Immobilization of CALB on lysine-modified magnetic nanoparticles: influence of the immobilization protocol

Autores
Nicolás, Paula; Lassalle, Verónica Leticia; Ferreira, María Luján
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Magnetic biocatalysts offer enormous advantages over traditional ones. Their ability to be isolated by means of a magnet, in combination with their extensive reuse possibilities, makes them highly attractive and competitive from the commercial point of view. In this work, magnetic biocatalysts were prepared by immobilization of Candida antarctica Lipase B (E.C. 3.1.1.3, CALB) on magnetite–lysine nanoparticles. Two methodologies were explored tending to find the optimal biocatalyst in terms of its practical implementation: I—physical adsorption of CALB followed by cross-linking, and II—covalent coupling of the lipase on the nanoparticles surface. Both procedures involved the use of glutaraldehyde (GLUT) as cross-linker or coupling agent, respectively. A range of GLUT concentrations was evaluated in method I and the optimum one, in terms of efficiency and operational stability, was chosen to induce the covalent linkage CALB-support in method II. The chosen test reaction was solvent-free ethyl oleate synthesis. Method I produced operationally unstable catalysts that deactivated totally in four to six cycles. On the other hand, covalently attached CALB (method II) preserved 60% of its initial activity after eight cycles and also retained 90% of its initial activity along 6 weeks in storage. CALB immobilization by covalent linkage using controlled GLUT concentration appears as the optimum methodology to asses efficient and stable biocatalysts. The materials prepared within this work may be competitive with commercially available biocatalysts.
Fil: Nicolás, Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; Argentina
Fil: Lassalle, Verónica Leticia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; Argentina
Fil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Materia
Calb
Glutaraldehyde
Immobilized Calb
Magnetic Nanoparticles
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/56516
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/56516
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Immobilization of CALB on lysine-modified magnetic nanoparticles: influence of the immobilization protocolNicolás, PaulaLassalle, Verónica LeticiaFerreira, María LujánCalbGlutaraldehydeImmobilized CalbMagnetic Nanoparticleshttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2Magnetic biocatalysts offer enormous advantages over traditional ones. Their ability to be isolated by means of a magnet, in combination with their extensive reuse possibilities, makes them highly attractive and competitive from the commercial point of view. In this work, magnetic biocatalysts were prepared by immobilization of Candida antarctica Lipase B (E.C. 3.1.1.3, CALB) on magnetite–lysine nanoparticles. Two methodologies were explored tending to find the optimal biocatalyst in terms of its practical implementation: I—physical adsorption of CALB followed by cross-linking, and II—covalent coupling of the lipase on the nanoparticles surface. Both procedures involved the use of glutaraldehyde (GLUT) as cross-linker or coupling agent, respectively. A range of GLUT concentrations was evaluated in method I and the optimum one, in terms of efficiency and operational stability, was chosen to induce the covalent linkage CALB-support in method II. The chosen test reaction was solvent-free ethyl oleate synthesis. Method I produced operationally unstable catalysts that deactivated totally in four to six cycles. On the other hand, covalently attached CALB (method II) preserved 60% of its initial activity after eight cycles and also retained 90% of its initial activity along 6 weeks in storage. CALB immobilization by covalent linkage using controlled GLUT concentration appears as the optimum methodology to asses efficient and stable biocatalysts. The materials prepared within this work may be competitive with commercially available biocatalysts.Fil: Nicolás, Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; ArgentinaFil: Lassalle, Verónica Leticia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; ArgentinaFil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; ArgentinaSpringer2017-10-13info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/56516Nicolás, Paula; Lassalle, Verónica Leticia; Ferreira, María Luján; Immobilization of CALB on lysine-modified magnetic nanoparticles: influence of the immobilization protocol; Springer; Bioprocess And Biosystems Engineering; 41; 2; 13-10-2017; 171-1841615-75911615-7605CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs00449-017-1855-2info:eu-repo/semantics/altIdentifier/doi/10.1007/s00449-017-1855-2info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:43:45Zoai:ri.conicet.gov.ar:11336/56516instacron: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:34982025-09-03 09:43:45.555CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Immobilization of CALB on lysine-modified magnetic nanoparticles: influence of the immobilization protocol
title Immobilization of CALB on lysine-modified magnetic nanoparticles: influence of the immobilization protocol
spellingShingle Immobilization of CALB on lysine-modified magnetic nanoparticles: influence of the immobilization protocol
Nicolás, Paula
Calb
Glutaraldehyde
Immobilized Calb
Magnetic Nanoparticles
title_short Immobilization of CALB on lysine-modified magnetic nanoparticles: influence of the immobilization protocol
title_full Immobilization of CALB on lysine-modified magnetic nanoparticles: influence of the immobilization protocol
title_fullStr Immobilization of CALB on lysine-modified magnetic nanoparticles: influence of the immobilization protocol
title_full_unstemmed Immobilization of CALB on lysine-modified magnetic nanoparticles: influence of the immobilization protocol
title_sort Immobilization of CALB on lysine-modified magnetic nanoparticles: influence of the immobilization protocol
dc.creator.none.fl_str_mv Nicolás, Paula
Lassalle, Verónica Leticia
Ferreira, María Luján
author Nicolás, Paula
author_facet Nicolás, Paula
Lassalle, Verónica Leticia
Ferreira, María Luján
author_role author
author2 Lassalle, Verónica Leticia
Ferreira, María Luján
author2_role author
author
dc.subject.none.fl_str_mv Calb
Glutaraldehyde
Immobilized Calb
Magnetic Nanoparticles
topic Calb
Glutaraldehyde
Immobilized Calb
Magnetic Nanoparticles
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Magnetic biocatalysts offer enormous advantages over traditional ones. Their ability to be isolated by means of a magnet, in combination with their extensive reuse possibilities, makes them highly attractive and competitive from the commercial point of view. In this work, magnetic biocatalysts were prepared by immobilization of Candida antarctica Lipase B (E.C. 3.1.1.3, CALB) on magnetite–lysine nanoparticles. Two methodologies were explored tending to find the optimal biocatalyst in terms of its practical implementation: I—physical adsorption of CALB followed by cross-linking, and II—covalent coupling of the lipase on the nanoparticles surface. Both procedures involved the use of glutaraldehyde (GLUT) as cross-linker or coupling agent, respectively. A range of GLUT concentrations was evaluated in method I and the optimum one, in terms of efficiency and operational stability, was chosen to induce the covalent linkage CALB-support in method II. The chosen test reaction was solvent-free ethyl oleate synthesis. Method I produced operationally unstable catalysts that deactivated totally in four to six cycles. On the other hand, covalently attached CALB (method II) preserved 60% of its initial activity after eight cycles and also retained 90% of its initial activity along 6 weeks in storage. CALB immobilization by covalent linkage using controlled GLUT concentration appears as the optimum methodology to asses efficient and stable biocatalysts. The materials prepared within this work may be competitive with commercially available biocatalysts.
Fil: Nicolás, Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; Argentina
Fil: Lassalle, Verónica Leticia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; Argentina
Fil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
description Magnetic biocatalysts offer enormous advantages over traditional ones. Their ability to be isolated by means of a magnet, in combination with their extensive reuse possibilities, makes them highly attractive and competitive from the commercial point of view. In this work, magnetic biocatalysts were prepared by immobilization of Candida antarctica Lipase B (E.C. 3.1.1.3, CALB) on magnetite–lysine nanoparticles. Two methodologies were explored tending to find the optimal biocatalyst in terms of its practical implementation: I—physical adsorption of CALB followed by cross-linking, and II—covalent coupling of the lipase on the nanoparticles surface. Both procedures involved the use of glutaraldehyde (GLUT) as cross-linker or coupling agent, respectively. A range of GLUT concentrations was evaluated in method I and the optimum one, in terms of efficiency and operational stability, was chosen to induce the covalent linkage CALB-support in method II. The chosen test reaction was solvent-free ethyl oleate synthesis. Method I produced operationally unstable catalysts that deactivated totally in four to six cycles. On the other hand, covalently attached CALB (method II) preserved 60% of its initial activity after eight cycles and also retained 90% of its initial activity along 6 weeks in storage. CALB immobilization by covalent linkage using controlled GLUT concentration appears as the optimum methodology to asses efficient and stable biocatalysts. The materials prepared within this work may be competitive with commercially available biocatalysts.
publishDate 2017
dc.date.none.fl_str_mv 2017-10-13
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/11336/56516
Nicolás, Paula; Lassalle, Verónica Leticia; Ferreira, María Luján; Immobilization of CALB on lysine-modified magnetic nanoparticles: influence of the immobilization protocol; Springer; Bioprocess And Biosystems Engineering; 41; 2; 13-10-2017; 171-184
1615-7591
1615-7605
CONICET Digital
CONICET
url http://hdl.handle.net/11336/56516
identifier_str_mv Nicolás, Paula; Lassalle, Verónica Leticia; Ferreira, María Luján; Immobilization of CALB on lysine-modified magnetic nanoparticles: influence of the immobilization protocol; Springer; Bioprocess And Biosystems Engineering; 41; 2; 13-10-2017; 171-184
1615-7591
1615-7605
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://link.springer.com/article/10.1007%2Fs00449-017-1855-2
info:eu-repo/semantics/altIdentifier/doi/10.1007/s00449-017-1855-2
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Springer
publisher.none.fl_str_mv Springer
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 13.13397

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