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
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author Barbosa, Eduardo Fernandes
Molina, Fernando Javier
Lopes, Flavio Marques
García-Ruíz, Pedro Antonio
Caramori, Samantha Salomão
Fernandes, Kátia Flávia
author_facet Barbosa, Eduardo Fernandes
Molina, Fernando Javier
Lopes, Flavio Marques
García-Ruíz, Pedro Antonio
Caramori, Samantha Salomão
Fernandes, Kátia Flávia
author_sort Barbosa, Eduardo Fernandes
collection PubMed
description 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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spelling pubmed-33199872012-04-09 Immobilization of Peroxidase onto Magnetite Modified Polyaniline Barbosa, Eduardo Fernandes Molina, Fernando Javier Lopes, Flavio Marques García-Ruíz, Pedro Antonio Caramori, Samantha Salomão Fernandes, Kátia Flávia ScientificWorldJournal Research Article 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. The Scientific World Journal 2012-03-12 /pmc/articles/PMC3319987/ /pubmed/22489198 http://dx.doi.org/10.1100/2012/716374 Text en Copyright © 2012 Eduardo Fernandes Barbosa et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Barbosa, Eduardo Fernandes
Molina, Fernando Javier
Lopes, Flavio Marques
García-Ruíz, Pedro Antonio
Caramori, Samantha Salomão
Fernandes, Kátia Flávia
Immobilization of Peroxidase onto Magnetite Modified Polyaniline
title Immobilization of Peroxidase onto Magnetite Modified Polyaniline
title_full Immobilization of Peroxidase onto Magnetite Modified Polyaniline
title_fullStr Immobilization of Peroxidase onto Magnetite Modified Polyaniline
title_full_unstemmed Immobilization of Peroxidase onto Magnetite Modified Polyaniline
title_short Immobilization of Peroxidase onto Magnetite Modified Polyaniline
title_sort immobilization of peroxidase onto magnetite modified polyaniline
topic Research Article
url 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
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