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)

Selected isolates of fungi were grown on wheat straw and corncob in the presence of different moistening agents such as water, molasses, potato dextrose broth and distillery effluent. All the fungal isolates responded differently with respect to growth and ligninolytic enzyme production. Fungal growth on different substrates was checked by calculating ergosterol content, which varied widely within a single species when grown on different substrates. The maximum laccase production was obtained for Aspergillus flavus TERI DB9 grown on wheat straw with molasses. For manganese peroxidase, highest production was in Aspergillus niger TERI DB20 grown on corncob with effluent. Among the two isolates positive for lignin peroxidase, the highest production was in Fusarium verticillioides ITCC 6140. This immobilized fungal biomass was then used for decolorization of effluent from a cane molasses based distillery. Maximum decolorization (86.33%) was achieved in Pleurotus ostreatus (Florida) Eger EM 1303 immobilized on corncob with molasses in a period of 28 days.
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PMID:Enhanced production of ligninolytic enzymes and decolorization of molasses distillery wastewater by fungi under solid state fermentation. 1717 4

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

The white-rot fungus Trametes versicolor decolorized the mono-azo-substituted naphthalenic dye Amaranth. The relationship between the amount of enzymes present in the system and the efficiency of the decoloration process was investigated. The two responses used to quantify the process of decoloration (i.e., initial decoloration rate, v0, and the percent concentration of dye decolorized in 1 h, %c) were correlated with the amount of three enzymes considered for the study (lignin peroxidase, manganese peroxidase, and laccase) and analyzed through stepwise regression analysis (forward, backward, and mixed). The results of the correlation analysis and those of the regression analysis indicated that lignin peroxidase is the enzyme having the greatest influence on the two responses.
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PMID:Decoloration of Amaranth by the white-rot fungus Trametes versicolor. Part I. Statistical analysis. 1749 81

The involvement of lignin peroxidase (LiP) in the decoloration of the mono-azo substituted napthalenic dye Amaranth was investigated with pure enzymes and whole cultures of Trametes versicolor. The verification study confirmed that LiP has a direct influence on the initial decoloration rate and showed that another enzyme, which does not need hydrogen peroxide to function and is not a laccase, also plays a role during decoloration. These results confirm the results of a previous statistical analysis. Furthermore, the fungal mycelium affects the performance of the decoloration process.
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PMID:Decoloration of Amaranth by the white-rot fungus Trametes versicolor. Part II. Verification study. 1749 82

Due to production of lignocellulose-degrading enzymes, saprotrophic litter-decomposing basidiomycetes can significantly contribute to the turnover of soil organic matter. The production of lignin and polysaccharide-degrading enzymes and changes in the chemical composition of litter was studied with Marasmius quercophilus, Mycena inclinata and Pholiota lenta, three basidiomycete species typical of oak (Quercus petraea) forests. Within 12weeks of incubation, M. inclinata decomposed 33%, M. quercophilus 36% and P. lenta 48% of the substrate dry mass. All fungi produced laccase and Mn-peroxidase and none of them produced lignin peroxidase or Mn-independent peroxidases. M. inclinata and M. quercophilus produced considerable laccase activity, while production by P. lenta was low. M. quercophilus and P. lenta produced most Mn-peroxidase at the beginning of the experiment, while the production by M. inclinata was more stable in time. Endo-1,4-beta-xylanase exhibited the highest activity among endocleaving glycosyl hydrolases while 1,4-beta-glucosidase was the main exocleaving enzyme. All fungi decreased the C:N ratio of the litter from 27 to 13-17 and M. inclinata and M. quercophilus also decreased the lignin content. Analytical pyrolysis of decayed litter showed changes in litter composition similar to those caused by white-rot fungi during wood decay, e.g. a decrease in the syringyl/guaiacyl lignin ratio. These changes were more pronounced in M. inclinata and M. quercophilus. The results indicate that different litter-decomposing fungi can cause substantial litter transformation despite considerable differences in the production of lignocellulose-degrading enzymes.
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PMID:Differential degradation of oak (Quercus petraea) leaf litter by litter-decomposing basidiomycetes. 1753 15

Lentinula edodes is considered an alternative recycling agent for agricultural wastes, and there have been several studies to understand the relationship between its growth and ligninolytic activity. We tested the effect of wood from viticulture pruning, extracted with solvents of differing polarity, on the biomass production and activity pattern of ligninolytic enzymes. The analysis was done by measuring the mycelial dry mass and enzyme activity of liquid growth medium during the culture of L. edodes, adding either single extracts or a combination of extracts. Polar extracts enhanced mycelial production, and the activity patterns of lignin peroxidase, manganese peroxidase, aryl alcohol oxidase, and laccase were comparable to their activities predicted by ligninolysis models proposed for other fungi. We conclude that the polar extracts could be useful for enhancing fungal biomass production and for modifying lignin degradation because the regulation of ligninolytic enzyme activity is differentially influenced by the polarity of the extract.
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PMID:Polar vineyard pruning extracts increase the activity of the main ligninolytic enzymes in Lentinula edodes cultures. 1802 7

Soil samples collected from the vicinity of "Manpasand textile industry", located near Ichalkaranji, India were studied for screening and isolation of bacterial strains capable of degradation of textile dyes. A potential strain was selected on the basis of rapid dye degradation and later identified as Comamonas sp. UVS. Comamonas sp. UVS showed 100% decolorization of Direct Red 5B (DR5B) dye at 40 degrees C and pH 6.5. The maximum Direct Red 5B concentration decolorized was 1,100 mg/l in nutrient broth within 125 h. A numerical simulation with the Michaelis-Menten kinetics model gives an optimal value of 16.01+/-0.36 mg dye/g cell/h for maximum rate (V(max)) and 7.97+/-0.21 mg/l for the Michaelis constant (K(m)). The induction in the activities of laccase and LiP was observed during decolorization. These enzymes were inhibited by the addition of sodium azide. The biodegradation was monitored by UV-vis, FTIR spectroscopy and HPLC. The GCMS analysis indicated the presence of 7-benzoylamino-3-diazenyl-4-hydroxy-naphthalene-2-sulfonic acid in degraded product of the dye. The germination of Triticum aestivum seeds was inhibited with DR5B treatment but not with the treatment of dye degradation products.
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PMID:Biodegradation of Direct Red 5B, a textile dye by newly isolated Comamonas sp. UVS. 1832

Trametes pubescens and Pleurotus ostreatus, immobilized on polyurethane foam cubes in bioreactors, were used to decolorize three industrial and model dyes at concentrations of 200, 1000 and 2000 ppm. Five sequential cycles were run for each dye and fungus. The activity of laccase, Mn-dependent and independent peroxidases, lignin peroxidase, and aryl-alcohol oxidase were daily monitored during the cycles and the toxicity of media containing 1000 and 2000 ppm of each dye was assessed by the Lemna minor (duckweed) ecotoxicity test. Both fungi were able to efficiently decolorize all dyes even at the highest concentration, and the duckweed test showed a significant reduction (p < or = 0.05) of the toxicity after the decolorization treatment. T. pubescens enzyme activities varied greatly and no clear correlation between decolorization and enzyme activity was observed, while P. ostreatus showed constantly a high laccase activity during decolorization cycles. T. pubescens showed better decolorization and detoxication capability (compared to the better known P. ostreatus). As wide differences in enzyme activity of the individual strains were observed, the strong decolorization obtained with the two fungi suggested that different dye decolorization mechanisms might be involved.
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PMID:Decolorization and detoxication of reactive industrial dyes by immobilized fungi Trametes pubescens and Pleurotus ostreatus. 1848 Dec 17

The objective of this study was to exploit the decolorization potential of a newly isolated white-rot fungus Schizophyllum commune IBL-6 for the biodegradation of reactive textile dye Cibacron Red FN-2BL. In the initial decolorization study of 10 days, it was observed that S. commune IBL-6 was a better decolorizer of Cibacron Red FN-2BL. Various process parameters like composition of basal nutrient medium, pH, temperature, additional carbon and nitrogen sources, and initial dyestuff concentration were optimized to develop an economic decolorization process. The optimum dye decolorization was achieved in basal nutrient medium II containing 0.1% Cibacron Red FN-2BL and supplemented with 1% glucose after 3 days incubation at pH 4.5 and 30 degrees C. All the additional carbon sources were found to enhance decolorization process, whereas most of the nitrogen supplements caused fungal-growth inhibition. The pattern of enzymes involved in the biodegradation of this dye was studied, and manganese peroxidase was found to be the major peroxidase with minor lignin peroxidase and laccase activities.
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PMID:Optimization of culture conditions for enhanced decolorization of cibacron red FN-2BL by Schizophyllum commune IBL-6. 1850 May 86

For hydrophobic ionic liquid 1-butyl-3-methylimidazolium hexafluorophosphate ([BMIM][PF(6)]), an H(2)O-in-[BMIM][PF(6)] microemulsion could be formed in the presence of nonionic surfactant Triton X-100 (TX-100). In such a medium, both lignin peroxidase (LiP) and laccase could express their catalytic activity with the optimum molar ratio of H(2)O to TX-100 at 8.0 for LiP and >20 for laccase, and the optimum pH values at 3.2 for LiP and 4.2 for laccase, respectively. As compared with pure or water saturated [BMIM][PF(6)], in which the two oxidases had negligible catalytic activity due to the strong inactivating effect of [BMIM][PF(6)] on both enzymes, the use of the [BMIM][PF(6)]-based microemulsion had some advantages. Not only the catalytic activities of both fungal oxidases greatly enhanced, but also the apparent viscosity of the medium decreased.
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PMID:Catalytic activities of fungal oxidases in hydrophobic ionic liquid 1-butyl-3-methylimidazolium hexafluorophosphate-based microemulsion. 1860 99


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