Immobilization of Peroxidase onto Magnetite Modified Polyaniline
Author(s) -
Eduardo Fernandes Barbosa,
Fernando Javier Molina,
Flávio Marques Lopes,
Pedro Antonio Garcı́a-Ruiz,
Samantha Salomão Caramori,
Kátia Flávia Fernandes
Publication year - 2012
Publication title -
the scientific world journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.453
H-Index - 93
eISSN - 2356-6140
pISSN - 1537-744X
DOI - 10.1100/2012/716374
Subject(s) - horseradish peroxidase , polyaniline , glutaraldehyde , magnetite , peroxidase , chemistry , nuclear chemistry , chemical engineering , chromatography , materials science , biochemistry , enzyme , polymer , organic chemistry , engineering , metallurgy , polymerization
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom