Oxidative degradation of polyaromatic hydrocarbons catalyzed by blue laccase from Pleurotus ostreatus D1 in the presence of synthetic mediators

Pozdnyakova, N. N.; Rodakiewicz-Nowak, Janina; Turkovskaya, O. V.; Haber, J.

doi:10.1016/j.enzmictec.2006.03.009

Cited by 77 publications

(56 citation statements)

References 37 publications

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“…No apparent correlation between the oxidation by laccase and the molecular weight of the PAH, structures, or ionization potential (IP) was found, as has been previously noted 35,36 . Anthracene, with its low molecular weight and linear structure, was quickly oxidized compared to those with a higher molecular weight and/or benzene rings arranged in an angular or clustered manner, such as benzo[a]pyrene and phenanthrene.…”

Section: Pah Oxidation By Crude Laccasementioning

confidence: 58%

“…Regardless, the crude laccase from P. coccineus Thongkred 013 BCU appeared to be more efficient in the oxidation of all five PAHs tested here compared to the laccase from Trametes after incubation for 24 h or longer 1,31 . In the presence of ABTS, blue and yellow laccase from Pleurotus ostreatus can degrade anthracene, fluoranthene, pyrene, and phenanthrene at a comparable or higher rate compared to the P. coccineus Thongkred 013 BCU crude laccase, but the P. ostreatus blue laccase is unable to degrade these PAHs without adding the mediator 36,40 . In conclusion, laccase, produced as a culture medium filtrate by a Thai isolate of P. coccineus (Thongkred 013 BCU), could oxidize all five tested PAHs, from an initial level of 100 ppm to nearly 90% of anthracene within 24 h without a mediator.…”

Section: Pah Oxidation By Crude Laccasementioning

confidence: 98%

“…However, fluoranthene and pyrene, which have clustered structures, were oxidized relatively quickly. The IP values of these PAHs are 7.12, 7.40-7.55, 7.43-7.72, 7.76-7.89, and 7.91-8.03 eV for benzo[a]pyrene, pyrene, anthracene, fluoranthene, and phenanthrene, respectively [35][36][37][38] , which mostly fall within the range of the reported threshold IP value for laccase (7.45-7.80 eV) 39 . Similar effects of the addition of ABTS to the reaction on the degradation of PAHs were also reported for the Trametes laccase, where the addition of ABTS only slightly enhanced the degradation of some PAHs while it reduced the degradation of other 1 .…”

Section: Pah Oxidation By Crude Laccasementioning

confidence: 99%

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Thongkred¹,

Lotrakul²,

Prasongsuk³

et al. 2011

ScienceAsia

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Basidiocarps of Pycnoporus coccineus and P. sanguineus were collected from Kanchanaburi, Phetchaburi, and Mae Hong Son provinces in Thailand. Liquid culture of P. coccineus isolates provided higher laccase and manganese peroxidase activities than those of P. sanguineus. Lignin peroxidase activity was not detectable in any of the three Pycnoporus isolates. P. coccineus Thongkred 013 BCU, the best laccase producer among these isolates, was selected to optimize laccase production. The highest laccase yield (5.97 ± 0.40 U/ml) was obtained when grown at 28°C for 8 days in basal medium containing 2% (w/v) glucose and 0.25% (w/v) peptone at an initial pH of 5.0. The optimum conditions for stability and activity of the crude laccase enzyme were at pH 3.5 and room temperature (25 ± 2°C). FeSO4 (10 mM) and SDS (1% w/v) were both inhibitory to the laccase activity. When five different types of polycyclic aromatic hydrocarbons (PAHs) were individually added to liquid culture of P. coccineus at 100 ppm, the oxidation of anthracene, pyrene, and fluoranthene detected within 24 h were 59.7, 50.7, and 49.8%, respectively, whereas only 25.3% of benzo[a]pyrene and 32.4% of phenanthrene were oxidized. When P. coccineus crude laccase (1 U/ml) was used, these PAHs were more readily oxidized, with 76.4 and 74.3% of pyrene and anthracene, respectively, being oxidized within 2 h and 84.2% of fluoranthene oxidized within 24 h. Benzo[a]pyrene and phenanthrene oxidation by the enzyme were enhanced when 1 mM 2,2'-azinobis(3-ethylbenzothiazoline-6-sulphonic acid) was added as a mediator to the reaction mixture, resulting in 66.3 and 50.5% of the initial 100 ppm being oxidized after 24 h.

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Section: Pah Oxidation By Crude Laccasementioning

confidence: 58%

Section: Pah Oxidation By Crude Laccasementioning

confidence: 98%

Section: Pah Oxidation By Crude Laccasementioning

confidence: 99%

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Thongkred¹,

Lotrakul²,

Prasongsuk³

et al. 2011

ScienceAsia

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“…ostreatus belongs to a subclass of lignin-degrading fungi that produces laccases, Mn-peroxidases, and versatile peroxidases but no lignin peroxidases [4,36]. Our early studies showed that the strain P. ostreatus D1 could actively degrade PAHs [34]. The aim of the present study was to investigate the influence of PAHs and their derivatives on ligninolytic enzyme activities (laccase, Mn-peroxidase, and/or versatile peroxidase) during submerged cultivation of the fungus P. ostreatus D1.…”

Section: Introductionmentioning

confidence: 97%

“…The involvement of extracellular ligninolytic enzymes, such as Mn-peroxidase and laccase, in PAH degradation has been discussed by many researchers. Both enzymes can catalyze PAH oxidation under appropriate conditions [5,[31][32][33][34]. Unfortunately, very few data are available on the influence of PAHs on ligninolytic peroxidases and laccase production.…”

Section: Introductionmentioning

confidence: 99%

Influence of PAHs on ligninolytic enzymes of the fungus Pleurotus ostreatus D1

2010

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Polycyclic aromatic hydrocarbons (PAHs), their derivatives, and their degradation products were assayed for the ability to enhance activities of ligninolytic enzymes (laccase and versatile peroxidase) of the fungus Pleurotus ostreatus D1. The activities of both laccase and versatile peroxidase were induced by the PAHs, their derivatives, and their degradation products. Laccase was produced mostly in the first 7-10 days, whereas the production of versatile peroxidase began after 5-7 days of cultivation. Non-denaturing PAGE showed the presence of additional forms of laccase and versatile peroxidase in the presence of the xenobiotics in the cultivation medium. The difference in the production time for these enzymes may reflect that laccases are involved in the first stages of PAHs degradation and that versatile peroxidase can be necessary for oxidation of some degradation products. This is the first report on versatile peroxidase induction by PAHs and their derivatives.

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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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Oxidative degradation of polyaromatic hydrocarbons catalyzed by blue laccase from Pleurotus ostreatus D1 in the presence of synthetic mediators

Cited by 77 publications

References 37 publications

Untitled

Untitled

Influence of PAHs on ligninolytic enzymes of the fungus Pleurotus ostreatus D1

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

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