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dc.contributor.author
Horst, María Fernanda  
dc.contributor.author
Rueda, Elsa Haydee  
dc.contributor.author
Ferreira, María Luján  
dc.date.available
2019-07-12T19:41:25Z  
dc.date.issued
2006-05-03  
dc.identifier.citation
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  
dc.identifier.issn
0141-0229  
dc.identifier.uri
http://hdl.handle.net/11336/79508  
dc.description.abstract
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).  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Elsevier Science Inc  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
Catalase  
dc.subject
Enzymatic  
dc.subject
Hydrogen Peroxide  
dc.subject
Magnetite  
dc.subject
Supported Catalase  
dc.subject.classification
Química Inorgánica y Nuclear  
dc.subject.classification
Ciencias Químicas  
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS  
dc.title
Activity of magnetite-immobilized catalase in hydrogen peroxide decomposition  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2019-06-11T19:34:29Z  
dc.journal.volume
38  
dc.journal.number
7  
dc.journal.pagination
1005-1012  
dc.journal.pais
Estados Unidos  
dc.journal.ciudad
Nueva York  
dc.description.fil
Fil: Horst, María Fernanda. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Sur. Departamento de Química; Argentina  
dc.description.fil
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  
dc.description.fil
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  
dc.journal.title
Enzyme and Microbial Technology  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0141022905004059  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.enzmictec.2005.08.035