Green Production of Cladribine by Using Immobilized 20-Deoxyribosyltransferase from Lactobacillus delbrueckii Stabilized through a Double Covalent/Entrapment Technology

Autores
Rivero, Cintia Wanda; García, 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 20-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 glutaraldehydeactivated 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.
Centro de Investigación y Desarrollo en Ciencias Aplicadas
Materia
Ciencias Exactas
Biomimetic silica
Enzyme immobilization
Glutaraldehyde
Entrapment
Calcium alginate
Antineoplastic drug
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/118990
Acceder
id SEDICI_1452b173b660e034d145670b05be8d80
oai_identifier_str oai:sedici.unlp.edu.ar:10915/118990
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Green Production of Cladribine by Using Immobilized 20-Deoxyribosyltransferase from Lactobacillus delbrueckii Stabilized through a Double Covalent/Entrapment TechnologyRivero, Cintia WandaGarcía, Natalia SoledadFernández Lucas, JesúsBetancor, LorenaRomanelli, Gustavo PabloTrelles, Jorge AbelCiencias ExactasBiomimetic silicaEnzyme immobilizationGlutaraldehydeEntrapmentCalcium alginateAntineoplastic drugNowadays, 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 20-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 glutaraldehydeactivated 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.Centro de Investigación y Desarrollo en Ciencias Aplicadas2021info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://sedici.unlp.edu.ar/handle/10915/118990enginfo:eu-repo/semantics/altIdentifier/issn/2218-273Xinfo:eu-repo/semantics/altIdentifier/doi/10.3390/biom11050657info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:28:04Zoai:sedici.unlp.edu.ar:10915/118990Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:28:04.743SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Green Production of Cladribine by Using Immobilized 20-Deoxyribosyltransferase from Lactobacillus delbrueckii Stabilized through a Double Covalent/Entrapment Technology
title Green Production of Cladribine by Using Immobilized 20-Deoxyribosyltransferase from Lactobacillus delbrueckii Stabilized through a Double Covalent/Entrapment Technology
spellingShingle Green Production of Cladribine by Using Immobilized 20-Deoxyribosyltransferase from Lactobacillus delbrueckii Stabilized through a Double Covalent/Entrapment Technology
Rivero, Cintia Wanda
Ciencias Exactas
Biomimetic silica
Enzyme immobilization
Glutaraldehyde
Entrapment
Calcium alginate
Antineoplastic drug
title_short Green Production of Cladribine by Using Immobilized 20-Deoxyribosyltransferase from Lactobacillus delbrueckii Stabilized through a Double Covalent/Entrapment Technology
title_full Green Production of Cladribine by Using Immobilized 20-Deoxyribosyltransferase from Lactobacillus delbrueckii Stabilized through a Double Covalent/Entrapment Technology
title_fullStr Green Production of Cladribine by Using Immobilized 20-Deoxyribosyltransferase from Lactobacillus delbrueckii Stabilized through a Double Covalent/Entrapment Technology
title_full_unstemmed Green Production of Cladribine by Using Immobilized 20-Deoxyribosyltransferase from Lactobacillus delbrueckii Stabilized through a Double Covalent/Entrapment Technology
title_sort Green Production of Cladribine by Using Immobilized 20-Deoxyribosyltransferase from Lactobacillus delbrueckii Stabilized through a Double Covalent/Entrapment Technology
dc.creator.none.fl_str_mv Rivero, Cintia Wanda
García, Natalia Soledad
Fernández Lucas, Jesús
Betancor, Lorena
Romanelli, Gustavo Pablo
Trelles, Jorge Abel
author Rivero, Cintia Wanda
author_facet Rivero, Cintia Wanda
García, Natalia Soledad
Fernández Lucas, Jesús
Betancor, Lorena
Romanelli, Gustavo Pablo
Trelles, Jorge Abel
author_role author
author2 García, 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 Ciencias Exactas
Biomimetic silica
Enzyme immobilization
Glutaraldehyde
Entrapment
Calcium alginate
Antineoplastic drug
topic Ciencias Exactas
Biomimetic silica
Enzyme immobilization
Glutaraldehyde
Entrapment
Calcium alginate
Antineoplastic drug
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 20-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 glutaraldehydeactivated 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.
Centro de Investigación y Desarrollo en Ciencias Aplicadas
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 20-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 glutaraldehydeactivated 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
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/10915/118990
url http://sedici.unlp.edu.ar/handle/10915/118990
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/2218-273X
info:eu-repo/semantics/altIdentifier/doi/10.3390/biom11050657
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
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
_version_ 1844616158714527744
score 13.070432

Publicaciones similares