Decolorization of a chromophore molecule with immobilized horseradish peroxidase / Descoloração de uma molécula de cromóforo com peroxidase de rábano imobilizada

Priscila S. Corrêa, Suzana G. de Lima, Caio F. Pastusiak, Alfredo J. T. Bosco, Eliana M. Alhadeff

Abstract


The enzymes can modify some effluent characteristics in order to increase the degradability, or the bioconversion of liquid  effluents. The oxireductases, laccases and peroxidases have been used due their high potentiality in many environmental treatments of natural and synthetic organic compounds as dyes, phenols and polyphenolics molecules. The performance of immobilized horseradish peroxidase on aminopropyl glass beads was investigated in this work in a decolorization reaction of methylene blue colorant. The experiments were conducted in batch conditions during 3 hours, with different aqueous solutions of peroxide hydrogen (H2O2) concentration solutions (2-10 mg/L), methylene blue (ME)  (5-20 mg/L) and the pH in the range from 4 to 8, according an experimental design proposed by the software STATISTICA®. After 3 hours of treatment the reduction of  the color was 60% when comparing to the original color and 50% when the immobilized enzymes were reused in five sequential batch treatment cycles for a 10 mg/L of H2O2 solution, 20 mg/L of ME  and pH 8.0.  Working in continuous process with two microreactors in series the system showed a good performance with 97% of decolorization in the first 15 minutes. After 1 hour of continuous treatment the percentage of the color removing was around 70%.

 


Keywords


immobilized horseradish peroxidase; enzymatic decolorization; sequential enzymatic microreactors.

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References


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DOI: https://doi.org/10.34117/bjdv5n8-028