Immobilization of Aspergillus niger lipase on chitosan-coated magnetic nanoparticles using two covalent-binding methods

Autores
Osuna, Yolanda; Sandoval, José; Saade, Hened; López, Raúl G.; Martinez, José L.; Colunga, Edith M.; de la Cruz, Gabriela; Segura, Elda P.; Arevalo, Fernando Javier; Zon, María Alicia; Fernandez, Hector; Ilyina, Anna
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Aspergillus niger lipase immobilization by covalent binding on chitosan-coated magnetic nanoparticles (CMNP), obtained by one-step co-precipitation, was studied. Hydroxyl and amino groups of support were activated using glycidol and glutaraldehyde, respectively. Fourier transform infrared spectrometry, high-resolution transmission electron microscopy and thermogravimetric analysis confirmed reaction of these coupling agents with the enzyme and achievement of a successful immobilization. The derivatives showed activities of 309.5 ± 2.0 and 266.2 ± 2.8 U (g support)(-1) for the CMNP treated with glutaraldehyde and with glycidol, respectively. Immobilization enhanced the enzyme stability against changes of pH and temperature, compared to free lipase. Furthermore, the kinetic parameters K m and V max were determined for the free and immobilized enzyme. K m value quantified for enzyme immobilized by means of glutaraldehyde was 1.7 times lowers than for free lipase. High storage stability during 50 days was observed in the immobilized derivatives. Finally, immobilized derivatives retained above 80% of their initial activity after 15 hydrolytic cycles. The immobilized enzyme can be applied in various biotechnological processes involving magnetic separation.
Fil: Osuna, Yolanda. Universidad Autónoma de Coahuila; México
Fil: Sandoval, José. Universidad Autónoma de Coahuila; México
Fil: Saade, Hened. Centro de Investigación en Química Aplicada; México
Fil: López, Raúl G.. Centro de Investigación en Química Aplicada; México
Fil: Martinez, José L.. Universidad Autónoma de Coahuila; México
Fil: Colunga, Edith M.. Universidad Autónoma de Coahuila; México
Fil: de la Cruz, Gabriela. Universidad Autónoma de Coahuila; México
Fil: Segura, Elda P.. Universidad Autónoma de Coahuila; México
Fil: Arevalo, Fernando Javier. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Departamento de Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Zon, María Alicia. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Departamento de Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Fernandez, Hector. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Departamento de Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Ilyina, Anna. Universidad Autónoma de Coahuila; México
Materia
A. Niger Lipase
Immovilization On Magnetic Nanoparticles Coated with Chitosan
Glycidol And Glutaraldehyde as Coupling Agents
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:11336/39866

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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Immobilization of Aspergillus niger lipase on chitosan-coated magnetic nanoparticles using two covalent-binding methodsOsuna, YolandaSandoval, JoséSaade, HenedLópez, Raúl G.Martinez, José L.Colunga, Edith M.de la Cruz, GabrielaSegura, Elda P.Arevalo, Fernando JavierZon, María AliciaFernandez, HectorIlyina, AnnaA. Niger LipaseImmovilization On Magnetic Nanoparticles Coated with ChitosanGlycidol And Glutaraldehyde as Coupling Agentshttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Aspergillus niger lipase immobilization by covalent binding on chitosan-coated magnetic nanoparticles (CMNP), obtained by one-step co-precipitation, was studied. Hydroxyl and amino groups of support were activated using glycidol and glutaraldehyde, respectively. Fourier transform infrared spectrometry, high-resolution transmission electron microscopy and thermogravimetric analysis confirmed reaction of these coupling agents with the enzyme and achievement of a successful immobilization. The derivatives showed activities of 309.5 ± 2.0 and 266.2 ± 2.8 U (g support)(-1) for the CMNP treated with glutaraldehyde and with glycidol, respectively. Immobilization enhanced the enzyme stability against changes of pH and temperature, compared to free lipase. Furthermore, the kinetic parameters K m and V max were determined for the free and immobilized enzyme. K m value quantified for enzyme immobilized by means of glutaraldehyde was 1.7 times lowers than for free lipase. High storage stability during 50 days was observed in the immobilized derivatives. Finally, immobilized derivatives retained above 80% of their initial activity after 15 hydrolytic cycles. The immobilized enzyme can be applied in various biotechnological processes involving magnetic separation.Fil: Osuna, Yolanda. Universidad Autónoma de Coahuila; MéxicoFil: Sandoval, José. Universidad Autónoma de Coahuila; MéxicoFil: Saade, Hened. Centro de Investigación en Química Aplicada; MéxicoFil: López, Raúl G.. Centro de Investigación en Química Aplicada; MéxicoFil: Martinez, José L.. Universidad Autónoma de Coahuila; MéxicoFil: Colunga, Edith M.. Universidad Autónoma de Coahuila; MéxicoFil: de la Cruz, Gabriela. Universidad Autónoma de Coahuila; MéxicoFil: Segura, Elda P.. Universidad Autónoma de Coahuila; MéxicoFil: Arevalo, Fernando Javier. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Departamento de Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Zon, María Alicia. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Departamento de Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Fernandez, Hector. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Departamento de Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Ilyina, Anna. Universidad Autónoma de Coahuila; MéxicoSpringer2015-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/39866Osuna, Yolanda; Sandoval, José; Saade, Hened; López, Raúl G.; Martinez, José L.; et al.; Immobilization of Aspergillus niger lipase on chitosan-coated magnetic nanoparticles using two covalent-binding methods; Springer; Bioprocess and biosystems engineering; 38; 8; 8-2015; 1437-14451615-75911615-7605CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1007/s00449-015-1385-8info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs00449-015-1385-8info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:40:21Zoai:ri.conicet.gov.ar:11336/39866instacron: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 09:40:21.396CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Immobilization of Aspergillus niger lipase on chitosan-coated magnetic nanoparticles using two covalent-binding methods
title Immobilization of Aspergillus niger lipase on chitosan-coated magnetic nanoparticles using two covalent-binding methods
spellingShingle Immobilization of Aspergillus niger lipase on chitosan-coated magnetic nanoparticles using two covalent-binding methods
Osuna, Yolanda
A. Niger Lipase
Immovilization On Magnetic Nanoparticles Coated with Chitosan
Glycidol And Glutaraldehyde as Coupling Agents
title_short Immobilization of Aspergillus niger lipase on chitosan-coated magnetic nanoparticles using two covalent-binding methods
title_full Immobilization of Aspergillus niger lipase on chitosan-coated magnetic nanoparticles using two covalent-binding methods
title_fullStr Immobilization of Aspergillus niger lipase on chitosan-coated magnetic nanoparticles using two covalent-binding methods
title_full_unstemmed Immobilization of Aspergillus niger lipase on chitosan-coated magnetic nanoparticles using two covalent-binding methods
title_sort Immobilization of Aspergillus niger lipase on chitosan-coated magnetic nanoparticles using two covalent-binding methods
dc.creator.none.fl_str_mv Osuna, Yolanda
Sandoval, José
Saade, Hened
López, Raúl G.
Martinez, José L.
Colunga, Edith M.
de la Cruz, Gabriela
Segura, Elda P.
Arevalo, Fernando Javier
Zon, María Alicia
Fernandez, Hector
Ilyina, Anna
author Osuna, Yolanda
author_facet Osuna, Yolanda
Sandoval, José
Saade, Hened
López, Raúl G.
Martinez, José L.
Colunga, Edith M.
de la Cruz, Gabriela
Segura, Elda P.
Arevalo, Fernando Javier
Zon, María Alicia
Fernandez, Hector
Ilyina, Anna
author_role author
author2 Sandoval, José
Saade, Hened
López, Raúl G.
Martinez, José L.
Colunga, Edith M.
de la Cruz, Gabriela
Segura, Elda P.
Arevalo, Fernando Javier
Zon, María Alicia
Fernandez, Hector
Ilyina, Anna
author2_role author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv A. Niger Lipase
Immovilization On Magnetic Nanoparticles Coated with Chitosan
Glycidol And Glutaraldehyde as Coupling Agents
topic A. Niger Lipase
Immovilization On Magnetic Nanoparticles Coated with Chitosan
Glycidol And Glutaraldehyde as Coupling Agents
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Aspergillus niger lipase immobilization by covalent binding on chitosan-coated magnetic nanoparticles (CMNP), obtained by one-step co-precipitation, was studied. Hydroxyl and amino groups of support were activated using glycidol and glutaraldehyde, respectively. Fourier transform infrared spectrometry, high-resolution transmission electron microscopy and thermogravimetric analysis confirmed reaction of these coupling agents with the enzyme and achievement of a successful immobilization. The derivatives showed activities of 309.5 ± 2.0 and 266.2 ± 2.8 U (g support)(-1) for the CMNP treated with glutaraldehyde and with glycidol, respectively. Immobilization enhanced the enzyme stability against changes of pH and temperature, compared to free lipase. Furthermore, the kinetic parameters K m and V max were determined for the free and immobilized enzyme. K m value quantified for enzyme immobilized by means of glutaraldehyde was 1.7 times lowers than for free lipase. High storage stability during 50 days was observed in the immobilized derivatives. Finally, immobilized derivatives retained above 80% of their initial activity after 15 hydrolytic cycles. The immobilized enzyme can be applied in various biotechnological processes involving magnetic separation.
Fil: Osuna, Yolanda. Universidad Autónoma de Coahuila; México
Fil: Sandoval, José. Universidad Autónoma de Coahuila; México
Fil: Saade, Hened. Centro de Investigación en Química Aplicada; México
Fil: López, Raúl G.. Centro de Investigación en Química Aplicada; México
Fil: Martinez, José L.. Universidad Autónoma de Coahuila; México
Fil: Colunga, Edith M.. Universidad Autónoma de Coahuila; México
Fil: de la Cruz, Gabriela. Universidad Autónoma de Coahuila; México
Fil: Segura, Elda P.. Universidad Autónoma de Coahuila; México
Fil: Arevalo, Fernando Javier. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Departamento de Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Zon, María Alicia. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Departamento de Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Fernandez, Hector. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Departamento de Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Ilyina, Anna. Universidad Autónoma de Coahuila; México
description Aspergillus niger lipase immobilization by covalent binding on chitosan-coated magnetic nanoparticles (CMNP), obtained by one-step co-precipitation, was studied. Hydroxyl and amino groups of support were activated using glycidol and glutaraldehyde, respectively. Fourier transform infrared spectrometry, high-resolution transmission electron microscopy and thermogravimetric analysis confirmed reaction of these coupling agents with the enzyme and achievement of a successful immobilization. The derivatives showed activities of 309.5 ± 2.0 and 266.2 ± 2.8 U (g support)(-1) for the CMNP treated with glutaraldehyde and with glycidol, respectively. Immobilization enhanced the enzyme stability against changes of pH and temperature, compared to free lipase. Furthermore, the kinetic parameters K m and V max were determined for the free and immobilized enzyme. K m value quantified for enzyme immobilized by means of glutaraldehyde was 1.7 times lowers than for free lipase. High storage stability during 50 days was observed in the immobilized derivatives. Finally, immobilized derivatives retained above 80% of their initial activity after 15 hydrolytic cycles. The immobilized enzyme can be applied in various biotechnological processes involving magnetic separation.
publishDate 2015
dc.date.none.fl_str_mv 2015-08
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/11336/39866
Osuna, Yolanda; Sandoval, José; Saade, Hened; López, Raúl G.; Martinez, José L.; et al.; Immobilization of Aspergillus niger lipase on chitosan-coated magnetic nanoparticles using two covalent-binding methods; Springer; Bioprocess and biosystems engineering; 38; 8; 8-2015; 1437-1445
1615-7591
1615-7605
CONICET Digital
CONICET
url http://hdl.handle.net/11336/39866
identifier_str_mv Osuna, Yolanda; Sandoval, José; Saade, Hened; López, Raúl G.; Martinez, José L.; et al.; Immobilization of Aspergillus niger lipase on chitosan-coated magnetic nanoparticles using two covalent-binding methods; Springer; Bioprocess and biosystems engineering; 38; 8; 8-2015; 1437-1445
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/doi/10.1007/s00449-015-1385-8
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs00449-015-1385-8
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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