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)

A multicomponent protein complex containing manganese (II)-dependent peroxidase, laccase and beta-glucosidase was isolated from culture extracts of the white rot basidiomycete Lentinula edodes. This protein complex showed a single protein band on native polyacrylamide gel electrophoresis (PAGE). On sodium dodecyl sulfate (SDS)-PAGE, however, it displayed three major bands and several additional minor bands ranging in size from 60 kDa to 180 kDa, suggesting it being a complex of six to eight different proteins. The molecular mass of this complex was estimated to be approximately 660 kDa from the elution position of gel filtration. This enzyme complex was effective in transforming environmentally persistent xenobiotics, pentachlorophenol and 2,5-dichlorophenol.
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PMID:Lentinula edodes produces a multicomponent protein complex containing manganese (II)-dependent peroxidase, laccase and beta-glucosidase. 1142 71

The activities of carboxymethylcellulase and xylanase in the higher basidial fungus Cerrena unicolor grown in avicel-containing medium reached 1.95 and 1.50 units per mg protein, respectively, whereas in mannitol-containing medium they ranged from 0.02 to 0.05 units per mg protein. The activity of fungal beta-glucosidase depended on the carbon source in the culture medium and ranged from 2.1 units per mg protein in the presence of mannitol to 17.3 units per mg protein in the presence of avicel. In contrast to polysaccharides, easily metabolizable substrates (cellobiose, mannitol, and glucose) provided the highest rates of secretion of laccase (52.7-123.5 ncat per mg protein) and ligninase (22-106 units per mg protein). The addition of tangerine pomace, a substrate enriched with aromatic compounds, to the culture medium caused an increase in the rate of bio-synthesis of laccase and ligninase to 862 ncat per ml and 557 units per ml, respectively. Aromatic compounds such as p-xylidine and veratric aldehyde increased the laccase activity of C. unicolor IBB 62 from 7.9 to 23.6 and 18.3 ncat per mg protein, respectively. Veratryl alcohol caused a sevenfold increase in the activity of Mn-dependent peroxidase in the culture medium.
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PMID:[Dependence of activities of polysaccharide hydrolases and oxidases from Cerrena unicolor on the source of carbon and aromatic acids in culture media]. 1206 74

Activities of cellulolytic and hemicellulolytic enzymes endo-1,4-beta-glucanase, exo-1,4-beta-glucanase, 1,4-beta-glucosidase, endo-1,4-beta-xylanase, 1,4-beta-xylosidase and 1,4-beta-mannosidase and ligninolytic enzymes Mn-peroxidase and laccase were detected during the growth of the white-rot fungus Pleurotus ostreatus on wheat straw in the presence and absence of cadmium. The loss of substrate dry weight and Mn-peroxidase activity decreased with increasing Cd concentration, whereas the activities of endo-1,4-beta-glucanase, 1,4-beta-glucosidase and laccase were highly increased in the presence of metal. The onset of hemicellulose-degrading enzyme activity was delayed in the presence of cadmium. The degradation of a model synthetic dye Poly B-411 did not correspond to the activities of ligninolytic enzymes. This is the first report about 1,4-beta-mannosidase in P. ostreatus.
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PMID:Lignocellulose degradation by Pleurotus ostreatus in the presence of cadmium. 1267 Jun 86

The effect of the addition of the nonionic surfactant tributylphenyltetraethoxylate to culture media on pH and extracellular protein content, and on production of beta-glucosidase, xylanase, laccase, and manganese-dependent and -independent peroxidases by the edible fungus Pleurotus ostreatus was determined. The relationship between fermentation parameters and concentration of surfactant was assessed by multiple linear regression analysis, and the similarities and differences among the fermentation parameters were elucidated by principal component analysis. Calculations proved that except for xylanase all other cultivation parameters were significantly influenced by the surfactant, with the effect higher at higher surfactant concentrations. Surfactant increased the production of beta-glucosidase and inhibited laccase and manganese-dependent and -independent peroxidase activities.
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PMID:Effect of tributylphenyltetraethoxylate on enzyme production of Pleurotus ostreatus. 1290 30

Twenty-six species of aquatic hyphomycetes were isolated from woody sources (unidentified wood segments, leaf skeletons and neck of leaves and bark) in the North River Nile (Delta region). Alatospora acuminata, Anguillospora crassa, Flagellaspora penicillioides, Lunulospra curvula, Tetracladium marchalianum and Triscelophorus monosporus were the most common species. Temperature was the highest physico-chemical parameter affecting the aquatic hyphomycetes occurrence. Twelve species of hyphomycetes, isolated from woody substrates, were screened for their ability to produce extracellular lignocellulolytic enzymes on solid media. The enzymes tested included: endoglucanase, endoxylanase, beta-glucosidase, laccase, peroxidase, polyphenoloxidase, tyrosinase and beta-xylosidase. Three species, A. acuminata, F. penicillioides, T. monosporus, were positive for all tested enzymes. Also, A. longissima was positive for all enzymes except lignin-peroxidase. The ability to produce cellulase was 100% for all species while only, four species were positive for lignin-peroxidase. The ability of the species to produce other lignocellulotic enzyme ranged from 50% to 83%. Freshwater hyphomycetes have been shown to produce a rich array of enzymes able to degrade the polysaccharides of plant debris.
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PMID:Lignocellulolytic enzyme production by aquatic hyphomycetes species isolated from the Nile's delta region. 1518 Jan 56

In this study we examined the extracellular enzymatic activity of two white rot fungi (Phanerochaete chrysosporium and Trametes versicolor) in a soil extract broth in relation to differential degradation of a mixture of different concentrations (0-30 p.p.m.) of simazine, dieldrin and trifluralin under different osmotic stress (-0.7 and -2.8 MPa) and quantified enzyme production, relevant to P and N release (phosphomonoesterase, protease), carbon cycling (beta-glucosidase, cellulase) and laccase activity, involved in lignin degradation. Our results suggest that T. versicolor and P. chrysosporium have the ability to degrade different groups of pesticides, supported by the capacity for expression of a range of extracellular enzymes at both -0.7 and -2.8 MPa water potential. Phanerochaete chrysosporium was able to degrade this mixture of pesticides independently of laccase activity. In soil extract, T. versicolor was able to produce the same range of enzymes as P. chrysoporium plus laccase, even in the presence of 30 p.p.m. of the pesticide mixture. Complete degradation of dieldrin and trifluralin was observed, while about 80% of the simazine was degraded regardless of osmotic stress treatment in a nutritionally poor soil extract broth. The capacity of tolerance and degradation of high concentrations of mixtures of pesticides and production of a range of enzymes, even under osmotic stress, suggest potential bioremediation applications.
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PMID:Enzymatic activity, osmotic stress and degradation of pesticide mixtures in soil extract liquid broth inoculated with Phanerochaete chrysosporium and Trametes versicolor. 1568 95

Pleurotus ostreatus produces the cellulolytic and hemicellulolytic enzymes endo-1,4-beta-glucanase, exo-1,4-beta-glucanase, 1,4-beta-glucosidase, endo-1,4-beta-xylanase, 1,4-beta-xylosidase, endo-1,4-beta-mannanase and 1,4-beta-mannosidase and ligninolytic enzymes Mn-peroxidase and laccase during growth on wheat straw in the presence and absence of Cu, Mn, Pb, and Zn. This is the first report concerning endo-1,4-beta-mannanase in P. ostreatus. Although the concentrations of trace metals in wheat straw ranged from units to tens of microg g(-1), only 3-6% (Fe, Pb) or 30-45% (Cu, Mn, Zn) of the total amount was extractable and available for the fungus. The substrate colonization rate was only decreased by high concentrations of Cu and Zn; the loss of dry mass differed among treatments in the initial phase of fungal growth, and at the end of the experiment (day 98) it was significantly lower in metal-containing treatments (63-66%) than in the control (70%). The cellulolytic and hemicellulolytic enzyme were prone to a metal effect except for the increase in endo-1,4-beta-glucanase and 1,4-beta-glucosidase in the presence of Zn. Laccase activity was increased by all tested metals, and unlike other white-rot fungi, Mn-peroxidase levels were low in the presence of manganese.
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PMID:Degradation of lignocellulose by Pleurotus ostreatus in the presence of copper, manganese, lead and zinc. 1592 94

To evaluate the potential of using the enzymes from spent mushroom compost (SMC) as an industrial enzyme, the production of alpha-amylase, cellulase, beta-glucosidase, laccase, and xylanase was determined from the SMC of four edible mushroom species (Pleurotus ostreatus, Lentinula edodes, Flammulina velutipes and Hericium erinaceum). Among the tested SMC, the SMC of L. edodes showed the highest enzyme activity in alpha-amylase (229 nkat/g), cellulase (759 nkat/g) and beta-glucosidase (767 nkat/g) in 0.5% Triton X-100, and that of P. ostreatus showed the highest activity in laccase (1452 nkat/g) in phosphate-buffered 0.2% Triton X-100. The highest xylanase activity (119 nkat/g) was found in the SMC of F. velutipes.
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PMID:Detection and recovery of hydrolytic enzymes from spent compost of four mushroom species. 1611 Sep 12

Liquid cultures with cellulose and solid state fermentation cultures on wheat straw of the white-rot fungi Pleurotus ostreatus and Trametes versicolor and the brown-rot fungus Piptoporus betulinus were assayed for the free and solid fraction-bound activity of lignocellulose-degrading enzymes. The majority of the ligninolytic enzymes laccase and Mn peroxidase was detected in the free fraction of P. ostreatus and T. versicolor. The endocleaving enzymes endo-1,4-beta-glucanase, endo-1,4-beta-mannanase and endo-1,4-beta-xylanase were detected almost exclusively in the free fraction, while significant amounts of 1,4-beta-glucosidase, cellobiohydrolase, 1,4-beta-xylosidase and 1,4-beta-mannosidase were present in the bound fraction depending on the mode of cultivation and the species. The bound enzymes accounted for 66% of the total activity in P. ostreatus straw cultures, 35% in T. versicolor and only 8% in P. betulinus. The enzymes also showed significant differences in freeze-drying stability. Hydrolases in general showed high stability, whereas laccase and Mn peroxidase of P. ostreatus were the least stable.
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PMID:Estimation of bound and free fractions of lignocellulose-degrading enzymes of wood-rotting fungi Pleurotus ostreatus, Trametes versicolor and Piptoporus betulinus. 1612 11

Dimethyl sulfoxide (DMSO) is commonly used as a co-solvent to dissolve poorly water-soluble biologically active agents to assess their biological activities such as for enzyme induction. The question addressed was whether DMSO can be assumed to be an inert co-solvent. The influence of DMSO on the production of extracellular enzymes by Pleurotus ostreatus was investigated. DMSO functioned as either an inducer or a repressor, depending on the enzyme studied. The production of laccase and endo-1,4-beta-xylanase increased by 29 and 250%, respectively, in presence of DMSO. However, DMSO repressed the activities of manganese peroxidase, beta-glucosidase, beta-xylanase, and endo-1,4-beta-glucanase by 30, 33, 99 and 16%, respectively. These results raise concerns about the interpretation of bioactivity measurements when DMSO is assumed to function as an inert co-solvent to solubilize water-insoluble molecules.
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PMID:Influence of dimethyl sulfoxide on extracellular enzyme production by Pleurotus ostreatus. 1664 4


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