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Immobilization of peroxidase onto magnetite modified polyaniline
Eduardo Fernandes Barbosa1, Fernando Javier Molina, Flavio Marques Lopes
1Laboratório de Química de Proteínas, Instituto de Ciências Biológicas, Universidade Federal de Goiás, Codigo Postal 131, 74001-970 Goiânia, GO, Brazil.
Abstract:
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.
