Immobilization of peroxidase onto magnetite modified polyaniline

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dc.creatorBarbosa, Eduardo Fernandes
dc.creatorMolina, Fernando Javier
dc.creatorLopes, Flavio Marques
dc.creatorGarcía-Ruíz, Pedro Antonio
dc.creatorCaramori, Samantha Salomão
dc.creatorFernanades, Kátia Flávia
dc.date.accessioned2018-10-03T14:52:58Z
dc.date.available2018-10-03T14:52:58Z
dc.date.issued2012
dc.description.abstractThe 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.pt_BR
dc.identifier.citationBARBOSA, Eduardo Fernandes et al . Immobilization of peroxidase onto magnetite modified polyaniline. The Scientific World Journal, London, v. 2012, p. 1-5, 2012.pt_BR
dc.identifier.doi10.1100/2012/716374
dc.identifier.urihttp://repositorio.bc.ufg.br/handle/ri/16113
dc.language.isoengpt_BR
dc.publisher.countryGra-bretanhapt_BR
dc.publisher.departmentInstituto de Ciências Biológicas - ICB (RG)pt_BR
dc.rightsAcesso Abertopt_BR
dc.titleImmobilization of peroxidase onto magnetite modified polyanilinept_BR
dc.typeArtigopt_BR

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