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)

This study was performed to determine which oxidoreductive catalysts were most efficient in catalyzing the binding of 8-hydroxybentazon to soil humic substances. 8-Hydroxybentazon was completely transformed by an oxidoreductive enzyme, laccase of Myceliophthora thermophila, at pH 3.0-7.0 within 30 min. When abiotic catalysts, manganese(IV), iron(III), and aluminum oxides were used in the same pH range, 8-hydroxybentazon was completely transformed only by manganese(IV) oxide (delta-MnO2), but a relatively small amount of 8-hydroxybentazon was transformed by iron(III) oxide and aluminum oxide. The adsorption of 8-hydroxybentazon in the soil showed an H-type and coincided well with the Langmuir isotherm. To better understand the factors involved in the rapid and strong binding of 8-hydroxybentazon with soil humic substances, 8-hydroxybentazon transformation by oxidoreductive catalysts was studied in various soil conditions: air-dried, preincubated, sterilized, and iron(III) oxide and manganese(IV) oxide free. 8-Hydroxybentazon was completely transformed within 24 h in the decreasing order of preincubated, air-dried, and sterilized soils. However, little transformation was observed in the iron(III) oxide and manganese(IV) oxide free soils. These results suggest that the major catalyst responsible for the rapid and strong binding of 8-hydroxybentazon to soil humic substances is a metal oxide, manganese(IV) oxide, not a soil oxidoreductive enzyme.
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PMID:Formation of bound residues of 8-hydroxybentazon by oxidoreductive catalysts in soil. 1203 19

Hot water-extraction was performed on decomposed leaf litter in order to solubilize the toxic fraction involved in the dietary interaction against mosquito larvae in subalpine breeding sites. The toxic fraction was partially extracted by water with an optimum temperature of 60 degrees C and recovered in an insoluble form. Phytochemical characterization was achieved through differential enzymatic hydrolyses, using the laccase mediator delignifying system, and aluminum chloride chelation monitored by standard bioassays; comparative spectrophotometric analyses in ultraviolet light after solubilization in acetyl bromide; and comparative reversed-phase high-performance liquid chromatography of the phenolic aldehydes after alkaline nitrobenzene oxidation. The results suggested the involvement of ligninlike compounds in the toxicity of the isolated fraction. Toxicity of this fraction appeared far stronger than that of the crude leaf litter. The involvement of this ligninlike fraction in the dietary toxicity of leaf litter against larval mosquito was then investigated.
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PMID:Hot extraction and characterization of a ligninlike fraction involved in larvicidal effects of decomposed leaf litter against mosquito. 1237 6

Decolorization of textile dyes by a laccase from Trametes modesta immobilized on gamma-aluminum oxide pellets was studied. An enzyme reactor was equipped with various UV/Vis spectroscopic sensors allowing the continuous online monitoring of the decolorization reactions. Decolorization of the dye solutions was followed via an immersion transmission probe. Adsorption processes were observed using diffuse reflectance measurements of the solid carrier material. Generally, immobilization of the laccase does not seem to sterically affect dye decolorization. A range of commercial textile dyes was screened for decolorization and it was found that the application of this enzymatic remediation system is not limited to a certain structural group of dyes. Anthrachinonic dyes (Lanaset Blue 2R, Terasil Pink 2GLA), some azo dyes, Indigo Carmine, and the triphenylmethane dye Crystal Violet were efficiently decolorized. However, the laccase displayed pronounced substrate specificities when a range of structurally related model azodyes was subjected to the biotransformation. Azodyes containing hydroxy groups in ortho or para position relative to the azo bond were preferentially oxidized. The reactor performance was studied more closely using Indigo Carmine.
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PMID:Study of dye decolorization in an immobilized laccase enzyme-reactor using online spectroscopy. 1528 93

Cyanide is commonly found as ferrocyanide [Fe(II)(CN)(6)](-4) and in the more mobile form, ferricyanide [Fe(III)(CN)(6)](-3) in contaminated soils and sediments. Although soil minerals may influence ferrocyanide speciation, and thus mobility, the possible influence of soil enzymes has not been examined. In a series of experiments conducted under a range of soil-like conditions, laccase, a phenoloxidase enzyme derived from the fungi Trametes versicolor, was found to exert a large influence on iron-cyanide speciation and mobility. In the presence of laccase, up to 93% of ferrocyanide (36-362ppm) was oxidized to ferricyanide within 4h. No significant effect of pH (3.6 and 6.2) or initial ferrocyanide concentration on the extent or rate of oxidation was found and ferrocyanide oxidation did not occur in the absence of laccase. Relative to iron-cyanide-mineral systems without laccase, ferrocyanide adsorption to aluminum hydroxide and montmorillonite decreased in the presence of laccase and was similar to or somewhat greater than that of ferricyanide without laccase. Laccase-catalyzed conversion of ferrocyanide to ferricyanide was extensive though up to 33% of the enzyme was mineral-bound. These results demonstrate that soil enzymes can play a major role in ferrocyanide speciation and mobility. Biotic soil components must be considered as highly effective oxidation catalysts that may alter the mobility of metals and metal complexes in soil. Immobilized enzymes should also be considered for use in soil metal remediation efforts.
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PMID:Influence of a soil enzyme on iron-cyanide complex speciation and mineral adsorption. 1784 13

Glucose/O(2) biofuel cells (BFCs) with an improved power density and stability were developed, using glucose oxidase (GOD) nanotubes with polypyrrole (PPy)-carbon nanotubes (CNTs)-GOD layers deposited on their surface as an anode and a PPy-laccase-2,2'-azinobis (3-ethylbenzothiazoline-6-sulfonate) diammonium salt (ABTS) film type cathode. The GOD nanotubes were fabricated within the nanopores of an anodized aluminum oxide membrane using a template-assisted layer-by-layer deposition method. These BFCs exhibited a higher volumetric power than the best performance reported previously; this was likely due to an increase in enzyme loading of GOD nanotubes and improved electrochemical properties of the PPy-CNTs-GOD layers. The stability of BFCs was closely related to the leakage of ABTS from the cathode. When the leakage of ABTS was suppressed, the power density of BFCs was nearly unchanged for at least 8 days under physiological conditions.
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PMID:Glucose oxidase nanotube-based enzymatic biofuel cells with improved laccase biocathodes. 2337 23

Laccases play an important role in the degradation of soil phenol or phenol-like substance and can be potentially used in soil remediation through immobilization. Iron and aluminum minerals can adsorb extracellular enzymes in soil environment. In the present study, we investigated the adsorptive interaction of laccase, from the white-rot fungus Trametes versicolor, with soil iron and aluminum minerals and characterized the properties of the enzyme after adsorption to minerals. Results showed that both soil iron and aluminum minerals adsorbed great amount of laccase, independent of the mineral specific surface areas. Adsorbed laccases retained 26-64% of the activity of the free enzyme. Compared to the free laccase, all adsorbed laccases showed higher Km values and lower Vmax values, indicating a reduced enzyme-substrate affinity and a lower rate of substrate conversion in reactions catalyzed by the adsorbed laccase. Adsorbed laccases exhibited increased catalytic activities compared to the free laccase at low pH, implying the suitable application of iron and aluminum mineral-adsorbed T. versicolor laccase in soil bioremediation, especially in acid soils. In terms of the thermal profiles, adsorbed laccases showed decreased thermal stability and higher temperature sensitivity relative to the free laccase. Moreover, adsorption improved the resistance of laccase to proteolysis and extended the lifespan of laccase. Our results implied that adsorbed T. versicolor laccase on soil iron and aluminum minerals had promising potential in soil remediation.
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PMID:Adsorption of Trametes versicolor laccase to soil iron and aluminum minerals: enzyme activity, kinetics and stability studies. 2422 44

By using a carbon-coated anodic aluminum oxide (CAAO) film as a monolithic porous electrode for the immobilization of Trametes laccases (LACs), an attempt is made to control the orientation of LAC molecules toward the electrode surface simply by applying an electric potential to the CAAO film. Because the resulting film is characterized by a myriad of open, simple, and straight nanochannels with diameters as large as 40 nm, the O2 diffusion problem in pores is minimized, thereby making it possible to highlight the effect of such orientation on the electrocatalytic activity as a biocathode. It has been evidenced that LAC molecules are favorably oriented for a smooth electron transfer from the electrode when the LACs are immobilized with applying a positive voltage to the electrode, and such favorable orientation exhibits 3.7-times higher electrocatalytic activity than unfavorable orientation. Furthermore, the orientation mechanism has been rationally explained in terms of local surface chemistry on a LAC molecule.
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PMID:Orientation Control of Trametes Laccases on a Carbon Electrode Surface to Understand the Orientation Effect on the Electrocatalytic Activity. 2995 51