Direct dechlorination of chlorophenolic compounds by laccases from Trametes (Coriolus) versicolor

Roy-Arcand, L.; Archibald, Frederick

doi:10.1016/0141-0229(91)90128-w

Cited by 167 publications

(48 citation statements)

References 44 publications

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“…Although there are many reports dealing with extracellular Lccs produced by white-rot basidiomycetes (Leonowicz et al, 2001), there are few studies of the intracellular Lccs produced by these fungi (Burke & Cairney, 2002;Schlosser et al, 1997;Roy-Arcand & Archibald, 1991). In A. bisporus, the biological significance of intracellular Lccs is considered to be very limited because of their low levels (Turner, 1974), but their significance remains unclear.…”

Section: Introductionmentioning

confidence: 99%

Important role of fungal intracellular laccase for melanin synthesis: purification and characterization of an intracellular laccase from Lentinula edodes fruit bodies

et al. 2003

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A laccase (EC 1.10.3.2) was isolated from the fully browned gills of Lentinula edodes fruit bodies. The enzyme was purified to a homogeneous preparation using hydrophobic, cation-exchange and size-exclusion chromatography. SDS-PAGE analysis showed the purified laccase, Lcc 2, to be a monomeric protein of 58?0 kDa. The enzyme had an isoelectric point of around pH 6?9. The optimum pH for enzyme activity was around 3?0 against 2,29-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)diammonium salt (ABTS), and it was most active at 40 6C and stable up to 50 6C. The enzyme contained 8?6 % carbohydrate and some copper atoms. The enzyme oxidized ABTS, p-phenylenediamine, pyrogallol, guaiacol, 2,6-dimethoxyphenol, catechol and ferulic acid, but not veratryl alcohol and tyrosine. b-(3,4-Dihydroxyphenyl)alanine (L-DOPA), which was not oxidized by a laccase previously reported from the culture filtrate of L. edodes, was also oxidized by Lcc 2, and the oxidative product of L-DOPA was identified as L-DOPA quinone by HPLC analysis. Lcc 2 was able to oxidize phenolic compounds extracted from fresh gills to brown-coloured products, suggesting a role for laccase in melanin synthesis in this strain.

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Section: Introductionmentioning

confidence: 99%

Important role of fungal intracellular laccase for melanin synthesis: purification and characterization of an intracellular laccase from Lentinula edodes fruit bodies

et al. 2003

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“…Several other lignolytic fungi were shown to degrade azo dyes investigated including P. chrysosporium [47,48], T. versicolor [49], T. modesta [50] and Aspergillus niger [51]. Previously, a purified laccase from A. niger was shown to decolourize one of four diazo dyes tested, demonstrating a specificity for the type or position of substituents on the phenolic ring of the dye structure [14].…”

Section: Dye Decolourizationmentioning

confidence: 99%

An acid-stable laccase from Sclerotium rolfsii with potential for wool dye decolourization

Ryan

Schnitzhofer

Tzanov

et al. 2003

Enzyme and Microbial Technology

108

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The plant pathogen basidiomycete S. rolfsii secretes two laccases (SRL1 and SRL2) with molecular weights of 55 and 86 kDa, respectively. Laccase production was shown to be inducible by the addition of 2,5-xylidine to the cultural media. After treatment with a combination of chitinase and ␤-1,3-glucanase, two different laccases were isolated from the sclerotia depending on the stage of sclerotia development.The more prominent laccase, SRL1, was purified and found to decolourize the industrially important wool azo dye Diamond Black PV 200 without the addition of redox mediators. The enzyme (pI 5.2) was active in the acidic pH range, showing an optimal activity at pH 2.4, with ABTS as substrate. The optimum temperature for activity was determined to be 62 • C. Enzyme stability studies revealed that SRL1 was notably stable at 18 • C and pH 4.5, retaining almost full activity after a week. Oxidation of tyrosine was not detectable under the reaction conditions but the enzyme did oxidize a variety of the usual laccase substrates. SRL1 was strongly inhibited by sodium azide and fluoride. Dye solutions decolourized with the immobilized laccase were successfully used for redyeing.

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“…(3,4). The BPA degradation by T. villosa laccase might be based on the high oxidation potential and the wide substrate specificity deduced from the radical enzyme reaction (5)(6)(7). In this paper, we report on preparation of electrophoretically homogeneous laccase, optimum conditions for BPA degradation, and recent progress in isolation and identification of the reaction products.…”

mentioning

confidence: 99%

Degradation of Bisphenol A by Purified Laccase from Trametes villosa

Fukuda¹,

Uchida²,

Takashima³

et al. 2001

Biochemical and Biophysical Research Communications

146

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Direct dechlorination of chlorophenolic compounds by laccases from Trametes (Coriolus) versicolor

Cited by 167 publications

References 44 publications

Important role of fungal intracellular laccase for melanin synthesis: purification and characterization of an intracellular laccase from Lentinula edodes fruit bodies

Important role of fungal intracellular laccase for melanin synthesis: purification and characterization of an intracellular laccase from Lentinula edodes fruit bodies

An acid-stable laccase from Sclerotium rolfsii with potential for wool dye decolourization

Degradation of Bisphenol A by Purified Laccase from Trametes villosa

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