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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/39866
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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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1844613276966584320 |
score |
13.070432 |