Imobilização de horseradish peroxidase em diferentes polianilinas

AUTOR(ES)
DATA DE PUBLICAÇÃO

2000

RESUMO

This work describes peroxidase immobilization on chemically synthesized polyaniline activated with polyglutaraldehyde. Five polyanilines with different ranges of oxidation, counter-íons and levels of ring substitution were synthesized and characterized. The polymers were then activated with polyglutaraldehyde to chemically bind the peroxidase. The best enzyme retention capacities were observed in those polymers with intermediate oxidation levels (PANIG, PANIG e PANIG). The polymer designated PANIG was used in immobilization optimization experiments. The highest retentions (25%) were obtained when the immobilization was made by adding 1,0 mL of 10mg mL peroxidase solution prepared in 0,1 mol L phosphate buffer, pH 6,0, to 5,0 mg of PANIG, and allowing the reaction to proceed for 2h at 4 °C. The kinetic parameters reveal that immobilization does not modify either the optimum pH (6-8 range) or the Kmap of the immobilized enzyme. However, immobilization increased thermal stability, stability in organic solvents and stability during storage. at room temperature and 4 °C. The system PANIG-HRP was used to construct a mini-reactor for flow injection analysis which was used for determination of hydrogen peroxide (linear range from 3.3 to 163.3 mmol L) and glucose (linear range from 2.0 to 3.0 mmol L). System stability and reprodutibility allowed its use for 1500 analysis. This leads to the conclusion that PANIG is a very good suport for peroxidase immobilization.

ASSUNTO(S)

peroxidade analise por injeção de fluxo

ACESSO AO ARTIGO

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