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)

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

Cross-linking enzymes generate covalent bonds in and between food biopolymers. These enzymes are interesting tools for tailoring dough and bread structures, as the characteristics of the biopolymers significantly determine the viscoelastic and fracture properties of dough and bread. In this study, the influence of oxidative cross-linking enzymes, tyrosinase from the filamentous fungus Trichoderma reesei and laccase from the white rot fungus Trametes hirsuta, on dough and bread were examined. Oxidation of low molecular weight phenolic model compounds of flour, cross-linking of gluten proteins, dough rheology, and bread making were characterized during or after the enzymatic treatments. In the dough and bread experiments, laccase and tyrosinase were also studied in combination with xylanase. Of the model compounds tyrosine, p-coumaric acid, caffeic acid, ferulic acid, and Gly-Leu-Tyr tripeptide, tyrosinase oxidized all except ferulic acid. Laccase was able to oxidize each of the studied compounds. The phenolic acids were notably better substrates for laccase than l-tyrosine. When the ability of the enzymes to cross-link isolated gliadin and glutenin proteins was studied by the SDS-PAGE analysis, tyrosinase was found to cross-link the gliadin proteins effectively, whereas polymerization of the gliadins by laccase was observed only when a high enzyme dosage and prolonged incubation were used. Examination of large deformation rheology of dough showed that both laccase and tyrosinase made doughs harder and less extensible, and the effects increased as a function of the enzyme dosage. In bread making, interestingly, the pore size of the breads baked with tyrosinase turned out to be remarkably larger and more irregular when compared to that of the other breads. Nevertheless, both of the oxidative enzymes were found to soften the bread crumb and increase the volume of breads, and the best results were achieved in combination with xylanase.
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PMID:Elucidating the mechanism of laccase and tyrosinase in wheat bread making. 1760 67

Tomato pomace and pectin were used as the sole carbon sources for the production of polygalacturonase from a strain of Coriolus versicolor in submerged culture. The culture of C. versicolor grown on tomato pomace exhibited a peak of polygalacturonase activity (1,427 U/l) on the third day of culture with a specific activity of 14.5 U/mg protein. The production of polygalacturonase by C. versicolor grown on pectin as a sole carbon source increased with the time of cultivation, reaching a maximum activity of 3,207 U/l of fermentation broth with a specific activity of 248 U/mg protein. The levels of different isoenzymes of polygalacturonase produced during the culture growth were analysed by native PAGE. Differential chromatographic behaviour of lignocellulosic enzymes produced by C. versicolor (i.e. polygalacturonase, xylanase and laccase) was studied on immobilized metal chelates. The effect of ligand concentration, pH, the length of spacer arm and the nature of metal ion were studied for enzyme adsorption on immobilized metal affinity chromatography (IMAC). The adsorption of these lignocellulosic enzymes onto immobilized metal chelates was pH-dependent since an increase in protein adsorption was observed as the pH was increased from 6.0 to 8.0. The adsorption of polygalacturonase as well as other enzymes to immobilized metal chelates was due to coordination of histidine residues which are available at the protein surface since the presence of imidazole in the equilibration buffer abolished the adsorption of the enzyme to immobilized metal chelates. A one-step purification of polygalacturonase from C. versicolor was devised by using a column of Sepharose 6B-EPI 30-IDA-Cu(II) and purified enzyme exhibited a specific activity of about 150 U/mg protein, final recovery of enzyme activity of 100% and a purification factor of about 10. The use of short spacer arm and the presence of imidazole in equilibration buffer exhibited a higher selectivity for purification of polygalacturonase on this column with a high purification factor. The purified enzyme preparation was analysed by SDS-PAGE as well as by "in situ" detection of enzyme activity.
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PMID:Production of polygalacturonase from Coriolus versicolor grown on tomato pomace and its chromatographic behaviour on immobilized metal chelates. 1825 72

Commercial mushroom tyrosinase contains other proteins, enzymes, carbohydrates, and phenolic material besides tyrosinase. Carbohydrate and phenolic material comprise a large percentage of the powder resuspensions derived from Agaricus bisporus. Enzyme assays identified the presence of tyrosinase, laccase, beta-glucosidase, beta-galactosidase, beta-xylosidase, cellulase, chitinase, xylanase, and mannanase in the commercial tyrosinase. Protein sequencing indicated the presence of tyrosinase, a lectin, and a putative mannanase as well as 10 unidentified protein/peptides in the commercial tyrosinase preparations. Characteristics of tyrosinase isoforms were similar in two different commercial tyrosinase sources. Inhibition studies indicated that I 50 values for some tyrosinase inhibitors were different when the crude powder was compared to a partially purified tyrosinase. The presence of these contaminants has the potential to affect studies using commercial tyrosinase.
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PMID:Enzyme, protein, carbohydrate, and phenolic contaminants in commercial tyrosinase preparations: potential problems affecting tyrosinase activity and inhibition studies. 1850 Aug 13

The effects of Trametes hirsuta laccase and Pentopan Mono BG xylanase and their combination on oat, wheat, and mixed oat-wheat doughs and the corresponding breads were investigated. Laccase treatment decreased the content of water-extractable arabinoxylan (WEAX) in oat dough due to oxidative cross-linking of feruloylated arabinoxylans. Laccase treatment also increased the proportion of water-soluble polysaccharides (WSNSP) apparently due to the beta-glucanase side activity present in the laccase preparation. As a result of the laccase treatment, the firmness of fresh oat bread was increased. Xylanase treatment doubled the content of WEAX in oat dough and slightly increased the amount of WSNSP. Increased stiffness of the dough and firmness of the fresh bread were detected, probably because of the increased WEAX content, which decreased the amount of water available for beta-glucan. The combination of laccase and xylanase produced slight hydrolysis of beta-glucan by the beta-glucanase side activity of laccase and enhanced the availability of AX for xylanase with concomitant reduction of the amount and molar mass of WSNSP. Subsequently, the volume of oat bread was increased. Laccase treatment tightened wheat dough, probably due to cross-linking of WEAX to higher molecular weight. In oat-wheat dough, laccase slightly increased the proportion of WSNSP between medium to low molecular weight and increased the specific volume of the bread. Xylanase increased the contents of WEAX and WSNSP between medium to low molecular weight in oat-wheat dough, which increased the softness of the dough, as well as the specific volume and softness of the bread. The results thus indicate that a combination of laccase and xylanase was beneficial for the textures of both oat and oat-wheat breads.
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PMID:Effects of laccase and xylanase on the chemical and rheological properties of oat and wheat doughs. 1855 94

The exploration of seven physiologically different white rot fungi potential to produce cellulase, xylanase, laccase, and manganese peroxidase (MnP) showed that the enzyme yield and their ratio in enzyme preparations significantly depends on the fungus species, lignocellulosic growth substrate, and cultivation method. The fruit residues were appropriate growth substrates for the production of hydrolytic enzymes and laccase. The highest endoglucanase (111 U ml(-1)) and xylanase (135 U ml(-1)) activities were revealed in submerged fermentation (SF) of banana peels by Pycnoporus coccineus. In the same cultivation conditions Cerrena maxima accumulated the highest level of laccase activity (7,620 U l(-1)). The lignified materials (wheat straw and tree leaves) appeared to be appropriate for the MnP secretion by majority basidiomycetes. With few exceptions, SF favored to hydrolases and laccase production by fungi tested whereas SSF was appropriate for the MnP accumulation. Thus, the Coriolopsis polyzona hydrolases activity increased more than threefold, while laccase yield increased 15-fold when tree leaves were undergone to SF instead SSF. The supplementation of nitrogen to the control medium seemed to have a negative effect on all enzyme production in SSF of wheat straw and tree leaves by Pleurotus ostreatus. In SF peptone and ammonium containing salts significantly increased C. polyzona and Trametes versicolor hydrolases and laccase yields. However, in most cases the supplementation of media with additional nitrogen lowered the fungi specific enzyme activities. Especially strong repression of T. versicolor MnP production was revealed.
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PMID:Effect of growth substrate, method of fermentation, and nitrogen source on lignocellulose-degrading enzymes production by white-rot basidiomycetes. 1871 10

The degradation and utilization of solid waste (SW) from anaerobic digestion of poultry litter by Agrocybe aegerita was evaluated through mushroom production, loss of organic matter (LOM), lignocellulolytic enzymes activity, lignocellulose degradation and mushroom nutrients content. Among the substrate combinations (SCs) tested, substrates composed of 10-20% SW, 70-80% wheat straw and 10% millet was found to produce the highest mushroom yield (770.5 and 642.9 g per 1.5 kg of substrate). LOM in all SCs tested varied between 8.8 and 48.2%. A. aegerita appears to degrade macromolecule components (0.6-21.8% lignin, 33.1-55.2% cellulose and 14-53.9% hemicellulose) during cultivation on the different SCs. Among the seven extracellular enzymes monitored, laccase, peroxidase and CMCase activities were higher before fruiting; while xylanase showed higher activities after fruiting. A source of carbohydrates (e.g., millet) in the substrate is needed in order to obtain yield and biological efficiency comparable to other commercially cultivated exotic mushrooms.
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PMID:Application of solid waste from anaerobic digestion of poultry litter in Agrocybe aegerita cultivation: mushroom production, lignocellulolytic enzymes activity and substrate utilization. 1898 15

Two enzyme treatments involving xylanase (X) and laccase (L) were used jointly in an XLE sequence (where E denotes alkaline extraction) to bleach oxygen-delignified eucalyptus kraft pulp in the presence of 1-hydroxybenzotriazol (HBT) as mediator. The results of the XLE sequence were compared with those of an LE sequence. The application conditions for the laccase-mediator system were optimized by using a sequential statistical plan involving three variables (viz., the laccase and mediator doses, and the reaction time) with both sequences. The models used to predict the kappa number and brightness revealed that, once all accessible lignin was removed, the system altered other coloured compounds. The best conditions for the L stage involved a reduced mediator dose (0.5% odp). The xylanase pretreatment increased the accessibility of residual lignin and facilitated removal of hexenuronic acids. For a specific target brightness level of 70% ISO, the X pretreatment can save as much as 30% laccase and 80% mediator while shortening the reaction time by 45%.
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PMID:Using both xylanase and laccase enzymes for pulp bleaching. 1903 41

The wood-decomposing fungal species Antrodia macra, A. pulvinascens, Ceriporiopsis aneirina, C. resinascens and Dichomitus albidofuscus were determined for production of laccase (LAC), Mn peroxidase (MnP), lignin peroxidase (LiP), endo-l,4-P-beta-glucanase, endo-l,4-beta-xylanase, cellobiohydrolase, 1,4-beta-glucosidase and 1,4-beta-xylosidase. The results confirmed the brown-rot mode of Antrodia spp. which did not produce the activity of LAC and MnP. The remaining species performed detectable activity of both enzymes while no strain produced LiP. Significant inhibition of LAC production by high nitrogen was found in all white-rot species while only MnP of D. albidofuscus was regulated in the same way. The endoglucanase and endoxylanase activities of white-rotting species were inhibited by glucose in the medium while those of Antrodia spp. were not influenced by glucose concentration. The regulation of enzyme activity and bio-mass production can vary even within a single fungal genus.
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PMID:Production and regulation of lignocellulose-degrading enzymes of Poria-like wood-inhabiting basidiomycetes. 1933 May 48

Mixed enzyme preparation having both xylanase and laccase activity was evaluated for its bleach enhancing ability of mixed wood pulp. The enzyme was produced through co-cultivation of mutant Penicillium oxalicum SAU(E)-3.510 and Pleurotus ostreatus MTCC 1804 under solid-state fermentation. Bleaching of pulp with mixed enzyme had resulted into a notable decrease in kappa number and increased brightness as compared to xylanase alone. Analysis of bleaching conditions had denoted that 8 IU g(-1) of mixed enzyme preparation (xylanase/laccase, 22:1) had led into maximal removal of lignin from pulp when bleaching was performed at 10% pulp consistency (55 degrees C, pH 9.0) for 3 h. An overall improvement of 21%, 8%, 3%, and 5% respectively in kappa number, brightness, yellowness, and viscosity of pulp was achieved under derived bleaching conditions. Process of enzymatic bleaching was further ascertained by analyzing the changes occurring in polysaccharide and lignin by HPLC and FTIR. The UV absorption spectrum of the compounds released during enzymatic treatment had denoted a characteristic peak at 280 nm, indicating the presence of lignin in released coloring matter. The changes in fiber morphology following enzymatic delignification were studied by scanning electron microscopy.
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PMID:Bleach enhancement of mixed wood pulp by xylanase-laccase concoction derived through co-culture strategy. 1942 22


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