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The Scientific World Journal
Volume 2012, Article ID 716374, 5 pages
Research Article

Immobilization of Peroxidase onto Magnetite Modified Polyaniline

1Laboratório de Química de Proteínas, Instituto de Ciências Biológicas, Universidade Federal de Goiás, Codigo Postal 131, 74001-970 Goiânia, GO, Brazil
2Grupo de Química de Carboydratos y Biotecnología de Alimentos, Departamento de Química Orgánica, Universidad de Murcia, Campus Espinardo, 34100 Murcia, Spain
3Unidade Universitária de Ciências Exatas e Tecnológicas, Campus Dr. Henrique Santillo, Universidade Estadual de Goiás, Rodovia BR 153 Km 98, Codigo Postal 459, 75132-903 Anápolis, GO, Brazil

Received 1 November 2011; Accepted 29 November 2011

Academic Editors: P. Andrade and C. Mateo

Copyright © 2012 Eduardo Fernandes Barbosa et al. 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.


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.