Oxidation of anthracene and benzo[a]pyrene by immobilized laccase from Trametes versicolor

Dodor, Daniel E.; Hwang, Huey‐Min; Ekunwe, Stephen I.N.

doi:10.1016/j.enzmictec.2004.04.007

Cited by 185 publications

(79 citation statements)

References 37 publications

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“…The degradation of PAHs by a laccase-mediator system was reported as significantly higher in the presence of mediator compounds such as N-hydroxybenzotriazole (HBT), 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), and siringaldehyde [6]. Laccase (EC 1.10.3.2), p-diphenyl:dioxygen oxidoreductase, forms part of a group of multi-copper enzymes [5].…”

Section: Introductionmentioning

confidence: 99%

Oxidation of Polycyclic Aromatic Hydrocarbons using Partially Purified Laccase from Residual Compost of Agaricus bisporus

et al. 2011

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Laccase partially purified from residual compost of Agaricus bisporus by an aqueous two-phase system (Lac ATPS) was used in degrading polycyclic aromatic hydrocarbons: fluorene (Flu), phenanthrene (Phe), anthracene (Ant), benzo[a]pyrene (BaP), and benzo[a]anthracene (BaA). The capacity of the enzyme to oxidize polyaromatic compounds was compared to that of the crude laccase extract (CE). After treatment of 72 h, Lac ATPS and CE were not capable of oxidizing Flu and Phe, while Ant, BaP, and BaA were oxidized, resulting in percentages of oxidation of 11.2 ± 1, 26 ± 2, and 11.7 ± 4 % with CE, respectively. When Lac ATPS was used, the following percentages of oxidation were obtained: 11.4 ± 3 % for Ant, 34 ± 0.1 % for BaP, and 13.6 ± 2 % for BaA. The results reported here demonstrate the potential application of Lac ATPS for the oxidation of polycyclic aromatic hydrocarbons.

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Section: Introductionmentioning

confidence: 99%

Oxidation of Polycyclic Aromatic Hydrocarbons using Partially Purified Laccase from Residual Compost of Agaricus bisporus

et al. 2011

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“…On the other hand, Ahn et al (2002) demonstrated that immobilized laccase in soil polluted by 2,4-DCP was more effective than the free enzyme in 2,4-DCP removal. Dodor et al (2004), studying T. versicolor laccase immobilized on kaolinite and its potential to oxidize anthracene and benzo [a] pyrene, indicated that immobilization improved stability of laccase to temperature, pH, inhibitors, and storage time compared with the free enzyme. Oxidative enzymes have been immobilized on several natural and synthetic supports and often proposed as efficient catalytic tools to overcome several disadvantages linked to the use of free enzymes (Duran et al 2002).…”

Section: Discussionmentioning

confidence: 97%

White-Rot Fungi in Bioremediation

2012

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“…Our previous study [Dodor et al, 2004] indicated that immobilization of the laccase from Trametes versicolor on functionalized kaolinite improved the catalytic properties of the enzyme, including its pH and temperature stability, and its reusability. The mechanism of substrate oxidation by laccase mediator systems is incompletely understood.…”

Section: Discussionmentioning

confidence: 99%

“…APTES modified the surface properties of the kaolinite, enabling the kaolinite to be an effective support for immobilization of biological molecules. The laccase from Trametes versicolor was successfully immobilized on the functionalized kaolinite particles using the procedure described in our previous study [Dodor et al, 2004]. The immobilized laccase had an enzymatic activity of 20 U/mg protein.…”

Section: Immobilization Of Laccase On the Functionalized Kaolinitementioning

confidence: 99%

Biodegradation of benzo[a]pyrene with immobilized laccase: Genotoxicity of the products in HaCat and A3 cells

Zhang

Zhao

et al. 2007

Environ and Mol Mutagen

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Benzo[a]pyrene (BaP) is listed as a priority pollutant by the U.S. Environmental Protection Agency because it is one of the most potent carcinogens of all known polycyclic aromatic hydrocarbons (PAHs). The biodegradation of BaP is of interest as a means for mitigating its effects in polluted ecosystems. In the present study, BaP was oxidized with laccase from Trametes versicolor, which was immobilized on functionalized kaolinite particles, and the cytotoxicity and genotoxicity of BaP and its degradation intermediates were measured in human HaCaT keratinocytes and A3 T lymphocytes. Cytotoxicity was assessed by fluorescein diacetate (FDA) uptake, while the alkaline Comet assay measured genotoxicity, using tail moment, tail DNA content, and tail length as metrics for DNA damage. On the basis of first-order reaction kinetics, the half life (t(1/) (2)) for the oxidization of BaP by immobilized laccase was 58.5 hr. After 87 hr of oxidation, 20 muM of BaP had decreased to 9.6 muM. HPLC analysis identified 1,6-benzo[a]pyrene quinone (1,6-BaQ), 3,6-benzo[a]pyrene quinone (3,6-BaQ), and 6,12-benzo[a]pyrene quinone (6,12-BaQ) among the oxidation products. Most treatments of HaCaT cells and A3 lymphocytes with BaP or its quinone intermediates resulted in significant decreases in viability (P < 0.05); dose-dependent decreases in cell viability were detected at concentrations of 0.1, 1, and 5 muM, but none of these treatments resulted in decreases of >30%. While treatment of HaCaT cells with as little as 0.1 muM 6,12-BaQ caused significant DNA damage, DNA damage was detected in HaCaT cells only with 1 and 5 muM 1,6-BaQ and 3,6-BaQ, and 5 muM BaP. In Comet assays conducted with A3 lymphocytes, all three quinone intermediates caused significant increase in tail DNA content at 1 and 5 muM. The results indicate that immobilized laccase is capable of degrading BaP, but several of those biodegradation products produce significant levels of DNA damage in human cells.

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Oxidation of anthracene and benzo[a]pyrene by immobilized laccase from Trametes versicolor

Cited by 185 publications

References 37 publications

Oxidation of Polycyclic Aromatic Hydrocarbons using Partially Purified Laccase from Residual Compost of Agaricus bisporus

Oxidation of Polycyclic Aromatic Hydrocarbons using Partially Purified Laccase from Residual Compost of Agaricus bisporus

White-Rot Fungi in Bioremediation

Biodegradation of benzo[a]pyrene with immobilized laccase: Genotoxicity of the products in HaCat and A3 cells

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