Abstract

Decolorization of six synthetic dyes using three sources of fungal laccase with the origin of Aspergillus oryzae, Trametes versicolor, and Paraconiothyrium variabile was investigated. Among them, the enzyme from P. variabile was the most efficient which decolorized bromophenol blue (100%), commassie brilliant blue (91%), panseu-S (56%), Rimazol brilliant blue R (RBBR; 47%), Congo red (18.5%), and methylene blue (21.3%) after 3 h incubation in presence of hydroxybenzotriazole (HBT; 5 mM) as the laccase mediator. It was also observed that decolorization efficiency of all dyes was enhanced by increasing of HBT concentration from 0.1 mM to 5 mM. Laccase from A. oryzae was able to remove 53% of methylene blue and 26% of RBBR after 30 min incubation in absence of HBT, but the enzyme could not efficiently decolorize other dyes even in presence of 5 mM of HBT. In the case of laccase from T. versicolor, only RBBR was decolorized (93%) in absence of HBT after 3 h incubation.

Highlights

  • More than 10,000 various dyes stable to light, chemicals and microbial degradation are manufactured and used by textile, cosmetic, plastic and printing industries [1,2,3]

  • The aim of the present study was to evaluate decolorization ability of three sources of laccase obtained from Paraconiothyrium variabile, Trametes versicolor and Aspergillus oryzae on six synthetic dyes

  • Decolorization percent by using two other sources of fungal laccases did not increase higher than 25.3% even after 3 hours incubation (Figure 1)

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Summary

Introduction

More than 10,000 various dyes stable to light, chemicals and microbial degradation are manufactured and used by textile, cosmetic, plastic and printing industries [1,2,3]. Beside conventional physicochemical methods [9], application of fungal and bacterial strains capable of adsorbing or degrading [1,9,10] of different dye groups has been considered as a novel concern in this field during last decades. In contrast to other oxidases such as peroxidases, laccase requires no H2O2 for oxidation reaction [15,20]. Such properties make laccase s an important enzyme in biodegradation of xenobiotics and phenolic compounds and decolorization of dyes [2,21]

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