Immobilization of Peroxidase onto Magnetite Modified Polyaniline

The present study describes the immobilization of horseradish peroxidase (HRP) on magnetite-modified polyaniline (PANImG) activated with glutaraldehyde. After the optimization of the methodology, the immobilization of HRP on PANImG produced the same yield (25%) obtained for PANIG with an efficiency...

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Detalles Bibliográficos
Autores principales: Barbosa, Eduardo Fernandes, Molina, Fernando Javier, Lopes, Flavio Marques, García-Ruíz, Pedro Antonio, Caramori, Samantha Salomão, Fernandes, Kátia Flávia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Scientific World Journal 2012
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3319987/
https://www.ncbi.nlm.nih.gov/pubmed/22489198
http://dx.doi.org/10.1100/2012/716374
Descripción
Sumario:The present study describes the immobilization of horseradish peroxidase (HRP) on magnetite-modified polyaniline (PANImG) activated with glutaraldehyde. After the optimization of the methodology, the immobilization of HRP on PANImG produced the same yield (25%) obtained for PANIG with an efficiency of 100% (active protein). The optimum pH for immobilization was displaced by the effect of the partition of protons produced in the microenvironment by the magnetite. The tests of repeated use have shown that PANImG-HRP can be used for 13 cycles with maintenance of 50% of the initial activity.

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