070432

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