Biodegradation of chrysene, an aromatic hydrocarbon by Polyporus sp. S133 in liquid medium

Hadibarata, Tony; Tachibana, Sanro; Itoh, Kazuyoshi

doi:10.1016/j.jhazmat.2008.08.081

Cited by 94 publications

(39 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Reaction systems reached the maximal oxidation rate at 48 hr; however, there was no significant difference between 48 and 24 hr, suggesting that an incubation term of 24 hr was adequate for benzo[a]pyrene oxidation. To our knowledge, this is much faster than conventional biodegradation using bacteria or fungi, which usually required several weeks, 21,22) suggesting the rapidity advantage of enzymatic remediation.…”

Section: Effect Of Incubation Time On Enzymatic Catalysismentioning

confidence: 99%

Optimization of Laccase-mediated Benzo[a]pyrene Oxidation and the Bioremedial Application in Aged Polycyclic Aromatic Hydrocarbons-contaminated Soil

Lin

Yin

et al. 2010

JOURNAL OF HEALTH SCIENCE

View full text Add to dashboard Cite

Laccase is a polyphenol oxidase with the ability to oxidize a broad range of persistent organic pollutants, including benzo[a]pyrene, the most carcinogenic, mutagenic and teratogenic polycyclic aromatic hydrocarbons (PAHs). In this study, the reaction conditions for benzo [a]pyrene oxidation by laccase from Trametes versicolor were optimized in a liquid medium by a series of single factor experiments. The maximal benzo[a]pyrene oxidation rate was observed at 40• C, pH 4, 10% of acetonitrile and an incubation time of more than 24 hr, and the benzo[a]pyrene oxidation was enhanced significantly by the addition of a mediator, 2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonicacid) (ABTS). Laccase was also applied to aged PAHs polluted soil to examine the efficiency of enzymatic bioremediation. The results showed that the enzyme was still effective in the degradation of anthracene, benzo[a]pyrene and benzo [a]anthracene in soil. Moreover, the degradation rate of most PAHs increased by the addition of ABTS. Our results indicated that the bioremediation of PAHs contaminated soil using laccase is feasible but a suboptimal pH might be a limiting factor in the enzymatic treatment of soil.

show abstract

Section: Effect Of Incubation Time On Enzymatic Catalysismentioning

confidence: 99%

Optimization of Laccase-mediated Benzo[a]pyrene Oxidation and the Bioremedial Application in Aged Polycyclic Aromatic Hydrocarbons-contaminated Soil

Lin

Yin

et al. 2010

JOURNAL OF HEALTH SCIENCE

View full text Add to dashboard Cite

show abstract

“…1b). 1-Hydroxy-2-naphthoate is an intermediate in the microbial degradation of phenanthrene and chrysene (53,62,90). Salicylate can be formed in the degradation of naphthalene and derivatives, polycyclic aromatic hydrocarbons, dibenzofuran, and the organophosphorous insecticide isocarbophos, as described in the UM-BB database (http: //umbbd.msi.umn.edu/) (50).…”

Section: Gentisate 12-dioxygenase and Related Enzymesmentioning

confidence: 99%

Ring-Cleaving Dioxygenases with a Cupin Fold

Fetzner

2012

Appl Environ Microbiol

163

139

View full text Add to dashboard Cite

ABSTRACTRing-cleaving dioxygenases catalyze key reactions in the aerobic microbial degradation of aromatic compounds. Many pathways converge to catecholic intermediates, which are subject toorthoormetacleavage by intradiol or extradiol dioxygenases, respectively. However, a number of degradation pathways proceed via noncatecholic hydroxy-substituted aromatic carboxylic acids like gentisate, salicylate, 1-hydroxy-2-naphthoate, or aminohydroxybenzoates. The ring-cleaving dioxygenases active toward these compounds belong to the cupin superfamily, which is characterized by a six-stranded β-barrel fold and conserved amino acid motifs that provide the 3His or 2- or 3His-1Glu ligand environment of a divalent metal ion. Most cupin-type ring cleavage dioxygenases use an FeIIcenter for catalysis, and the proposed mechanism is very similar to that of the canonical (type I) extradiol dioxygenases. The metal ion is presumed to act as an electron conduit for single electron transfer from the metal-bound substrate anion to O2, resulting in activation of both substrates to radical species. The family of cupin-type dioxygenases also involves quercetinase (flavonol 2,4-dioxygenase), which opens up two C-C bonds of the heterocyclic ring of quercetin, a wide-spread plant flavonol. Remarkably, bacterial quercetinases are capable of using different divalent metal ions for catalysis, suggesting that the redox properties of the metal are relatively unimportant for the catalytic reaction. The major role of the active-site metal ion could be to correctly position the substrate and to stabilize transition states and intermediates rather than to mediate electron transfer. The tentative hypothesis that quercetinase catalysis involves direct electron transfer from metal-bound flavonolate to O2is supported by model chemistry.

show abstract

“…Recently, Polyporus sp. S133, white-rot fungi, had been extensively degraded chrysene and phenanthrene (Hadibarata et al 2009;Hadibarata and Tachibana 2010). However, up until now there is no information about its ability to decolorize synthetic dyes.…”

Section: Introductionmentioning

confidence: 99%

Decolorization and Metabolism of Anthraquionone-Type Dye by Laccase of White-Rot Fungi Polyporus sp. S133

Hadibarata

Yusoff

Kristanti

2011

Water Air Soil Pollut

Self Cite

View full text Add to dashboard Cite

Utilization of microbes including white-rot fungi and bacterial strains for decolorization of synthetic dyes is one promising strategy of an environmentally friendly and cost-competitive alternative to physicochemical decomposition processes for treating industrial effluents. In this study, the biodegradation ability of the white-rot fungi Polyporus sp. S133 that produce high laccase was investigated in order to decolorize anthraquinone-type dye. Parameter including pH, temperature, and non-ionic surfactant were used to comparatively study the decolorizing effects on Remazol Brilliant Blue R (RBBR). The purified laccase totally decolorized 200 mg L −1 initial concentration of RBBR dye when only 1.5 UL −1 of laccase was used in the reaction mixture. The optimal decolorization rates were achieved at pH 5 and at a temperature of 50°C. N-hydroxybenzotriazole, a small molecular weight redox mediator, was found to accelerate the decolorization. Tween 20 inhibited the decolorization while Tween 80 and Brij 35 showed no inhibition effect. Two compounds were identified as the intermediates (m/z 304.3 and m/z 342.2). These results suggest that laccase from Polyporus sp. S133 is a powerful tool for the decolorization of anthraquinone dyes. A pathway for the metabolism of the RBBR by laccase of Polyporus sp S133 was proposed. These proposed pathways could contribute to a better comprehension of the mechanisms used by oxidative enzymes to transform organic compounds.

show abstract

Biodegradation of chrysene, an aromatic hydrocarbon by Polyporus sp. S133 in liquid medium

Cited by 94 publications

References 38 publications

Optimization of Laccase-mediated Benzo[a]pyrene Oxidation and the Bioremedial Application in Aged Polycyclic Aromatic Hydrocarbons-contaminated Soil

Optimization of Laccase-mediated Benzo[a]pyrene Oxidation and the Bioremedial Application in Aged Polycyclic Aromatic Hydrocarbons-contaminated Soil

Ring-Cleaving Dioxygenases with a Cupin Fold

Decolorization and Metabolism of Anthraquionone-Type Dye by Laccase of White-Rot Fungi Polyporus sp. S133

Contact Info

Product

Resources

About