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

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,...

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Autores principales: Rivero, Cintia Wanda, García, Natalia Soledad, Fernández Lucas, Jesús, Betancor, Lorena, Romanelli, Gustavo Pablo, Trelles, Jorge Abel
Formato: Articulo
Lenguaje:Inglés
Publicado: 2021
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Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/118990
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id I19-R120-10915-118990
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Exactas
Biomimetic silica
Enzyme immobilization
Glutaraldehyde
Entrapment
Calcium alginate
Antineoplastic drug
spellingShingle Ciencias Exactas
Biomimetic silica
Enzyme immobilization
Glutaraldehyde
Entrapment
Calcium alginate
Antineoplastic drug
Rivero, Cintia Wanda
García, Natalia Soledad
Fernández Lucas, Jesús
Betancor, Lorena
Romanelli, Gustavo Pablo
Trelles, Jorge Abel
Green Production of Cladribine by Using Immobilized 20-Deoxyribosyltransferase from Lactobacillus delbrueckii Stabilized through a Double Covalent/Entrapment Technology
topic_facet Ciencias Exactas
Biomimetic silica
Enzyme immobilization
Glutaraldehyde
Entrapment
Calcium alginate
Antineoplastic drug
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.
format Articulo
Articulo
author Rivero, Cintia Wanda
García, Natalia Soledad
Fernández Lucas, Jesús
Betancor, Lorena
Romanelli, Gustavo Pablo
Trelles, Jorge Abel
author_facet Rivero, Cintia Wanda
García, Natalia Soledad
Fernández Lucas, Jesús
Betancor, Lorena
Romanelli, Gustavo Pablo
Trelles, Jorge Abel
author_sort Rivero, Cintia Wanda
title Green Production of Cladribine by Using Immobilized 20-Deoxyribosyltransferase from Lactobacillus delbrueckii Stabilized through a Double Covalent/Entrapment Technology
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
publishDate 2021
url http://sedici.unlp.edu.ar/handle/10915/118990
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