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)

In order to enhance the bleaching effect of manganese peroxidase (MnP), unsaturated fatty acids, thiol-containing compounds and various other organic compounds were applied in pulp bleaching experiments with MnP. Thiol-containing compounds did not improve the pulp bleaching effect by MnP. Some unsaturated fatty acids, linoleic acid and linolenic acid provided a better pulp bleaching effect than Tween 80. The correlation between the number of C=C bonds in a fatty acid and its pulp bleaching effect was also investigated. The MnP pulp bleaching capability was shown to depend on the carboxylic acid used. A combination of Tween 80 and a carboxylic acid resulted in higher pulp brightness than that obtained with Tween 80 alone. A laccase mediator, 3-hydroxy-1,2,3-benzotriazin-4(3H)-one, could also enhance the MnP pulp bleaching effect.
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PMID:Studies on mediators of manganese peroxidase for bleaching of wood pulps. 1236 91

Ligninolytic enzymes, manganese peroxidase (MnP), laccase, and lignin peroxidase (LiP), from white-rot fungi were used in an attempt to treat methoxychlor (MC), a chemical widely used as a pesticide. MnP and laccase in the presence of Tween 80 and 1-hydroxybenzotriazole (HBT), respectively, and LiP were found to degrade MC, and MnP-Tween 80 decreased MC levels by about 65% after a 24-h treatment. MC was converted into methoxychlor olefin (MCO) and 4,4'-dimethoxybenzophenone by MnP-Tween 80 or laccase-HBT treatment. These results indicate that ligninolytic enzymes from white-rot fungi can catalyze the oxidative dechlorination of MC. Moreover, a metabolite MCO was also degraded by MnP-Tween 80 or laccase-HBT treatment.
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PMID:Oxidative dechlorination of methoxychlor by ligninolytic enzymes from white-rot fungi. 1500 17

Laccase from Trametes versicolor was immobilized on nanoparticles and kaolinite by physical adsorption or chemical covalence in which the supporters were activated by cross-linked with glutaraldehyde. Thermal and pH stabilities of immobilized laccase on these different supporters were compared. The degradation efficiencies of these immobilized laccases on oxidation of benzo[a]pyrene (BaP) were also compared. The results showed that the immobilized laccases on nanoparticles were more stable in resisting pH and thermal changes. After 48h oxidation, laccase immobilized on kaolinite using the covalent coupling method showed a higher efficiency of oxidation with the BaP residue of 23% in the presence of 1mM HBT and with BaP residue of 37% in 1mM ABTS as the mediator. The results also exhibited a significant inhibition by 1% surfactant Tween 80. According to the HPLC analysis, the oxidation products including 1,6-benzo[a]pyrene quinone, 3,6-benzo[a]pyrene quinone and 6,12-benzo[a]pyrene quinone were identified.
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PMID:Comparative study of immobilized Trametes versicolor laccase on nanoparticles and kaolinite. 1697 19

The regulation of culture conditions, especially the optimization of substrate constituents, is crucial for laccase production by solid fermentation. To develop an inexpensive optimized substrate formulation to produce high-activity laccase, a uniform design formulation experiment was devised. The solid fermentation of Trametes versicolor was performed with natural aeration, natural substrate pH (about 6.5), environmental humidity of 60% and two different temperature stages (at 37 degrees C for 3 days, and then at 30 degrees C for the next 17 days). From the experiment, a regression equation for laccase activity, in the form of a second-degree polynomial model, was constructed using multivariate regression analysis and solved with unconstrained optimization programming. The optimized substrate formulation for laccase production was then calculated. Tween 80 was found to have a negative effect on laccase production in solid fermentation; the optimized solid substrate formulation was 10.8% glucose, 27.7% wheat bran, 9.0% (NH4)2SO4, and 52.5% water. In a scaled-up verification of solid fermentation at a 10 kg scale, laccase activity from T. versicolor in the optimized substrate formulation reached 110.9 IU/g of dry mass.
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PMID:Optimization of laccase production from Trametes versicolor by solid fermentation. 1749 73

The physiological requirements needed to enhance the production of laccases by the ascomycete Botryosphaeria rhodina MAMB-05 in submerged cultivation were examined under non-induced and induced (veratryl alcohol, VA) conditions. Under non-induced conditions (-VA), the initial pH, C:N ratio, and inorganic N source did not influence laccase production, in contrast to Tween 80, soybean oil, and copper, which significantly increased laccase production, and proline and urea, which suppressed laccase formation. In addition, Tween 60 could serve as the sole carbon source for the production of these enzymes. Under VA-induced conditions of fungal growth, factors such as inoculum type, time-point of addition of inducer, initial pH, C:N ratio, and type of N source, influenced the production of laccases; however, unlike the non-induced conditions, proline and urea did not act as suppressors. Each of these physiological conditions exerted different effects on biomass production. The nutritional conditions examined for B. rhodina MAMB-05 are discussed in relation to their influence on fungal growth and laccase production.
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PMID:Influence of nutrients on enhancing laccase production by Botryosphaeria rhodina MAMB-05. 1807 99

Some conditions in media composition for laccases production, such as different sources of carbon and organic nitrogen, antifoams and a surfactant, were studied in liquid cultures of Pleurotus sajor-caju strain PS-2001. Cultivation with fructose or glucose as carbon sources produced maximum enzyme activities of 37 and 36 U mL(-1), respectively. When sucrose was present in the medium, the best results were obtained using 5 g L(-1) of this carbohydrate, on the 11th day of the process, attaining laccase titres of 13 U mL(-1). In a medium without casein, practically no enzyme was produced during the experiments; among the sources of nitrogen studied, pure casein led to the highest titres of laccase activity. Different concentrations of pure casein and sucrose were also tested. As to the different concentrations of casein, the addition of 1.5 g L(-1) resulted in the highest titres of laccase activity. Negligible levels of manganese peroxidase activity were also detected in the culture medium. In low concentrations, polypropylene glycol or silicon-based antifoams and the surfactant Tween 80 have no significant influence on the formation of laccases by P. sajor-caju. However, enhanced concentration of polypropylene glycol negatively affected the production of laccases but favored the titres in total peroxidases, lignin peroxidase and veratryl alcohol oxidase.
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PMID:Production of laccases in submerged process by Pleurotus sajor-caju PS-2001 in relation to carbon and organic nitrogen sources, antifoams and Tween 80. 1875 36

The capabilities of p-coumaric acid (PCA), ferulic acid (FA), and sinapic acid (SA) as laccase mediators are compared in oxidation of industrial dyes and polycyclic aromatic hydrocarbons (PAH). SA behaved as highly efficient mediator in decolorization of dyes, including the recalcitrant Reactive Black 5. This mediating capacity was related to the specificity constant of the enzyme oxidizing this p-hydroxycinnamic acid, which was 16 times higher than for the typical substrate 2,2'-azinobis-(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS). The kinetics of ABTS oxidation by laccase in the presence of p-hydroxycinnamic acids suggested that the stable phenoxyl radical of a SA transformation product acts as laccase mediator. On the other hand, FA and, especially PCA, easily mediated benzo[a]pyrene oxidation, the latter also promoting the oxidation of the more recalcitrant phenanthrene. Phenanthrene transformation by laccase-PCA was enhanced by Tween 80. This fact, together with the detection of TBARS (thiobarbituric acid-reactive-substances) from unsaturated fatty acids, revealed that laccase can also initiate lipid peroxidation reactions in the presence of p-hydroxycinnamic acids enabling oxidation of the most recalcitrant PAH.
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PMID:P-hydroxycinnamic acids as natural mediators for laccase oxidation of recalcitrant compounds. 1880 May 52

The ability of pure manganese peroxidase (MnP), laccase, lignin peroxidase (LiP) and horseradish peroxidase (HRP) to degrade the widely used herbicide glyphosate and other pesticides was studied in separate in vitro assays with addition of different mediators. Complete degradation of glyphosate was obtained with MnP, MnSO4 and Tween 80, with or without H2O2. In the presence of MnSO4, with or without H(2)O(2), MnP also transformed the herbicide, but to a lower rate. Laccase degraded glyphosate in the presence of (a) 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) (ABTS), (b) MnSO(4) and Tween 80 and (c) ABTS, MnSO4 and Tween 80. The metabolite AMPA was detected in all cases where degradation of glyphosate occurred and was not degraded. The LiP was tested alone or with MnSO4, Tween 80, veratryl alcohol or H2O2 and in the HRP assay the enzyme was added alone or with H2O2 in the reaction mixture. However, these enzymes did not degrade glyphosate. Further experiments using MnP together with MnSO4 and Tween 80 showed that the enzyme was also able to degrade glyphosate in its commercial formulation Roundup Bio. The same enzyme mixture was tested for degradation of 22 other pesticides and degradation products present in a mixture and all the compounds were transformed, with degradation percentages ranging between 20 and 100%. Our results highlight the potential of ligninolytic enzymes to degrade pesticides. Moreover, they suggest that the formation of AMPA, the main metabolite of glyphosate degradation found in soils, can be a result of the activity of lignin-degrading enzymes.
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PMID:Degradation of glyphosate and other pesticides by ligninolytic enzymes. 1939 51

The effects of various synthetic medium components and their interactions with each other ultimately impact laccase production in fungi. This was studied using a laccase-hyper-producing marine-derived basidiomycete, Cerrena unicolor MTCC 5159. Inducible laccases were produced in the idiophase only after addition of an inducer such as CuSO(4). Concentration of carbon and nitrogen acted antagonistically with respect to laccase production. A combination of low nitrogen and high carbon concentration favored both biomass and laccase production. The most favorable combination resulted in 917 U L(-1) of laccase. After sufficient growth had occurred, addition of a surfactant such as Tween 80 positively impacted biomass and increased the laccase activity to around 1,300 U L(-1). Increasing the surface to volume ratio of the culture vessel further increased its activity to almost 2,000 U L(-1).
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PMID:Effects and interactions of medium components on laccase from a marine-derived fungus using response surface methodology. 2009 6

Polyporus sp. S133, a fungus collected from contaminated soil, was used to degrade phenanthrene, a polycyclic aromatic hydrocarbon, in a mineral salt broth liquid culture. A maximal degradation rate (92%) was obtained when Polyporus sp. S133 was cultured for 30 days with agitation at 120 r/min, as compared to 44% degradation in non-agitated cultures. Furthermore, the degradation was affected by the addition of surfactants. Tween 80 was the most suitable surfactant for the degradation of phenanthrene by Polyporus sp. S133. The degradation rate increased as the amount of Tween 80 added increased. The rate in agitated cultures was about 2 times that in non-agitated cultures. The mechanism of degradation was determined through the identification of metabolites; 9,10-phenanthrenequinone, 2,2'-diphenic acid, phthalic acid, and protocatechuic acid. Several enzymes (manganese peroxidase, lignin peroxidase, laccase, 1,2-dioxygenase and 2,3-dioxygenase) produced by Polyporus sp. S133 were detected during the incubation. The highest level of activity was shown by 1,2-dioxygenase (187.4 U/L) after 20 days of culture.
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PMID:Characterization of phenanthrene degradation by strain polyporus sp. S133. 2039 98


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