Decolorization of triphenylmethane dyes by the bird's nest fungus Cyathus bulleri

Vasdev, Kavita; Kuhad, Ramesh Chander; Saxena, Rajendra Kumar

doi:10.1007/bf00295500

Cited by 79 publications

(40 citation statements)

References 10 publications

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“…Hardin et al [2000] also showed that the peroxidase enzymes LiP and MnP in the activities of decolorization. Laccase from the extracellular fraction of Cyathus bulleri decolorized triphenylmethane dyes [Vasdev et al, 1995]. So far, a few fungal genes encoding lignin peroxidase and laccase with the activity of removing dyes have been cloned and characterized [Cullen, 1997;Gold and Alic, 1993].…”

Section: Discussionmentioning

confidence: 99%

Decolorizing Activity of Malachite Green and Its Mechanisms Involved in Dye Biodegradation by <i>Achromobacter xylosoxidans</i> MG1

Wang

Qiao²,

Wei³

et al. 2011

Microb Physiol

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An Achromobacter xylosoxidans MG1 strainisolated from the effluent treatment plant of a textile and dyeing factory from Yunnan Province in China was found capable of decolorizing the malachite green dye at a high efficacy. Strain MG1 reduced 86% malachite green at the concentration of 2,000 mg/l within 1 h, representing a greater ability for decolorizing and a higher tolerance of this compound than all previously reported bacteria. Color removal was optimal at pH 6 and 38°C. Further experimental evidences demonstrated that both cytoplasmic and extracellular biodegradation contributed to the decolorization of malachite green. Nested PCR was employed to identify the candidate genes responsible for malachite green decolorization, and we identified a cytoplasmic triphenylmethane reductase gene with 100% amino acid similarity to the corresponding gene in Citrobacter sp. strain. In contrast to our expectation, the addition of metyrapone had little effect on the cytoplasmic biodegradation, suggesting that cytochrome P450 was not involved in the high-performance reduction. The extracellular biodegradation was likely attributable to the secretion of extracellular proteases and some heat-resistant compounds.

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Section: Discussionmentioning

confidence: 99%

Decolorizing Activity of Malachite Green and Its Mechanisms Involved in Dye Biodegradation by <i>Achromobacter xylosoxidans</i> MG1

Wang

Qiao²,

Wei³

et al. 2011

Microb Physiol

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“…Several triphenylmethane dye-decolorizing microorganisms have been reported and their characteristics reviewed (2). The biochemical mechanism underlying the decolorization of triphenylmethane dyes has been elucidated in fungi (2,7,20,23) but not in bacteria. Triphenylmethane dyes are decolorized by lignin peroxidase of Phanerochaete chrysosporium (7).…”

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confidence: 99%

“…Triphenylmethane dyes are decolorized by lignin peroxidase of Phanerochaete chrysosporium (7). Laccase from the extracellular fluid of Cyathus bulleri (23) and peroxidase from Pleurotus ostreatus (20) also decolorize triphenylmethane dyes. The structural genes encoding lignin peroxidase and laccase have been cloned and characterized (8,10).…”

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confidence: 99%

Triphenylmethane Reductase from Citrobacter sp. Strain KCTC 18061P: Purification, Characterization, Gene Cloning, and Overexpression of a Functional Protein in Escherichia coli

Jang

Lee

Kim

et al. 2005

Appl Environ Microbiol

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We purified to homogeneity an enzyme from Citrobacter sp. strain KCTC 18061P capable of decolorizing triphenylmethane dyes. The native form of the enzyme was identified as a homodimer with a subunit molecular mass of about 31 kDa. It catalyzes the NADH-dependent reduction of triphenylmethane dyes, with remarkable substrate specificity related to dye structure. Maximal enzyme activity occurred at pH 9.0 and 60°C. The enzymatic reaction product of the triphenylmethane dye crystal violet was identified as its leuco form by UV-visible spectral changes and thin-layer chromatography. A gene encoding this enzyme was isolated based on its N-terminal and internal amino acid sequences. The nucleotide sequence of the gene has a single open reading frame encoding 287 amino acids with a predicted molecular mass of 30,954 Da. Although the deduced amino acid sequence displays 99% identity to the hypothetical protein from Listeria monocytogenes strain 4b H7858, it shows no overall functional similarity to any known protein in the public databases. At the N terminus, the amino acid sequence has high homology to sequences of NAD(P)H-dependent enzymes containing the dinucleotide-binding motif GXXGXXG. The enzyme was heterologously expressed in Escherichia coli, and the purified recombinant enzyme showed characteristics similar to those of the native enzyme. This is the first report of a triphenylmethane reductase characterized from any organism.Triphenylmethane dyes are aromatic xenobiotic compounds that are used extensively in many industrial processes, such as textile dyeing, paper printing, and food and cosmetic manufacture (11). Studies of the biodegradation of triphenylmethane dyes have focused primarily on the decolorization of dyes via reduction reactions. Several triphenylmethane dye-decolorizing microorganisms have been reported and their characteristics reviewed (2). The biochemical mechanism underlying the decolorization of triphenylmethane dyes has been elucidated in fungi (2,7,20,23) but not in bacteria. Triphenylmethane dyes are decolorized by lignin peroxidase of Phanerochaete chrysosporium (7). Laccase from the extracellular fluid of Cyathus bulleri (23) and peroxidase from Pleurotus ostreatus (20) also decolorize triphenylmethane dyes. The structural genes encoding lignin peroxidase and laccase have been cloned and characterized (8, 10). Although several triphenylmethane dye-decolorizing bacteria have been isolated (2), there are no reports of specific enzymes that decolorize these dyes. The decolorization of malachite green and crystal violet by intestinal microflora and several anaerobic bacteria proceeds through enzymatic reduction to their respective leuco derivatives (12, 16). However, the enzymes involved in this reduction have not yet been isolated or characterized in their purified forms. Their amino acid sequences and other biophysical parameters remain unknown.We recently isolated a new bacterium, Citrobacter sp. strain KCTC 18061P, that has a higher decolorization capability than any microorganism repor...

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“…Most of these microorganisms decolorized crystal violet. The mechanism for biodecolorization of crystal violet has been elucidated by fungi (Azmi et al, 1998;Bumpus and Brock, 1988;Shin and Kim, 1998;Vasdev et al, 1995), but not by bacteria. Crystal violet was degraded by ligninolytic culture of Phanerochaete chrysosporium, and its initial oxidation proceeds via Ndemethylation catalyzed by lignin peroxidase (Bumpus and Brock, 1988).…”

mentioning

confidence: 99%

“…Crystal violet was degraded by ligninolytic culture of Phanerochaete chrysosporium, and its initial oxidation proceeds via Ndemethylation catalyzed by lignin peroxidase (Bumpus and Brock, 1988). Decolorization of crystal violet was found to be carried out by laccase in extracellular fluid from Cyathus bulleri (Vasdev et al, 1995), and by peroxidase from Pleurotus ostreatus (Shin and Kim, 1998). The structural genes encoding lignin peroxidase and laccase have been cloned and characterized (Gold and Alic, 1993;Mayer and Staples, 2002).…”

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confidence: 99%

Identification of genes required for decolorization of crystal violet in Citrobacter sp. MY-5

Kim

Lee

Jang

et al. 2005

J. Gen. Appl. Microbiol.

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Decolorization of triphenylmethane dyes by the bird's nest fungus Cyathus bulleri

Cited by 79 publications

References 10 publications

Decolorizing Activity of Malachite Green and Its Mechanisms Involved in Dye Biodegradation by <i>Achromobacter xylosoxidans</i> MG1

Decolorizing Activity of Malachite Green and Its Mechanisms Involved in Dye Biodegradation by <i>Achromobacter xylosoxidans</i> MG1

Triphenylmethane Reductase from Citrobacter sp. Strain KCTC 18061P: Purification, Characterization, Gene Cloning, and Overexpression of a Functional Protein in Escherichia coli

Identification of genes required for decolorization of crystal violet in Citrobacter sp. MY-5

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