Covalent immobilization of Candida rugosa lipase at alkaline pH and their application in the regioselective deprotection of per-O-acetylated thymidine

Autores
Rivero, Cintia Wanda; Palomo, Jose M.
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Lipase from Candida rugosa (CRL) was stabilized at alkaline pH to overcome the inactivation problem and was immobilized for the first time by multipoint covalent attachment on different aldehyde-activated matrices. PEG was used as a stabilizing agent on the activity of CRL. At these conditions, CRL maintained 50% activity at pH 10 after 17 h incubation in the presence of 40% (w/v) of PEG, whereas the enzyme without additive was instantaneously inactive after incubation at pH 10. Thus, this enzyme was covalently immobilized at alkaline pH on three aldehyde-activated supports: aldehyde-activated Sepharose, aldehyde-activated Lewatit105 and heterofunctional aldehyde-activated EDA-Sepharose in high overall yields. Heterogeneous stable CRL catalysts at high temperature and solvent were obtained. The aldehyde-activated Sepharose-CRL preparation maintained 70% activity at 50 °C or 30% (v/v) acetonitrile after 22 h and exhibited high regioselectivity in the deprotection process of per-O-acetylated thymidine, producing the 3ʹ-OH-5ʹ-OAc-thymidine in 91% yield at pH 5.
Fil: Rivero, Cintia Wanda. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Palomo, Jose M.. Consejo Superior de Investigaciones Científicas; España
Materia
ALKALINE PH
CANDIDA RUGOSA LIPASE
COVALENT IMMOBILIZATION
NUCLEOSIDES
PEG
REGIOSELECTIVITY
STABILIZATION
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/114298
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/114298
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Covalent immobilization of Candida rugosa lipase at alkaline pH and their application in the regioselective deprotection of per-O-acetylated thymidineRivero, Cintia WandaPalomo, Jose M.ALKALINE PHCANDIDA RUGOSA LIPASECOVALENT IMMOBILIZATIONNUCLEOSIDESPEGREGIOSELECTIVITYSTABILIZATIONhttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2Lipase from Candida rugosa (CRL) was stabilized at alkaline pH to overcome the inactivation problem and was immobilized for the first time by multipoint covalent attachment on different aldehyde-activated matrices. PEG was used as a stabilizing agent on the activity of CRL. At these conditions, CRL maintained 50% activity at pH 10 after 17 h incubation in the presence of 40% (w/v) of PEG, whereas the enzyme without additive was instantaneously inactive after incubation at pH 10. Thus, this enzyme was covalently immobilized at alkaline pH on three aldehyde-activated supports: aldehyde-activated Sepharose, aldehyde-activated Lewatit105 and heterofunctional aldehyde-activated EDA-Sepharose in high overall yields. Heterogeneous stable CRL catalysts at high temperature and solvent were obtained. The aldehyde-activated Sepharose-CRL preparation maintained 70% activity at 50 °C or 30% (v/v) acetonitrile after 22 h and exhibited high regioselectivity in the deprotection process of per-O-acetylated thymidine, producing the 3ʹ-OH-5ʹ-OAc-thymidine in 91% yield at pH 5.Fil: Rivero, Cintia Wanda. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Palomo, Jose M.. Consejo Superior de Investigaciones Científicas; EspañaMDPI AG2016-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/114298Rivero, Cintia Wanda; Palomo, Jose M.; Covalent immobilization of Candida rugosa lipase at alkaline pH and their application in the regioselective deprotection of per-O-acetylated thymidine; MDPI AG; Catalysts; 6; 8; 8-2016; 1-112073-4344CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3390/catal6080115info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2073-4344/6/8/115info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:06:42Zoai:ri.conicet.gov.ar:11336/114298instacron: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:34982025-09-29 10:06:42.798CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Covalent immobilization of Candida rugosa lipase at alkaline pH and their application in the regioselective deprotection of per-O-acetylated thymidine
title Covalent immobilization of Candida rugosa lipase at alkaline pH and their application in the regioselective deprotection of per-O-acetylated thymidine
spellingShingle Covalent immobilization of Candida rugosa lipase at alkaline pH and their application in the regioselective deprotection of per-O-acetylated thymidine
Rivero, Cintia Wanda
ALKALINE PH
CANDIDA RUGOSA LIPASE
COVALENT IMMOBILIZATION
NUCLEOSIDES
PEG
REGIOSELECTIVITY
STABILIZATION
title_short Covalent immobilization of Candida rugosa lipase at alkaline pH and their application in the regioselective deprotection of per-O-acetylated thymidine
title_full Covalent immobilization of Candida rugosa lipase at alkaline pH and their application in the regioselective deprotection of per-O-acetylated thymidine
title_fullStr Covalent immobilization of Candida rugosa lipase at alkaline pH and their application in the regioselective deprotection of per-O-acetylated thymidine
title_full_unstemmed Covalent immobilization of Candida rugosa lipase at alkaline pH and their application in the regioselective deprotection of per-O-acetylated thymidine
title_sort Covalent immobilization of Candida rugosa lipase at alkaline pH and their application in the regioselective deprotection of per-O-acetylated thymidine
dc.creator.none.fl_str_mv Rivero, Cintia Wanda
Palomo, Jose M.
author Rivero, Cintia Wanda
author_facet Rivero, Cintia Wanda
Palomo, Jose M.
author_role author
author2 Palomo, Jose M.
author2_role author
dc.subject.none.fl_str_mv ALKALINE PH
CANDIDA RUGOSA LIPASE
COVALENT IMMOBILIZATION
NUCLEOSIDES
PEG
REGIOSELECTIVITY
STABILIZATION
topic ALKALINE PH
CANDIDA RUGOSA LIPASE
COVALENT IMMOBILIZATION
NUCLEOSIDES
PEG
REGIOSELECTIVITY
STABILIZATION
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Lipase from Candida rugosa (CRL) was stabilized at alkaline pH to overcome the inactivation problem and was immobilized for the first time by multipoint covalent attachment on different aldehyde-activated matrices. PEG was used as a stabilizing agent on the activity of CRL. At these conditions, CRL maintained 50% activity at pH 10 after 17 h incubation in the presence of 40% (w/v) of PEG, whereas the enzyme without additive was instantaneously inactive after incubation at pH 10. Thus, this enzyme was covalently immobilized at alkaline pH on three aldehyde-activated supports: aldehyde-activated Sepharose, aldehyde-activated Lewatit105 and heterofunctional aldehyde-activated EDA-Sepharose in high overall yields. Heterogeneous stable CRL catalysts at high temperature and solvent were obtained. The aldehyde-activated Sepharose-CRL preparation maintained 70% activity at 50 °C or 30% (v/v) acetonitrile after 22 h and exhibited high regioselectivity in the deprotection process of per-O-acetylated thymidine, producing the 3ʹ-OH-5ʹ-OAc-thymidine in 91% yield at pH 5.
Fil: Rivero, Cintia Wanda. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Palomo, Jose M.. Consejo Superior de Investigaciones Científicas; España
description Lipase from Candida rugosa (CRL) was stabilized at alkaline pH to overcome the inactivation problem and was immobilized for the first time by multipoint covalent attachment on different aldehyde-activated matrices. PEG was used as a stabilizing agent on the activity of CRL. At these conditions, CRL maintained 50% activity at pH 10 after 17 h incubation in the presence of 40% (w/v) of PEG, whereas the enzyme without additive was instantaneously inactive after incubation at pH 10. Thus, this enzyme was covalently immobilized at alkaline pH on three aldehyde-activated supports: aldehyde-activated Sepharose, aldehyde-activated Lewatit105 and heterofunctional aldehyde-activated EDA-Sepharose in high overall yields. Heterogeneous stable CRL catalysts at high temperature and solvent were obtained. The aldehyde-activated Sepharose-CRL preparation maintained 70% activity at 50 °C or 30% (v/v) acetonitrile after 22 h and exhibited high regioselectivity in the deprotection process of per-O-acetylated thymidine, producing the 3ʹ-OH-5ʹ-OAc-thymidine in 91% yield at pH 5.
publishDate 2016
dc.date.none.fl_str_mv 2016-08
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/11336/114298
Rivero, Cintia Wanda; Palomo, Jose M.; Covalent immobilization of Candida rugosa lipase at alkaline pH and their application in the regioselective deprotection of per-O-acetylated thymidine; MDPI AG; Catalysts; 6; 8; 8-2016; 1-11
2073-4344
CONICET Digital
CONICET
url http://hdl.handle.net/11336/114298
identifier_str_mv Rivero, Cintia Wanda; Palomo, Jose M.; Covalent immobilization of Candida rugosa lipase at alkaline pH and their application in the regioselective deprotection of per-O-acetylated thymidine; MDPI AG; Catalysts; 6; 8; 8-2016; 1-11
2073-4344
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.3390/catal6080115
info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2073-4344/6/8/115
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv MDPI AG
publisher.none.fl_str_mv MDPI AG
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
_version_ 1844613918505304064
score 13.070432

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