INIFTA   05425
INSTITUTO DE INVESTIGACIONES FISICO-QUIMICAS TEORICAS Y APLICADAS
Unidad Ejecutora - UE
artículos
Título:
Horseradish peroxidase and hematin as biocatalysts for alizarin degradation using hydrogen peroxide
Autor/es:
SILVINA PIRILLO; FERNANDO S. GARCÍA EINSCHLAG; ELSA H. RUEDA; MARÍA LUJÁN FERREIRA
Revista:
INDUSTRIAL & ENGINEERING CHEMICAL RESEARCH
Editorial:
AMER CHEMICAL SOC
Referencias:
Año: 2010
ISSN:
0888-5885
Resumen:
Degradation of organic dyes from the textile industry is a matter of enormous environmental concern. The horseradish peroxidase enzyme is known for its capacity to remove phenolic compounds and aromatic amines from aqueous solutions and also to decolorize textile effluents. This study evaluates the potential of the both enzyme horseradish peroxidase (HRP) and its biomimetic hematin in the decolorization of alizarin. We describe an UV-visible study of alizarin elimination from aqueous solutions by polymerization using HRP or hematin as catalysts, hydrogen peroxide as oxidant, and HCl as coagulant. The effects of the initial dye concentration and the temperature on the decolorization efficiencies, attained with each catalyst after 2 h of reaction time, are reported. Alizarin removal with HRP/H2O2 achieved the highest elimination level (88%) when the dye concentration was 50 mg/L. At the same dye concentration a degradation of 97% was obtained using hematin as biocatalyst. A comparative analysis of time-resolved spectra and dissolved oxygen profiles is presented. The oxygen profiles found for hematin/H2O2/alizarin and HRP/H2O2/alizarin systems are clearly different, pointing to oxygen consumption for hematin and oxygen production for peroxidase.