4.6 Article

In vitro degradation of a reactive azo dye by crude ligninolytic enzymes from nonimmersed liquid culture of Phanerochaete chrysosporium

Journal

PROCESS BIOCHEMISTRY
Volume 41, Issue 9, Pages 1987-1993

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.procbio.2006.04.008

Keywords

degradation characteristics; in vitro decolorization; lignin peroxidase; manganese peroxidase; nonimmersed culture; phanerochaete chrysosporium

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In vitro degradation of synthetic dyes by ligninolytic enzymes from white rot fungi is one potential way to deal with dye pollution compared with decolorization by conventional biological treatment. In this work, production of the ligninolytic enzymes was carried out at C/N ratios of 28/44 mM and 56/2.2 mM in nonimmersed liquid culture of Phanerochaete chrysosporium. In vitro decolorization of one industrial azo dye, Reactive brilliant red K-2BP, by crude lignin peroxidase (LiP) and manganese peroxidase (MnP) obtained under carbon and nitrogen limitation respectively, was examined and compared for their degradation characteristics. Both decolorization by LiP and MnP were sensitive to pH, peaking around pH 3.0, and improved at higher enzyme activities. Decolorization by LiP can be enhanced to the greatest degree (89%) with higher addition of H2O2 and veratryl alcohol, whereas decolorization by MnP was optimized only with a suitable dose of H2O2 (0.1 mM) and decreased by the addition of Mn2+. Decolorization declined at high dye concentrations; LiP was able to decolorize a dye concentration of 60 mg/l and below to no less than 85%, and MnP of 10 mg/l to a maximum of 71%. Decolorization by LiP and MnP together was somewhat lower than that by LiP alone. It is suggested that the optimization of the H2O2 supply was mainly responsible for a high efficiency in continuous dye degradation by crude UP and MnP. (c) 2006 Elsevier Ltd. All rights reserved.

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