Dehalogenation of Chlorinated Hydroxybiphenyls by Fungal Laccase

Schultz, Asgard; Jonas, Ulrike; Hammer, Elke; Schauer, Frieder

doi:10.1128/aem.67.9.4377-4381.2001

Cited by 97 publications

(40 citation statements)

References 29 publications

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“…Likewise halophenols [178][179][180][181][182] bisphenol A, [183][184][185] various hormones and so-called endocrine disrupting compounds [186][187][188] or even TNT [189,190] have been reported. Non-phenolic compounds may be ‗inactivated' using the LMS or PMS strategy [36,[191][192][193][194][195][196][197][198].…”

Section: Phenol Detoxificationmentioning

confidence: 99%

Enzyme Initiated Radical Polymerizations

2012

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Section: Phenol Detoxificationmentioning

confidence: 99%

Enzyme Initiated Radical Polymerizations

2012

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“…Laccase of the white rot fungi, Trametes versicolor and Pycnoporus cinnabarinus, was shown to transform 2-hyxroxyDF 96) . P. cinnabarinus laccase was reported to be capable of dehalogenating chlori-nated hydroxybiphenyls 167) .…”

Section: )mentioning

confidence: 99%

Biodiversity of Dioxin-Degrading Microorganisms and Potential Utilization in Bioremediation.

Hiraishi

2003

Microb. Environ.

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Dioxins are a group of chloroaromatic compounds known to be toxic and carcinogenic, and persistent environmental pollutants. How to remedy dioxin-polluted environments is one of the most challenging problems in environmental technology. From ecological and economical viewpoints, biological methods using particular microorganisms and microbial consortia capable of dioxin transformation and degradation have greater appeal than physicochemical methods in their application for environmental remediation. Large numbers of microorganisms capable of degrading dioxins and dioxin-like compounds have been isolated and characterized. Information about the biodiversity, ecophysiology and molecular biology of dioxin-degrading microorganisms has accumulated particularly during the past decade. There are three major modes of microbial degradation and transformation of dioxins; that is, oxidative degradation by aerobic bacteria containing aromatic hydrocarbon dioxygenases, reductive dechlorination by anaerobic microorganisms and fungal oxidation with cytochrome P-450, lignin peroxidases and laccases. This article overviews the current knowledge of microbial degradation and transformation of dioxins as well as the biodiversity of microorganisms involved. Strategies directed towards the bioremediation of dioxin-polluted environments are discussed.

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“…Among high-redox-potential laccases (HRPLs), the laccase from Pycnoporus cinnabarinus (PcL) shows particularly interesting biochemical characteristics in terms of stability and turnover rates for natural and synthetic substrates (36,67). Indeed, the last decade has seen exhaustive studies about the potential application of PcL in the delignification of paper pulps, pitch control, food industry, dye decolorization, or degradation of polycyclic aromatic hydrocarbon (14,15,24,25,29,33,57). Optimization of PcL production achieved the highest expression levels yet reported for any HRPL (over 1 g/liter from selected fungal monokaryotic strains and up to 100 mg/liter from heterologous expression in Aspergillus spp.)…”

mentioning

confidence: 99%

Engineering Platforms for Directed Evolution of Laccase from Pycnoporus cinnabarinus

Camarero

Pardo

Cañas

et al. 2012

Appl Environ Microbiol

120

173

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While the Pycnoporus cinnabarinus laccase (PcL) is one of the most promising high-redox-potential enzymes for environmental biocatalysis, its practical use has to date remained limited due to the lack of directed evolution platforms with which to improve its features. Here, we describe the construction of a PcL fusion gene and the optimization of conditions to induce its functional expression in Saccharomyces cerevisiae, facilitating its directed evolution and semirational engineering. The native PcL signal peptide was replaced by the ␣-factor preproleader, and this construct was subjected to six rounds of evolution coupled to a multiscreening assay based on the oxidation of natural and synthetic redox mediators at more neutral pHs. The laccase total activity was enhanced 8,000-fold: the evolved ␣-factor preproleader improved secretion levels 40-fold, and several mutations in mature laccase provided a 13.7-fold increase in k cat . While the pH activity profile was shifted to more neutral values, the thermostability and the broad substrate specificity of PcL were retained. Evolved variants were highly secreted by Aspergillus niger (ϳ23 mg/ liter), which addresses the potential use of this combined-expression system for protein engineering. The mapping of mutations onto the PcL crystal structure shed new light on the oxidation of phenolic and nonphenolic substrates. Furthermore, some mutations arising in the evolved preproleader highlighted its potential for heterologous expression of fungal laccases in yeast (S. cerevisiae).

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Dehalogenation of Chlorinated Hydroxybiphenyls by Fungal Laccase

Cited by 97 publications

References 29 publications

Enzyme Initiated Radical Polymerizations

Enzyme Initiated Radical Polymerizations

Biodiversity of Dioxin-Degrading Microorganisms and Potential Utilization in Bioremediation.

Engineering Platforms for Directed Evolution of Laccase from Pycnoporus cinnabarinus

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