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      Anthraquinone dyes decolorization capacity of anamorphic Bjerkandera adusta CCBAS 930 strain and its HRP-like negative mutants

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          Abstract

          Cultures of the anamorphic fungus Bjerkandera adusta CCBAS 930 decolorizing, in stationary cultures, 0.01 % solutions of carminic acid and Poly R-478, were characterised by a strong increase in the activity of the horseradish peroxidase (HRP-like) and manganese-dependent peroxidase (MnP) at a low activity of lignin peroxidase. Genotypically modified mutants of B. adusta CCBAS 930: 930-5 and 930-14, with total or partial loss of decolorization capabilities relative to anthraquinonic dyes, showed inhibition of the activity of HRP-like peroxidase and MnP. Whereas, compared to the parental strain, in the mutant cultures there was an increase in the activity of lignin peroxidase and laccase. The paper presents a discussion of the role of the studied enzymatic activities in the process of decolorization of anthraquinonic dyes by the strain B. adusta CCBAS 930.

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          Microbial decolorization of textile-dyecontaining effluents: A review

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            Fungal decolorization of dye wastewaters: a review.

            In recent years, there has been an intensive research on fungal decolorization of dye wastewater. It is becoming a promising alternative to replace or supplement present treatment processes. This paper examines various fungi, living or dead cells, which are capable of decolorizing dye wastewaters; discusses various mechanisms involved; reports some elution and regeneration methods for fungal biomass; summarizes the present pretreatment methods for increasing the biosorption capacity of fungal biomass; discusses the effect of various factors on decolorization.
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              Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites.

              Two major peroxidases are secreted by the fungus Pleurotus eryngii in lignocellulose cultures. One is similar to Phanerochaete chrysosporium manganese-dependent peroxidase. The second protein (PS1), although catalyzing the oxidation of Mn2+ to Mn3+ by H2O2, differs from the above enzymes by its manganese-independent activity enabling it to oxidize substituted phenols and synthetic dyes, as well as the lignin peroxidase (LiP) substrate veratryl alcohol. This is by a mechanism similar to that reported for LiP, as evidenced by p-dimethoxybenzene oxidation yielding benzoquinone. The apparent kinetic constants showed high activity on Mn2+, but methoxyhydroquinone was the natural substrate with the highest enzyme affinity (this and other phenolic substrates are not efficiently oxidized by the P. chrysosporium peroxidases). A three-dimensional model was built using crystal models from four fungal peroxidase as templates. The model suggests high structural affinity of this versatile peroxidase with LiP but shows a putative Mn2+ binding site near the internal heme propionate, involving Glu36, Glu40, and Asp181. A specific substrate interaction site for Mn2+ is supported by kinetic data showing noncompetitive inhibition with other peroxidase substrates. Moreover, residues reported as involved in LiP interaction with veratryl alcohol and other aromatic substrates are present in peroxidase PS1 such as His82 at the heme-channel opening, which is remarkably similar to that of P. chrysosporium LiP, and Trp170 at the protein surface. These residues could be involved in two different hypothetical long range electron transfer pathways from substrate (His82-Ala83-Asn84-His47-heme and Trp170-Leu171-heme) similar to those postulated for LiP.
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                Author and article information

                Contributors
                teresa.kornilowicz@up.lublin.pl
                Journal
                World J Microbiol Biotechnol
                World J. Microbiol. Biotechnol
                World Journal of Microbiology & Biotechnology
                Springer Netherlands (Dordrecht )
                0959-3993
                1573-0972
                11 January 2014
                11 January 2014
                2014
                : 30
                : 1725-1736
                Affiliations
                Department of Environmental Microbiology, Laboratory of Mycology, University of Life Sciences, Leszczyńskiego 7, 20-069 Lublin, Poland
                Article
                1595
                10.1007/s11274-014-1595-2
                4018482
                24415463
                31eb4644-49e8-4d1c-9547-9b8b250297e4
                © The Author(s) 2014

                Open AccessThis article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.

                History
                : 13 March 2013
                : 2 January 2014
                Categories
                Original Paper
                Custom metadata
                © Springer Science+Business Media Dordrecht 2014

                Biotechnology
                bjerkandera adusta,peroxidases,laccase,carminic acid,poly r-478,rapd
                Biotechnology
                bjerkandera adusta, peroxidases, laccase, carminic acid, poly r-478, rapd

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