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 major laccase isoenzyme LAP2 secreted by the white-rot basidiomycete Trametes pubescens in response to high copper concentrations was purified to apparent electrophoretic homogeneity using anion-exchange chromatography and gel filtration. The monomeric protein has a molecular mass of 65 kDa, of which 18% is glycosylation, and a pI value of 2.6. The pH optima of the laccase depend on the substrates oxidized and show bell-shaped pH activity profiles with an optimum of 3-4.5 for phenolic substrates such as 2,6-dimethoxyphenol or syringaldazine, while the non-phenolic substrates ABTS [2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)] and ferrocyanide show a monotonic pH profile with a rate increasing with decreasing pH. The catalytic efficiencies k(cat)/K(m) determined for some of its substrates were 48 x 10(6), 47 x 10(6), 20 x 10(6) and 7 x 10(6) M(-1) s(-1) for ABTS, syringaldazine, ferrocyanide and oxygen, respectively. Furthermore, the gene lap2 encoding the purified laccase was cloned and its nucleotide sequence determined. The gene consists of 1997 bp, with the coding sequence interrupted by eight introns and flanked by an upstream region in which putative CAAT, TATA, MRE and CreA consensus sequences were identified. Based on Northern analysis containing total RNA from both induced and uninduced cultures, expression of lap2 is highly induced by copper, which is also corroborated by an increase in laccase activity in response to copper. A stimulating effect of various other heavy metal ions on laccase synthesis was also observed. In addition to induction, a second regulatory mechanism seems to be repression of lap2 transcription by glucose.
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PMID:Characterization of the major laccase isoenzyme from Trametes pubescens and regulation of its synthesis by metal ions. 1210 3

The effects of the carbon and nitrogen sources, initial pH and incubation temperature on laccase production by Trametes modesta were evaluated using the one-factor-at-a-time method. The final optimisation was done using a central composite design resulting in a four-fold increase of the laccase activity to 178 nkat ml(-1). Response-surface analysis showed that 7.34 g l(-1) wheat bran, 0.87 g l(-1) glucose, 2.9 g l(-1) yeast extract, 0.25 g l(-1) ammonium chloride, an initial pH of 6.95 and an incubation temperature of 30.26 degrees C were the optimal conditions for laccase production. Laccase produced by T. modesta was fully active at pH 4 and at 50 degrees C. The laccase was very stable at pH 4.5 and at 40 degrees C but half-lives decreased to 120 and 125 min at higher temperature (60 degrees C) and lower pH (pH 3).
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PMID:Production of laccase by a newly isolated strain of Trametes modesta. 1211 3

The ability of the ligninolytic fungus Trametes trogii to degrade in vitro different xenobiotics (PCBs, PAHs and dyes) was evaluated. Either 200 ppm of a PCB mixture (Aroclor 1150) or 160 ppm of an industrial PAH mixture (10% V/V of PAHs, principal components hexaethylbenzene, naphthalene, 1-methyl naphthalene, acenaphthylene, anthracene, fluorene and phenanthrene), were added to trophophasic and idiophasic cultures growing in a nitrogen limited mineral medium (glucose/asparagine) and in a complex medium (malt extract/glucose). Gas-liquid chromatography proved that within 7 to 12 d more than 90% of the organopollutants added were removed. The decrease in absorbance at 620 nm demonstrated that cultures of this fungus were able to transform 80% of the dye Anthraquinone-blue (added at a concentration of 50 ppm) in 1.5 h. Enzyme estimations indicated high activity of laccase (up to 0.55 U/mL), as well as lower production of manganese-peroxidase. Laccase activity, detected in all the conditions assayed, could be implicated in the degradation of these organopollutants. Considering the results obtained, T. trogii seems promising for detoxification.
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PMID:Degradation of environmental pollutants by Trametes trogii. 1241 98

Volvariella volvacea, strain V14, produces multiple forms of extracellular laccase when grown in submerged culture in a defined medium with glucose as sole carbon source, and on cotton waste 'compost' representative of the conditions used for industrial-scale mushroom cultivation. In liquid culture, enzyme synthesis is associated with the onset of secondary growth, and is positively regulated by copper (up to 200 microM CuSO(4)) and by various aromatic compounds. In solid-state systems, only low levels of laccase are detectable during the vegetative growth phase but enzyme activity increases sharply at the onset of fruiting and during sporophore development.
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PMID:Induction of laccase activity in the edible straw mushroom, Volvariella volvacea. 1258 10

A new enzyme has been isolated from leaves of the weed Tellima grandiflora (fringe cups, Saxifragaceae) that catalyzed the O(2)-dependent oxidation of 1,2,3,4,6-penta-O-galloyl-beta-D-glucopyranose to tellimagrandin II, the first intermediate in the (4)C(1)-glucose derived series of ellagitannins. CD-spectra revealed that the 4,6-O-HHDP-residue of the in vitro product had the (S)-stereoconfiguration characteristic of tellimagrandin II from natural sources. The enzyme, for which a M(r) of ca. 60,000 was determined, was purified to apparent homogeneity. It had a pH-optimum at pH 5.0, an isoelectric point at pH 6.3 and was most stable at pH 4.2. Inhibition studies suggested that this new enzyme, for which the systematic name 'pentagalloylglucose: O(2) oxidoreductase' is proposed, belongs to the vast group of laccase-type phenol oxidases (EC 1.10.3.2).
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PMID:Oxidation of pentagalloylglucose to the ellagitannin, tellimagrandin II, by a phenol oxidase from Tellima grandiflora leaves. 1262 Mar 41

The aim of this work was to study the growth and production of ligninolytic enzymes by Fomes sclerodermeus using a natural medium based on wheat bran as the principal substrate in a solid-state fermentation. Growth was monitored by measuring the chitin content in the substrate. The maximum rate of growth was observed between days 7 and 18. A 38% total dry-weight loss of the substrate was measured after 28 days of cultivation. Differential hydrolysis of the substrate revealed that cellulose was more extensively degraded than lignin. In the 28-day incubation period, the losses of cellulose and lignin were 38 and 15%, respectively. No lignin peroxidase activity was found in any of the media tested. The maximum manganese-dependent peroxidase activity recorded was 6.3 U g(-1) at 14 days, while the maximum laccase activity was 270 U g(-1) at 28 days post-inoculation. Addition of commonly used inducers such as copper or manganese did not produce a further increase in the enzyme activities, nor did addition of glucose, asparagine, or malt extract.
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PMID:Production of laccase and manganese peroxidase by Fomes sclerodermeus grown on wheat bran. 1271 52

A well-known industrial fungus for enzyme production, Aspergillus niger, was selected to produce the feruloyl esterase FAEA by homologous overexpression for pulp bleaching application. The gpd gene promoter was used to drive FAEA expression. Changing the nature and concentration of the carbon source nature (maltose to glucose; from 2.5 to 60 g l(-1)), improved FAEA activity 24.5-fold and a yield of 1 g l(-1) of the corresponding protein in the culture medium was achieved. The secreted FAEA was purified 3.5-fold to homogeneity in a two-step purification procedure with a recovery of 69%. The overproduced protein was characterised and presented properties in good agreement with those of native FAEA. The recombinant FAEA was tested for wheat straw pulp bleaching, with or without a laccase mediator system and xylanase. Best results were obtained using a bi-sequential process with a sequence including xylanase, FAEA and laccase, and yielded very efficient delignification--close to 75%--and a kappa number of 3.9. This is the first report on the potential application of recombinant FAEA in the pulp and paper sector.
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PMID:Overproduction of the Aspergillus niger feruloyl esterase for pulp bleaching application. 1274 52

The influence of carbohydrates: glucose, fructose, galactose, galacturonic acid, xylose, lactose, sucrose, pectin and inulin, were evaluated as sole carbon source for the production of laccases by the ascomycete, Botryosphaeria sp. Veratryl alcohol, a laccase inducer, was added to culture media to study inducible laccase production on the same carbon sources. Inulinase and pectinase were also produced when Botryosphaeria sp. was grown on inulin, and galacturonic acid and pectin, respectively, and their levels were less in the presence of veratryl alcohol. Botryosphaeria sp. produced constitutive laccases on all carbon sources examined, and veratryl alcohol increased the laccase production on most of carbon sources studied except for inulin and galacturonic acid. Evidence is presented that Botryosphaeria sp. is also pectinolytic.
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PMID:The effect of carbohydrate carbon sources on the production of constitutive and inducible laccases by Botryosphaeria sp. 1296 81

The decolorizing capacity of 26 white rot fungi from Argentina was investigated. Extracellular production of ligninolytic enzymes by mycelium growing on solid malt extract/glucose medium supplemented with different dyes (Malachite Green, Azure B, Poly R-478, Anthraquinone Blue, Congo Red and Xylidine), dye decolorization and the relationship between these two processes were studied. Only ten strains decolorized all the dyes, all ten strains produced laccase, lignin peroxidase and manganese peroxidase on solid medium. However, six of the strains could not decolorize any of the dyes; all six strains tested negative for lignin peroxidase, and produced less than 0.05 U/g agar of manganese peroxidase. Comparing the isolates with the well-known dye-degrader Phanerochaete chrysosporium, a new fungus was identified: Coriolus versicolor f. antarcticus, potentially a candidate for use in biodecoloration processes. Eighteen day-old cultures of this fungus were able to decolorize in an hour 28%, 30%, 43%, 88% and 98% of Xylidine (24 mg/l), Poly R-478 (75 mg/l), Remazol Brilliant Blue R (9 mg/l), Malachite Green (6 mg/l) and Indigo Carmine (23 mg/l), respectively. Laccase activity was 0.13 U/ml, but neither lignin peroxidase nor manganese peroxidase were detected in the extracellular fluids for that day of incubation.
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PMID:Evaluation of Argentinean white rot fungi for their ability to produce lignin-modifying enzymes and decolorize industrial dyes. 1515 9

Constant laccase activities were detected in culture supernatant of newly isolated basidiomycete Trametes gallica. Tryptone and glucose have great effects on the production of laccase. Two laccase isoenzymes (Lac I and Lac II) produced by T. gallica were purified to homogeneity (51- and 50-fold, respectively) by gel filtration chromatography, anion exchange chromatography, and improved native PAGE, with an overall yield of 24.8%. Lac I and Lac II from this fungus are glycoproteins with 3.6% and 4% carbohydrate content, the same molecular masses (by SDS-PAGE) of 60 kDa, and the pI of 3.1 and 3.0, respectively. Native gel electrophoresis indicates that the two laccases have different migration ratios. Lac I and Lac II have the same optimal pH of 3.0 on 2,6-dimethoxyphenol (DMP), pH 2.2 on 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), and of pH 4.0 on guaiacol. The highest rate of ABTS oxidation for both laccases was reached at 70 degrees C. Both laccases are stable from pH 6 to 9, retaining 88-90% activity after 24 hr incubation, and show good stability when incubated at temperatures lower than 40 degrees C. The Km values of Lac I for ABTS, DMP, and guaiacol are 0.118 x 10(-2), 0.420, and 0.405 mM, respectively; the Km values of Lac II for ABTS, DMP, and guaiacol are 0.086 x 10(-2), 0.41, and 0.40 mM, respectively. Their N-terminal sequences are determined and show strong similarity with those from other basidiomycetes. Graphite-furnace atomic absorption analysis revealed that both laccases have four copper atoms per protein molecule, but they have no type I copper signal at around 600 nm and a type III copper signal near 330 nm. Cyanide, azide, and halides completely inhibit the enzyme activity, whereas EDTA has less inhibition.
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PMID:Purification and characterization of two laccase isoenzymes from a ligninolytic fungus Trametes gallica. 1519 12


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