Green production of cladribine by using immobilized 2′-deoxyribosyltransferase from lactobacillus delbrueckii stabilized through a double covalent/entrapment technology

Autores
Rivero, Cintia Wanda; Garcia, Natalia Soledad; Fernández Lucas, Jesús; Betancor, Lorena; Romanelli, Gustavo Pablo; Trelles, Jorge Abel
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Nowadays, enzyme-mediated processes offer an eco-friendly and efficient alternative to the traditional multistep and environmentally harmful chemical processes. Herein we report the enzymatic synthesis of cladribine by a novel 2′-deoxyribosyltransferase (NDT)-based combined biocatalyst. To this end, Lactobacillus delbrueckii NDT (LdNDT) was successfully immobilized through a two-step immobilization methodology, including a covalent immobilization onto glutaraldehyde-activated biomimetic silica nanoparticles followed by biocatalyst entrapment in calcium alginate. The resulting immobilized derivative, SiGPEI 25000-LdNDT-Alg, displayed 98% retained activity and was shown to be active and stable in a broad range of pH (5–9) and temperature (30–60◦ C), but also displayed an extremely high reusability (up to 2100 reuses without negligible loss of activity) in the enzymatic production of cladribine. Finally, as a proof of concept, SiGPEI 25000-LdNDT-Alg was successfully employed in the green production of cladribine at mg scale.
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: Garcia, Natalia Soledad. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina
Fil: Fernández Lucas, Jesús. Universidad Europea de Madrid; España. Universidad de la Costa; Colombia
Fil: Betancor, Lorena. Universidad ORT Uruguay; Uruguay
Fil: Romanelli, Gustavo Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Ciencias Aplicadas "Dr. Jorge J. Ronco". Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Ciencias Aplicadas; Argentina
Fil: Trelles, Jorge Abel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
ANTINEOPLASTIC DRUG
BIOMIMETIC SILICA
CALCIUM ALGINATE
ENTRAPMENT
ENZYME IMMOBILIZATION
GLUTARALDEHYDE
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:11336/165857
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/165857
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Green production of cladribine by using immobilized 2′-deoxyribosyltransferase from lactobacillus delbrueckii stabilized through a double covalent/entrapment technologyRivero, Cintia WandaGarcia, Natalia SoledadFernández Lucas, JesúsBetancor, LorenaRomanelli, Gustavo PabloTrelles, Jorge AbelANTINEOPLASTIC DRUGBIOMIMETIC SILICACALCIUM ALGINATEENTRAPMENTENZYME IMMOBILIZATIONGLUTARALDEHYDEhttps://purl.org/becyt/ford/3.4https://purl.org/becyt/ford/3Nowadays, enzyme-mediated processes offer an eco-friendly and efficient alternative to the traditional multistep and environmentally harmful chemical processes. Herein we report the enzymatic synthesis of cladribine by a novel 2′-deoxyribosyltransferase (NDT)-based combined biocatalyst. To this end, Lactobacillus delbrueckii NDT (LdNDT) was successfully immobilized through a two-step immobilization methodology, including a covalent immobilization onto glutaraldehyde-activated biomimetic silica nanoparticles followed by biocatalyst entrapment in calcium alginate. The resulting immobilized derivative, SiGPEI 25000-LdNDT-Alg, displayed 98% retained activity and was shown to be active and stable in a broad range of pH (5–9) and temperature (30–60◦ C), but also displayed an extremely high reusability (up to 2100 reuses without negligible loss of activity) in the enzymatic production of cladribine. Finally, as a proof of concept, SiGPEI 25000-LdNDT-Alg was successfully employed in the green production of cladribine at mg scale.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: Garcia, Natalia Soledad. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; ArgentinaFil: Fernández Lucas, Jesús. Universidad Europea de Madrid; España. Universidad de la Costa; ColombiaFil: Betancor, Lorena. Universidad ORT Uruguay; UruguayFil: Romanelli, Gustavo Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Ciencias Aplicadas "Dr. Jorge J. Ronco". Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Ciencias Aplicadas; ArgentinaFil: Trelles, Jorge Abel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaMDPI AG2021-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/165857Rivero, Cintia Wanda; Garcia, Natalia Soledad; Fernández Lucas, Jesús; Betancor, Lorena; Romanelli, Gustavo Pablo; et al.; Green production of cladribine by using immobilized 2′-deoxyribosyltransferase from lactobacillus delbrueckii stabilized through a double covalent/entrapment technology; MDPI AG; Biomolecules; 11; 5; 4-2021; 657-6602218-273XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2218-273X/11/5/657info:eu-repo/semantics/altIdentifier/doi/10.3390/biom11050657info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:15:15Zoai:ri.conicet.gov.ar:11336/165857instacron: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 10:15:15.407CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Green production of cladribine by using immobilized 2′-deoxyribosyltransferase from lactobacillus delbrueckii stabilized through a double covalent/entrapment technology
title Green production of cladribine by using immobilized 2′-deoxyribosyltransferase from lactobacillus delbrueckii stabilized through a double covalent/entrapment technology
spellingShingle Green production of cladribine by using immobilized 2′-deoxyribosyltransferase from lactobacillus delbrueckii stabilized through a double covalent/entrapment technology
Rivero, Cintia Wanda
ANTINEOPLASTIC DRUG
BIOMIMETIC SILICA
CALCIUM ALGINATE
ENTRAPMENT
ENZYME IMMOBILIZATION
GLUTARALDEHYDE
title_short Green production of cladribine by using immobilized 2′-deoxyribosyltransferase from lactobacillus delbrueckii stabilized through a double covalent/entrapment technology
title_full Green production of cladribine by using immobilized 2′-deoxyribosyltransferase from lactobacillus delbrueckii stabilized through a double covalent/entrapment technology
title_fullStr Green production of cladribine by using immobilized 2′-deoxyribosyltransferase from lactobacillus delbrueckii stabilized through a double covalent/entrapment technology
title_full_unstemmed Green production of cladribine by using immobilized 2′-deoxyribosyltransferase from lactobacillus delbrueckii stabilized through a double covalent/entrapment technology
title_sort Green production of cladribine by using immobilized 2′-deoxyribosyltransferase from lactobacillus delbrueckii stabilized through a double covalent/entrapment technology
dc.creator.none.fl_str_mv Rivero, Cintia Wanda
Garcia, Natalia Soledad
Fernández Lucas, Jesús
Betancor, Lorena
Romanelli, Gustavo Pablo
Trelles, Jorge Abel
author Rivero, Cintia Wanda
author_facet Rivero, Cintia Wanda
Garcia, Natalia Soledad
Fernández Lucas, Jesús
Betancor, Lorena
Romanelli, Gustavo Pablo
Trelles, Jorge Abel
author_role author
author2 Garcia, Natalia Soledad
Fernández Lucas, Jesús
Betancor, Lorena
Romanelli, Gustavo Pablo
Trelles, Jorge Abel
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv ANTINEOPLASTIC DRUG
BIOMIMETIC SILICA
CALCIUM ALGINATE
ENTRAPMENT
ENZYME IMMOBILIZATION
GLUTARALDEHYDE
topic ANTINEOPLASTIC DRUG
BIOMIMETIC SILICA
CALCIUM ALGINATE
ENTRAPMENT
ENZYME IMMOBILIZATION
GLUTARALDEHYDE
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.4
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Nowadays, enzyme-mediated processes offer an eco-friendly and efficient alternative to the traditional multistep and environmentally harmful chemical processes. Herein we report the enzymatic synthesis of cladribine by a novel 2′-deoxyribosyltransferase (NDT)-based combined biocatalyst. To this end, Lactobacillus delbrueckii NDT (LdNDT) was successfully immobilized through a two-step immobilization methodology, including a covalent immobilization onto glutaraldehyde-activated biomimetic silica nanoparticles followed by biocatalyst entrapment in calcium alginate. The resulting immobilized derivative, SiGPEI 25000-LdNDT-Alg, displayed 98% retained activity and was shown to be active and stable in a broad range of pH (5–9) and temperature (30–60◦ C), but also displayed an extremely high reusability (up to 2100 reuses without negligible loss of activity) in the enzymatic production of cladribine. Finally, as a proof of concept, SiGPEI 25000-LdNDT-Alg was successfully employed in the green production of cladribine at mg scale.
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: Garcia, Natalia Soledad. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina
Fil: Fernández Lucas, Jesús. Universidad Europea de Madrid; España. Universidad de la Costa; Colombia
Fil: Betancor, Lorena. Universidad ORT Uruguay; Uruguay
Fil: Romanelli, Gustavo Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Ciencias Aplicadas "Dr. Jorge J. Ronco". Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Ciencias Aplicadas; Argentina
Fil: Trelles, Jorge Abel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description Nowadays, enzyme-mediated processes offer an eco-friendly and efficient alternative to the traditional multistep and environmentally harmful chemical processes. Herein we report the enzymatic synthesis of cladribine by a novel 2′-deoxyribosyltransferase (NDT)-based combined biocatalyst. To this end, Lactobacillus delbrueckii NDT (LdNDT) was successfully immobilized through a two-step immobilization methodology, including a covalent immobilization onto glutaraldehyde-activated biomimetic silica nanoparticles followed by biocatalyst entrapment in calcium alginate. The resulting immobilized derivative, SiGPEI 25000-LdNDT-Alg, displayed 98% retained activity and was shown to be active and stable in a broad range of pH (5–9) and temperature (30–60◦ C), but also displayed an extremely high reusability (up to 2100 reuses without negligible loss of activity) in the enzymatic production of cladribine. Finally, as a proof of concept, SiGPEI 25000-LdNDT-Alg was successfully employed in the green production of cladribine at mg scale.
publishDate 2021
dc.date.none.fl_str_mv 2021-04
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/11336/165857
Rivero, Cintia Wanda; Garcia, Natalia Soledad; Fernández Lucas, Jesús; Betancor, Lorena; Romanelli, Gustavo Pablo; et al.; Green production of cladribine by using immobilized 2′-deoxyribosyltransferase from lactobacillus delbrueckii stabilized through a double covalent/entrapment technology; MDPI AG; Biomolecules; 11; 5; 4-2021; 657-660
2218-273X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/165857
identifier_str_mv Rivero, Cintia Wanda; Garcia, Natalia Soledad; Fernández Lucas, Jesús; Betancor, Lorena; Romanelli, Gustavo Pablo; et al.; Green production of cladribine by using immobilized 2′-deoxyribosyltransferase from lactobacillus delbrueckii stabilized through a double covalent/entrapment technology; MDPI AG; Biomolecules; 11; 5; 4-2021; 657-660
2218-273X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2218-273X/11/5/657
info:eu-repo/semantics/altIdentifier/doi/10.3390/biom11050657
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
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score 13.069144

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