Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.10.3.2 (laccase)
4,656 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The oxidation of polycyclic aromatic compounds was studied in systems consisting of laccase from Trametes versicolor and so-called mediator compounds. The enzymatic oxidation of acenaphthene, acenaphthylene, anthracene, and fluorene was mediated by various laccase substrates (phenols and aromatic amines) or compounds produced and secreted by white rot fungi. The best natural mediators, such as phenol, aniline, 4-hydroxybenzoic acid, and 4-hydroxybenzyl alcohol were as efficient as the previously described synthetic compounds ABTS [2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid)] and 1-hydroxybenzotriazole. The oxidation efficiency increased proportionally with the redox potentials of the phenolic mediators up to a maximum value of 0.9 V and decreased thereafter with redox potentials exceeding this value. Natural compounds such as methionine, cysteine, and reduced glutathione, containing sulfhydryl groups, were also active as mediator compounds.
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PMID:Natural mediators in the oxidation of polycyclic aromatic hydrocarbons by laccase mediator systems. 1065 13

Ten phenols were selected as natural laccase mediators after screening 44 different compounds with a recalcitrant dye (Reactive Black 5) as a substrate. Their performances were evaluated at different mediator/dye ratios and incubation times (up to 6 h) by the use of Pycnoporus cinnabarinus and Trametes villosa laccases and were compared with those of eight known synthetic mediators (including -NOH- compounds). Among the six types of dyes assayed, only Reactive Blue 38 (phthalocyanine) was resistant to laccase-mediator treatment under the conditions used. Acid Blue 74 (indigoid dye), Reactive Blue 19 (anthraquinoid dye), and Aniline Blue (triarylmethane-type dye) were partially decolorized by the laccases alone, although decolorization was much more efficient and rapid with mediators, whereas Reactive Black 5 (diazo dye) and Azure B (heterocyclic dye) could be decolorized only in the presence of mediators. The efficiency of each natural mediator depended on the type of dye to be treated but, with the only exception being Azure B (< 50% decolorization), nearly complete decolorization (80 to 100%) was attained in all cases. Similar rates were attained with the best synthetic mediators, but the reactions were significantly slower. Phenolic aldehydes, ketones, acids, and esters related to the three lignin units were among the best mediators, including p-coumaric acid, vanillin, acetovanillone, methyl vanillate, and above all, syringaldehyde and acetosyringone. The last two compounds are especially promising as ecofriendly (and potentially cheap) mediators for industrial applications since they provided the highest decolorization rates in only 5 to 30 min, depending on the type of dye to be treated.
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PMID:Lignin-derived compounds as efficient laccase mediators for decolorization of different types of recalcitrant dyes. 1581

The laccase of the fungus Trametes versicolor was able to polymerize various halogen-, alkyl-, and alkoxy-substituted anilines, showing substrate specificity similar to that of horseradish peroxidase, whereas the laccase of Rhizoctonia praticola was active only with p-methoxyaniline. The substrate specificities of the enzymes were determined by using gas chromatography to measure the decrease in substrate concentration during incubation. With p-chloroaniline as the substrate, the peroxidase and the Trametes laccase showed maximum activity near pH 4.2. The transformation of this substrate gave rise to a number of oligomers, ranging from dimers to pentamers, as determined by mass spectrometry. The product profiles obtained by high-pressure liquid chromatography were similar for the two enzymes. A chemical reaction was observed between p-chloroaniline and an enzymatically formed dimer, resulting in the formation of a trimer. All three enzymes oxidized p-methoxyaniline to 2-amino-5-p-anisidinobenzoquinone di-p-methoxyphenylimine, but only the T. versicolor laccase and the peroxidase caused the formation of a pentamer (2,5-di-p-anisidinobenzoquinone di-p-methoxyphenylimine). Our results demonstrate that in addition to horseradish peroxidase, a T. versicolor laccase can also polymerize aniline derivatives.
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PMID:Transformation of Halogen-, Alkyl-, and Alkoxy-Substituted Anilines by a Laccase of Trametes versicolor. 1634 78

Accelerated degradation of organic chemicals by aquatic plant-bacterial associations was reported for the first time with elucidation of the role and contribution of aquatic plant and bacteria in its rhizosphere using a fast-growing giant duckweed, Spirodela polyrrhiza. The results clearly showed the accelerated degradation of all the three aromatic compounds (phenol, aniline and 2,4-dichlorophenol [2,4-DCP]) tested by aquatic plant-bacterial associations. In phenol degradation system, phenol-degrading bacteria indigenous to the rhizosphere fraction of S. polyrrhiza mainly contributed, while in aniline degradation system S. polyrrhiza mainly contributed by stimulating aniline-degrading bacteria both in the rhizosphere and balk water fraction. On the other hand in 2,4-DCP degradation system, S. polyrrhiza itself mainly contributed to its removal by uptake and degradation. Thus, the mechanisms for accelerated removal of aromatic compounds were quite different depending on the substrates. S. polyrrhiza showed selective accumulation of phenol-degrading bacteria in its rhizosphere fraction, while aniline- and 2,4-DCP-degrading bacteria were not much accumulated. S. polyrrhiza secreted peroxidase and laccase. However, both of the enzymatic activities increased with the addition of aromatic compounds, degrading ability of S. polyrrhiza itself should be owing to the production of peroxidase rather than laccase because the change of peroxidase activity and concentration of each aromatic compound well concurred. From the results obtained in the present study, it can be concluded that the feasibility of the use of aquatic plant-bacterial associations to accelerate the degradation of organic chemicals especially recalcitrant compounds in aquatic environment was shown.
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PMID:Accelerated aromatic compounds degradation in aquatic environment by use of interaction between Spirodela polyrrhiza and bacteria in its rhizosphere. 1671 44

A method of enzymatic synthesis of electroconductive polyaniline on the micelles of dodecylben-zenesulfonic acid sodium salt (DBSNa) is proposed. The high potential laccase from the basidiomycete Trametes hirsuta was used as a biocatalyst. The conditions for polyaniline synthesis were optimized (pH 4.0; reagent concentrations, 10-20 mM; and aniline/DBSNa ratio, 2: 1). The resulting product was electrochemically active in the range of potentials from -200 to 600 mV, electroconductive, and capable of reversible dedoping with a change in pH of solution.
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PMID:[Micellar laccase-catalyzed synthesis of electroconductive polyaniline]. 1866 52

A new method for synthesis of the conductive complex between polyaniline (PANI) and poly(2-acrylamido-2-methyl-1-propanosulfonic acid) (PAMPS) was proposed; in this method, the immobilized laccase from the basidiomycete Trametes hirsuta is used as a biocatalyst for aniline oxidative polymerization. The conditions for laccase immobilization on CM cellulose by bifunctional Woodward's reagent were optimized. The catalytic properties of immobilized and native laccases were compared. The immobilized laccase appeared an efficient catalyst for the oxidative radical polymerization of aniline on polysulfonic acid matrix at 4 degrees C. It was demonstrated that the immobilized enzyme could be repeatedly used for enzymatic synthesis of this polymer. Several spectral characteristics of the PANI/PAMPS-complexes synthesized at various pH values were studied. The conductance of PANI specimens produced using immobilized laccase as a catalyst was 13 mS/cm.
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PMID:[Synthesis of electroconductive polyaniline using immobilized laccase]. 1923 6

Laccase/mediator systems are important bioremediation agents as the rates of reactions can be enhanced in the presence of the mediators. The decolorization mechanism of two triarylmethane dyes, namely, Basic Green 4 and Acid Violet 17 is reported using Cyathus bulleri laccase. Basic Green 4 was decolorized through N-demethylation by laccase alone, while in mediator assisted reactions, dye breakdown was initiated from oxidation of carbinol form of the dye. Benzaldehyde and N,N-dimethyl aniline were the major end products. With Acid Violet 17, laccase carried out N-deethylation and in mediator assisted reactions, oxidation of the carbinol form of the dye occurred resulting in formation of formyl benzene sulfonic acid, carboxy benzene sulfonic acid and benzene sulfonic acid. Toxicity analysis revealed that Basic Green 4 was toxic and treatment with laccase/mediators resulted in 80-100% detoxification. The treatment of the textile dye solution using laccase and 2,2'-azino-di-(-ethylbenzothiazoline-6-sulfonic acid) (ABTS) was demonstrated in an enzyme membrane reactor. At a hydraulic retention time of 6h, the process was operated for a period of 15 days with nearly 95% decolorization, 10% reduction in flux and 70% recovery of active ABTS.
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PMID:Laccase/mediator assisted degradation of triarylmethane dyes in a continuous membrane reactor. 1953 71

Laccases are members of the blue copper oxidases family found in nature. They commonly oxidise a wide range of phenol and aniline derivatives, which in turn are involved in oxidative coupling reactions. Yet, laccases remain rarely described as biocatalysts in organic synthesis. This paper describes the chemical preparation of original sulfonated aminophenol substrates and their enzyme-mediated dimerisation into phenoxazine chromophores that feature tuneable water solubility as a function of the sulfonyl substituent. The scope and limitations of the biocatalysed synthetic process are outlined. Kinetic data were collected to evaluate the influence of physicochemical parameters. The structure of the novel phenoxazine dyes ("head-to-head" or "head-to-tail" dimer) was assessed by NMR spectroscopic analysis. Two crystalline compounds were analysed by X-ray diffraction. Such laccase-mediated synthesis (a green chemistry process) was proven to be more efficient than the chemical oxidation of o-aminophenols with silver oxide.
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PMID:Laccase-mediated synthesis of novel substituted phenoxazine chromophores featuring tuneable water solubility. 1962 87

We report here on the facile preparation of polymer-enzyme-multiwalled carbon nanotubes (MWCNTs) cast films accompanying in situ laccase (Lac)-catalyzed polymerization for electrochemical biosensing and biofuel cell applications. Lac-catalyzed polymerization of dopamine (DA) as a new substrate was examined in detail by UV-vis spectroscopy, cyclic voltammetry, quartz crystal microbalance, and scanning electron microscopy. Casting the aqueous mixture of DA, Lac and MWCNTs on a glassy carbon electrode (GCE) yielded a robust polydopamine (PDA)-Lac-MWCNTs/GCE that can sense hydroquinone with 643 microA mM(-1) cm(-2) sensitivity and 20-nM detection limit (S/N = 3). The DA substrate yielded the best biosensing performance, as compared with aniline, o-phenylenediamine, or o-aminophenol as the substrate for similar Lac-catalyzed polymerization. Casting the aqueous mixture of DA, glucose oxidase (GOx), Lac, and MWCNTs on a Pt electrode yielded a robust PDA-GOx-Lac-MWCNTs/Pt electrode that exhibits glucose-detection sensitivity of 68.6 microA mM(-1) cm(-2). In addition, 2,2'-azinobis (3-ethylbenzothiazoline-6-sulfonate) diammonium salt (ABTS) was also coimmobilized to yield a PDA-Lac-MWCNTs-ABTS/GCE that can effectively catalyze the reduction of O(2), and it was successfully used as the biocathode of a membraneless glucose/O(2) biofuel cell (BFC) in pH 5.0 Britton-Robinson buffer. The proposed biomacromolecule-immobilization platform based on enzyme-catalyzed polymerization may be useful for preparing many other multifunctional polymeric bionanocomposites for wide applications.
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PMID:Polymeric bionanocomposite cast thin films with in situ laccase-catalyzed polymerization of dopamine for biosensing and biofuel cell applications. 2033 55

Soil metabolism of sulfonamides is largely unknown. Hence the sulfonamides sulfanilamide (SAA), sulfadimethoxine (SDT) and sulfapyridine (SPY) were reacted in model experiments with a fungal laccase from Trametes versicolor. Enzymatic transformation after a reaction time of 15 d ranged from 10.0% for SAA up to 95.6% for SPY and the difference was attributed to the different molecular substituents. Metabolites were first tentatively assigned after LC-ESI(+)-MS full-scan analysis. Secondly, the proposed metabolites were further confirmed employing either multiple reaction monitoring in comparison with standard substances or precursor ion scan LC-ESI(+)-MS/MS experiments striving for the precursor and two to three product ions. Aniline was confirmed as a breakdown product of SPY and further metabolites of SPY and of SDT were identified as rearranged SO(2) extrusion products. Thirdly, some of the metabolites matched those that were previously reported for sulfonamide photodegradation and degradation in soil. It was concluded that enzymatic metabolism as investigated here also occurs in soil.
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PMID:Metabolites from fungal laccase-catalysed transformation of sulfonamides. 2086 43


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