Oxidation of Polycyclic Aromatic Hydrocarbons (PAH) by Laccase of Trametes Versicolor

Majcherczyk, Andrzej; Johannes, Christian; Hüttermann, Aloys

doi:10.1016/s0141-0229(97)00199-3

Cited by 281 publications

(142 citation statements)

References 25 publications

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“…Previously, between 70 and 98% of the protein immobilised and 67-96% of laccase activity, recovery was reported with different carrier materials [52][53][54]. Out of a number of different carrier materials previously tested for laccase immobilization such as activated carbon [55], Eupergit ® C [56], Sepharose [57], silica-based matrices [58] and porous glass [53,59] only alumina was used in this study as it seems to be more suitable for application in dye decolourization, due to its mechanical stability.…”

Section: Redyeingmentioning

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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Section: Redyeingmentioning

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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“…2,4-Dimethoxyphenol (DMP), syringic alcohol (SAlc), syringaldehyde (SAld), syringic acid (SAcid) and transferulic acid (FAcid) can be obtained from the lignin in wood. ABTS and HBT were used as typical synthetic mediators, because they have been reported as high performance mediators in many papers (2,(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)21,22). The results of the oxidation of LO by various reaction systems are shown in Fig.…”

Section: Results and Discussion 1 Effect Of Mediatormentioning

confidence: 99%

“…Such processes have potential applications for biobleaching, i.e., degradation of lignin-containing phenol or benzyl alcohol derivatives (7)(8)(9)(10), and for bioremediation, e.g., oxidative degradation of PAHs (5,6,(11)(12)(13), estrogenic compounds (14) and dioxins (15) in the environment. In other words, oxidation reactions of these aromatic compounds by laccase/mediator systems can be solve the problems.…”

Section: Introductionmentioning

confidence: 99%

Oxidation of Triacyiglycerol by Laccase-Natural Mediator and Laccase-Mediator Derived from Natural Compound Systems.

Saba

Nakano

2003

J. Oleo Sci.

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Laccase, a type of polyphenoloxidase, was found to oxidize unsaturated triacylglycerol under mild reaction conditions in the presence of a simple natural mediator and mediator which is derived from a natural compound. The oxidized products were characterized by UV-and IR-spectroscopic analyses, ferric thiocyanate peroxide analysis and size exclusion chromatography. It was considered that conjugated diene peroxide units were formed in the triacylglycerol without substantial polymerization or degradation reactions of the main chain in the fatty acid residual group. As the mediator, 4-hydroxybenzoic acid, a simple natural phenol, which is secreted by white rot fungi, and the products derived from natural phenols were investigated. 4-Hydroxybenzaldehyde and methyl-4-hydroxybenzoate showed high oxidation activity comparable with synthesized mediators that have been previously reported. Trans-ferulic acid and 2,6-dimethoxyphenol that are not effective for the oxidation of anthracene showed a low oxidation activity for triacylglycerol in the present reaction system. The oxidation activity of the mediators used has some relationship to its oxidation potential. A bell-shaped curve with 4-hydroxybenzaldehyde as its apex may be drawn for the 4-substituted phenols when 4-hydroxybenzoic acid and alkyl-4-hydroxybenzoate were excluded.

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“…This circumstance hinders the application of laccase in lignin-biotechnology since in natural lignin most of the phenolic groups are substituted . Luckily, the detection of laccase mediators, small organic molecules with a high redox-potential (Bourbonnais & Paice 1990, Eggert et al 2006, Johannes et al 1996, Majcherczyk et al 1998, opened up chemical solutions to overcome weak properties of laccases (Call & Mücke 1997). Application of mediators enhances laccase reaction speeds and, most importantly, the substrate spectrum of the enzymes broadens dramatically.…”

Section: Homogenisationmentioning

confidence: 99%

Wood production, wood technology, and biotechnological impacts

Kües¹

2007

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Oxidation of Polycyclic Aromatic Hydrocarbons (PAH) by Laccase of Trametes Versicolor

Cited by 281 publications

References 25 publications

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

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

Oxidation of Triacyiglycerol by Laccase-Natural Mediator and Laccase-Mediator Derived from Natural Compound Systems.

Wood production, wood technology, and biotechnological impacts

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