Activity of magnetite-immobilized catalase in hydrogen peroxide decomposition

Autores
Horst, María Fernanda; Rueda, Elsa Haydee; Ferreira, María Luján
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The present work analyzes the activity in decomposition of H 2O2 using magnetite-immobilized catalase. The support of catalase is a glutaraldehyde-treated magnetite (Fe3O4). The data obtained in the H2O2 decomposition are analyzed. The fitting of the initial rate of the H2O2 decomposition versus hydrogen peroxide concentration data is discussed using a specific program for enzyme kinetics modeling (Leonora). The free catalase from Aspergillus niger (3.5 or 10 U/mL) does not show substrate inactivation up to 0.4 M H2O2. The immobilized catalase at low catalyst concentration shows substrate inhibition. Using 1 mg/mL of supported catalase the predicted maximum activity is higher than in the case of the free catalase at similar catalase concentration, although the optimum temperature is lower (40°C versus 60°C).
Fil: Horst, María Fernanda. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Sur. Departamento de Química; Argentina
Fil: Rueda, Elsa Haydee. 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
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
Catalase
Enzymatic
Hydrogen Peroxide
Magnetite
Supported Catalase
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:11336/79508
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/79508
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Activity of magnetite-immobilized catalase in hydrogen peroxide decompositionHorst, María FernandaRueda, Elsa HaydeeFerreira, María LujánCatalaseEnzymaticHydrogen PeroxideMagnetiteSupported Catalasehttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The present work analyzes the activity in decomposition of H 2O2 using magnetite-immobilized catalase. The support of catalase is a glutaraldehyde-treated magnetite (Fe3O4). The data obtained in the H2O2 decomposition are analyzed. The fitting of the initial rate of the H2O2 decomposition versus hydrogen peroxide concentration data is discussed using a specific program for enzyme kinetics modeling (Leonora). The free catalase from Aspergillus niger (3.5 or 10 U/mL) does not show substrate inactivation up to 0.4 M H2O2. The immobilized catalase at low catalyst concentration shows substrate inhibition. Using 1 mg/mL of supported catalase the predicted maximum activity is higher than in the case of the free catalase at similar catalase concentration, although the optimum temperature is lower (40°C versus 60°C).Fil: Horst, María Fernanda. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Sur. Departamento de Química; ArgentinaFil: Rueda, Elsa Haydee. 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; 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; ArgentinaElsevier Science Inc2006-05-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/79508Horst, María Fernanda; Rueda, Elsa Haydee; Ferreira, María Luján; Activity of magnetite-immobilized catalase in hydrogen peroxide decomposition; Elsevier Science Inc; Enzyme and Microbial Technology; 38; 7; 3-5-2006; 1005-10120141-0229CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0141022905004059info:eu-repo/semantics/altIdentifier/doi/10.1016/j.enzmictec.2005.08.035info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:05:30Zoai:ri.conicet.gov.ar:11336/79508instacron: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:34982025-09-10 13:05:31.172CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Activity of magnetite-immobilized catalase in hydrogen peroxide decomposition
title Activity of magnetite-immobilized catalase in hydrogen peroxide decomposition
spellingShingle Activity of magnetite-immobilized catalase in hydrogen peroxide decomposition
Horst, María Fernanda
Catalase
Enzymatic
Hydrogen Peroxide
Magnetite
Supported Catalase
title_short Activity of magnetite-immobilized catalase in hydrogen peroxide decomposition
title_full Activity of magnetite-immobilized catalase in hydrogen peroxide decomposition
title_fullStr Activity of magnetite-immobilized catalase in hydrogen peroxide decomposition
title_full_unstemmed Activity of magnetite-immobilized catalase in hydrogen peroxide decomposition
title_sort Activity of magnetite-immobilized catalase in hydrogen peroxide decomposition
dc.creator.none.fl_str_mv Horst, María Fernanda
Rueda, Elsa Haydee
Ferreira, María Luján
author Horst, María Fernanda
author_facet Horst, María Fernanda
Rueda, Elsa Haydee
Ferreira, María Luján
author_role author
author2 Rueda, Elsa Haydee
Ferreira, María Luján
author2_role author
author
dc.subject.none.fl_str_mv Catalase
Enzymatic
Hydrogen Peroxide
Magnetite
Supported Catalase
topic Catalase
Enzymatic
Hydrogen Peroxide
Magnetite
Supported Catalase
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The present work analyzes the activity in decomposition of H 2O2 using magnetite-immobilized catalase. The support of catalase is a glutaraldehyde-treated magnetite (Fe3O4). The data obtained in the H2O2 decomposition are analyzed. The fitting of the initial rate of the H2O2 decomposition versus hydrogen peroxide concentration data is discussed using a specific program for enzyme kinetics modeling (Leonora). The free catalase from Aspergillus niger (3.5 or 10 U/mL) does not show substrate inactivation up to 0.4 M H2O2. The immobilized catalase at low catalyst concentration shows substrate inhibition. Using 1 mg/mL of supported catalase the predicted maximum activity is higher than in the case of the free catalase at similar catalase concentration, although the optimum temperature is lower (40°C versus 60°C).
Fil: Horst, María Fernanda. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Sur. Departamento de Química; Argentina
Fil: Rueda, Elsa Haydee. 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
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 The present work analyzes the activity in decomposition of H 2O2 using magnetite-immobilized catalase. The support of catalase is a glutaraldehyde-treated magnetite (Fe3O4). The data obtained in the H2O2 decomposition are analyzed. The fitting of the initial rate of the H2O2 decomposition versus hydrogen peroxide concentration data is discussed using a specific program for enzyme kinetics modeling (Leonora). The free catalase from Aspergillus niger (3.5 or 10 U/mL) does not show substrate inactivation up to 0.4 M H2O2. The immobilized catalase at low catalyst concentration shows substrate inhibition. Using 1 mg/mL of supported catalase the predicted maximum activity is higher than in the case of the free catalase at similar catalase concentration, although the optimum temperature is lower (40°C versus 60°C).
publishDate 2006
dc.date.none.fl_str_mv 2006-05-03
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/11336/79508
Horst, María Fernanda; Rueda, Elsa Haydee; Ferreira, María Luján; Activity of magnetite-immobilized catalase in hydrogen peroxide decomposition; Elsevier Science Inc; Enzyme and Microbial Technology; 38; 7; 3-5-2006; 1005-1012
0141-0229
CONICET Digital
CONICET
url http://hdl.handle.net/11336/79508
identifier_str_mv Horst, María Fernanda; Rueda, Elsa Haydee; Ferreira, María Luján; Activity of magnetite-immobilized catalase in hydrogen peroxide decomposition; Elsevier Science Inc; Enzyme and Microbial Technology; 38; 7; 3-5-2006; 1005-1012
0141-0229
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://www.sciencedirect.com/science/article/pii/S0141022905004059
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.enzmictec.2005.08.035
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
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science Inc
publisher.none.fl_str_mv Elsevier Science Inc
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
_version_ 1842980205696647168
score 13.004268

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