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)

Activity of a number of enzymes related to lignin formation was measured in a Picea abies (L) Karsten suspension culture that is able to produce native-like lignin into the nutrient medium. This cell culture is an attractive model for studying lignin formation, as the process takes place independently of the complex macromolecular matrix of the native apoplast. Suspension culture proteins were fractionated into soluble cellular proteins, ionically and covalently bound cell wall proteins and nutrient medium proteins. The nutrient medium contained up to 5.3% of total coniferyl alcohol peroxidase (EC 1.11.1.7) activity and a significant NADH oxidase activity that is suggested to be responsible for hydrogen peroxide (H2O2) production. There also existed some malate dehydrogenase (EC 1.1.1.37) activity in the apoplast of suspension culture cells (in ionically and covalently bound cell wall protein fractions), possibly for the regeneration of NADH that is needed for peroxidase-catalysed H2O2 production. However, there is no proof of the existence of NADH in the apoplast. Nutrient medium peroxidases could be classified into acidic, slightly basic and highly basic isoenzyme groups by isoelectric focusing. Only acidic peroxidases were found in the covalently bound cell wall protein fraction. Several peroxidase isoenzymes across the whole pI range were detected in the protein fraction ionically bound to cell walls and in the soluble cellular protein fraction. One laccase-like isoenzyme with pI of approximately 8.5 was found in the nutrient medium that was able to form dehydrogenation polymer from coniferyl alcohol in the absence of H2O2. The total activity of this oxidase towards coniferyl alcohol was, however, several orders of magnitude smaller than that of peroxidases in vitro. According to 2D 1H-13C correlation NMR spectra, most of the abundant structural units of native lignin and released suspension culture lignin are present in the oxidase produced dehydrogenation polymer but in somewhat different amounts compared to peroxidase derived synthetic lignin preparations. A coniferin beta-glucosidase (EC 3.2.1.21) was observed to be secreted into the culture medium.
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PMID:Lignification related enzymes in Picea abies suspension cultures. 1206 Feb 56

The amplification cycle consisting of NADH independent oligosaccharide dehydrogenase (ODH) and laccase has been recently reported to be highly sensitive to several catecholamines and p-aminophenol. A competitive immunoassay for 2,4-dichlorophenoxyacetic acid has been developed by combining this amplification cycle with beta-galactosidase as enzyme label resulting in p-aminophenol as product. The combination of enzymatic amplification cycles with a competitive immunoassay yields a highly sensitive measurement of 2,4-dichlorophenoxyacetic acid. Using a monoclonal antibody the linear range of the assay was between 0.02 and 100 ng/l and the c(50) was found at 0.2 ng/l; the detection limit was at 5 pg/l (25 fmol/l) corresponding to 5 amol.
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PMID:High sensitive competitive immunodetection of 2,4-dichlorophenoxyacetic acid using enzymatic amplification with electrochemical detection. 1504 3

In recent years, use of microbial biomass for decolourization of textile industry wastewater is becoming a promising alternative in which some bacteria and fungi are used to replace present treatment processes. Saccharomyces cerevisiae MTCC 463 decolourized the triphenylmethane dyes (malachite green, cotton blue, methyl violet and crystal violet) by biosorption, showing different decolourization patterns. However, malachite green decolourized by biosorption at the initial stage and further biodegradation occurred, about 85% in plain distilled water within 7 h, and about 95.5% in 5% glucose medium within 4 h, under aerobic conditions and at room temperature. Decolourization of malachite green depends on various conditions, such as concentration of dye, concentration of cells, composition of medium and agitation. HPLC, UV-VIS, FTIR and TLC analysis of samples extracted with ethyl acetate from decolourized culture flasks confirmed the biodegradation of malachite green into several metabolites. A study of the enzymes responsible for the biodegradation of malachite green in the control and cells obtained after decolourization showed the activities of laccase, lignin peroxidase, NADH-DCIP reductase, malachite green reductase and aminopyrine N-demethylase in control cells. A significant increase in the activities of NADH-DCIP reductase and MG reductase was observed in the cells obtained after decolourization, indicating a major involvement of reductases in malachite green degradation.
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PMID:Biotransformation of malachite green by Saccharomyces cerevisiae MTCC 463. 1654 73

Saccharomyces cerevisiae MTCC 463 decolourizes toxic azo dye, methyl red by degradation process. Methyl red (100mgl(-1)) is degraded completely within 16min in plain distilled water under static anoxic condition, at the room temperature. Effect of physicochemical parameters (pH of medium, composition of medium, concentration of cells, concentration of dye, temperature and agitation) on methyl red decolourization focused the optimal condition required for decolourization. Biodegradation (fate of metabolism) of methyl red in plain distilled water was found to be pH dependent. Cells of Saccharomyces cerevisiae could degrade methyl red efficiently up to 10 cycles in plain distilled water. Analysis of samples extracted with ethyl acetate from decolourized culture flasks in plain distilled water (pH 6.5) and at pH 9 using UV-VIS, TLC, HPLC and FTIR confirm biodegradation of methyl red into several different metabolites. A study of the enzymes responsible for the biodegradation of methyl red in the control and cells obtained after decolourization in plain distilled water (pH 6.5) and at pH 9 showed different levels of the activities of laccase, lignin peroxidase, NADH-DCIP reductase, azoreductase, tyrosinase and aminopyrine N-demethylase. A significant increase in the activities of lignin peroxidase and NADH-DCIP reductase was observed in the cells obtained after decolourization in plain distilled water (pH 6.5), however cells obtained at pH 9 shows increased activities of azoreductase, tyrosinase, lignin peroxidase and NADH-DCIP reductase. High efficiency to decolourize methyl red in plain distilled water and low requirement of environmental conditions enables this yeast to be used in biological treatment of industrial effluent containing azo dye, methyl red.
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PMID:Decolourization of azo dye methyl red by Saccharomyces cerevisiae MTCC 463. 1729 52

A novel bacterial species identified as Exiguobacterium sp. RD3 degraded the diazo dye reactive yellow 84A (50 mg l(-1)) within 48 h at static condition, at 30 degrees C and pH 7. Lower salinity conditions were found to be favorable for growth and decolorization. Enzymatic activities of an H(2)O(2) independent oxidase along with laccase and an azoreductase suggest their prominent role during the decolorization of reactive yellow 84A. Presence of an H(2)O(2) independent oxidase in Exiguobacterium sp. RD3 was confirmed and hydrogen peroxide produced was detected by a coupled iodometric assay. Azoreductase activity was prominent in presence of cofactors NADH and NADP in mineral salt medium. Considerable depletion of COD of the dye solution during degradation of dye was indicative of conversion of complex dye into simple oxidizable products. Products of degradation were analyzed by HPLC, FTIR and GCMS. A possible product of the degradation was identified by GCMS. Degradation of dye resulted with significant reduction of phytotoxicity, confirming the environmentally safe nature of the degradation metabolites.
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PMID:Coordinate action of exiguobacterial oxidoreductive enzymes in biodegradation of reactive yellow 84A dye. 1880

This study demonstrates a novel compartment-less glucose/O(2) biofuel cell (BFC) based on highly ordered mesoporous carbons (OMCs) with three-dimensionally (3D) interconnected and ordered pore structures. OMCs are used as supports for both stably confining the electrocatalyst (i.e., meldola's blue, MDB) for NADH oxidation and the anodic biocatalyst (i.e., NAD(+)-dependent glucose dehydrogenase, GDH) for glucose oxidation, and for facilitating direct electrochemistry of the cathodic biocatalyst (i.e., laccase, LAC) for O(2) electroreduction. In 0.10 M pH 6.0 PBS containing 20 mM NAD(+) and 60 mM glucose under the air-saturated atmosphere, the open circuit voltage (0.82 V) and the maximum power output (38.7 microW cm(-2) (at 0.54 V)) of the assembled compartment-less OMCs-based BFC are both higher than those of carbon nanotubes (CNTs)-based BFC (0.75 V and 2.1 microW cm(-2) (at 0.46 V)). These may make OMCs to be another kind of robust and advanced carbon electrode material besides CNTs for BFCs applications.
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PMID:Highly ordered mesoporous carbons-based glucose/O2 biofuel cell. 1932 30

Bacillus sp. VUS decolorized azo dye Navy blue 2GL in 48 h at static anoxic condition in yeast extract medium, whereas it took only 18 h for the decolorization in presence of CaCl(2). Different inducers played role in the decolorization of Navy blue 2GL. CaCl(2) found to be the most effective inducer among all inducers tested. The activity of enzymes like lignin peroxidase, laccase and reductases viz. NADH-DCIP, azo and riboflavin induced during decolorization represents their role in the biodegradation. Extracellular LiP and intracellular laccase activity induced with CaCl(2). Yeast extract was best medium for faster decolorization than other media. UV-vis spectrophotometer analysis and visual examinations showed decolorization of dye. High performance liquid chromatography, Fourier transforms infrared spectroscopy showed degradation of dye. Gas Chromatography-Mass Spectroscopy revealed formation of 4-Amino-3-(2-bromo-4, 6-dinitro-phenylazo)-phenol and acetic acid 2-(-acetoxy-ethylamino)-ethyl ester as final products. Bacillus sp. VUS also decolorized synthetic effluent. Phytotoxicity study showed detoxification of Navy blue 2GL.
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PMID:Effect of inducers on the decolorization and biodegradation of textile azo dye Navy blue 2GL by Bacillus sp. VUS. 1946 42

Brevibacillus laterosporus MTCC 2298 was screened for the decolorization of eight triphenylmethane dyes. Decolorization of malachite green was found to be fastest (87% within 3 hours, at the concentration 0.1 g/L) among the screened dyes. Various triphenylmethane dyes showed differential induction patterns of the dye-degrading enzymes. The activities of the laccase, nicotinamide adenine dinucleotide-dichlorophenolindophenol reductase (NADH-DCIP reductase), malachite green reductase, and aminopyrine N-demethylase were increased in the cell-free extract obtained after decolorization of malachite green. Fourier transform infrared spectral analysis indicated formation of N-demethylated products, including primary and secondary aryl amines. High-performance liquid chromatography analysis confirmed the transformation of malachite green into new metabolites rather than its reduced form, leucomalachite green. Gas chromatography-mass spectroscopy analysis detected new degradation products, such as reduced tetradesmethyl leucomalachite green (m/z 283) and [4-(1-cyclohexyl)-(1'-phenyl)-methyl]-2, 4-hexenoic acid (m/z 282). Complete decolorization of malachite green also was observed by the partially purified laccase from B. laterosporus.
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PMID:Biodegradation of malachite green by Brevibacillus laterosporus MTCC 2298. 1995 64

Dihydrolipoamide dehydrogenase (LPD), a useful biocatalyst for regenerating NAD(+), was purified from Microbacterium luteolum JCM 9174, and the gene encoding LPD was cloned from the genomic DNA. The gene contained an opening reading frame consisting of 1395 nucleotides encoding 465 amino acid residues with a predicted molecular weight of 49912.1 Da, which displayed 36-78% homology to known LPDs. Moreover, the FAD- and NAD(+)-binding sites and the two catalytic residues in the LPDs were conserved. The enzyme was expressed in recombinant Escherichia coli cells and purified to homogeneity by column chromatography. LPD of M. luteolum (MluLPD) accepted not only lipoamide but also some artificial electron acceptors such as dichlorophenolindophenol (DCIP) and nitrotetrazolium blue (NTB), that is, it functions as a diaphorase. NAD(+) demonstrated a strong activating effect on MluLPD, and the activity was 5.2 times higher than that without NAD(+). The enzyme was suitable for regenerating NAD(+) in biocatalytic reactions because of its high affinity for NADH (6.1 microM). An NAD(+)-regenerating system with MluLPD and laccase using 2,5-dimethoxy-1,4-benzoquinone as a hydrogen acceptor was demonstrated.
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PMID:Gene cloning and characterization of dihydrolipoamide dehydrogenase from Microbacterium luteolum: A useful enzymatic regeneration system of NAD+ from NADH. 2015 66

The objective of this study was to develop consortium using Pseudomonas sp. SUK1 and Aspergillus ochraceus NCIM-1146 to decolorize adsorbed dyes from textile effluent wastewater under solid state fermentation. Among various agricultural wastes rice bran showed dye adsorption up to 90, 62 and 80% from textile dye reactive navy blue HE2R (RNB HE2R) solution, mixture of textile dyes and textile industry wastewater, respectively. Pseudomonas sp. SUK1 and A. ochraceus NCIM-1146 showed 62 and 38% decolorization of RNB HE2R adsorbed on rice bran in 24h under solid state fermentation. However, the consortium of Pseudomonas sp. SUK1 and A. ochraceus NCIM-1146 (consortium-PA) showed 80% decolorization in 24h. The consortium-PA showed effective ADMI removal ratio of adsorbed dyes from textile industry wastewater (77%), mixture of textile dyes (82%) and chemical precipitate of textile dye effluent (CPTDE) (86%). Secretion of extracellular enzymes such as laccase, azoreductase, tyrosinase and NADH-DCIP reductase and their significant induction in the presence of adsorbed dye suggests their role in the decolorization of RNB HE2R. GCMS and HPLC analysis of product suggests the different fates of biodegradation of RNB HE2R when used Pseudomonas sp. SUK1, A. ochraceus NCIM-1146 and consortium PA.
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PMID:Decolorization of adsorbed textile dyes by developed consortium of Pseudomonas sp. SUK1 and Aspergillus ochraceus NCIM-1146 under solid state fermentation. 2141 20


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