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
.jpg)
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/105708
Ver los metadatos del registro completo
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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:UNLP2025-10-22T17:04:23Zoai: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:13292025-10-22 17:04:23.677SEDICI (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 |
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2017 |
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http://sedici.unlp.edu.ar/handle/10915/105708 |
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