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Search term: degradation

Results 1 - 100 of 440 > >>
EC Number Recommended Name Application Commentary
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol dehydrogenase degradation direct conversion of switchgrass to ethanol without conventional pretreatment of the biomass is accomplished by deletion of lactate dehydrogenase and heterologous expression of a Clostridium thermocellum bifunctional acetaldehyde/alcohol dehydrogenase in Caldicellulosiruptor bescii. Whereas wild-type Caldicellulosiruptor bescii lacks the ability to make ethanol, 70% of the fermentation products in the engineered strain are ethanol (12.8 mM ethanol directly from 2% wt/vol switchgrass) with decreased production of acetate by 38% compared with wild-type
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol dehydrogenase degradation expression of AdhB gene in an ldh deletion mutant of Caldicellulosiruptor bescii leads to ethanol production at 75°C, near the ethanol boiling point. The AdhB expressing strain produces ethanol (1.4 mM on Avicel, 0.4 mM on switchgrass) as well as acetate (13.0 mM on Avicel, 15.7 mM on switchgrass). The addition of 40 mM MOPS to the growth medium increases the maximal growth yield of C. bescii by approximately twofold
Show all pathways known for 1.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1alcohol dehydrogenase degradation expression of AdhB gene in an ldh deletion mutant of Caldicellulosiruptor bescii leads to ethanol production at 75°C, near the ethanol boiling point. The AdhE expressing strain produce ethanol (2.3 mM on Avicel, 1.6 mM on switchgrass) and acetate (12.3 mM on Avicel, 15.1 mM on switchgrass). The addition of 40 mM MOPS to the growth medium increases the maximal growth yield of C. bescii by approximately twofold
Show all pathways known for 1.1.1.27Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.27L-lactate dehydrogenase degradation direct conversion of switchgrass to ethanol without conventional pretreatment of the biomass is accomplished by deletion of lactate dehydrogenase and heterologous expression of a Clostridium thermocellum bifunctional acetaldehyde/alcohol dehydrogenase. Whereas wild-type Caldicellulosiruptor bescii lacks the ability to make ethanol, 70% of the fermentation products in the engineered strain are ethanol (12.8 mM ethanol directly from 2% wt/vol switchgrass) with decreased production of acetate by 38% compared with wild-type
Show all pathways known for 1.1.1.90Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.90aryl-alcohol dehydrogenase degradation the enzyme is active in toluene degradtion in a reactor, containing the fungus Paecilomyces variotii strain CBS115145, for biofiltration of toluene
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1597alpha-hydroxysteroid dehydrogenase degradation new integrated chemo-enzymatic synthesis of ursodeoxycholic acid starting from sodium cholate by 7alpha- and 12alpha-hydroxysteroid dehydrogenases
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.17612alpha-hydroxysteroid dehydrogenase degradation new integrated chemo-enzymatic synthesis of ursodeoxycholic acid starting from sodium cholate by 7alpha- and 12alpha-hydroxysteroid dehydrogenases
Show all pathways known for 1.1.1.203Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.203uronate dehydrogenase degradation development of a simple and specific assay for D-glucuronate using Udh, stability in solution and high activity of Udh, as well as its relatively easy purification method, provide researchers with an alternative method to study D-glucuronate-related metabolism
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.211long-chain-3-hydroxyacyl-CoA dehydrogenase degradation when gene encoding 3-hydroxyacyl-CoA dehydrogenase is deleted, it is possible to produce medium-chain-length polyhydroxyalkanoates containing only two different monomer structures
Show all pathways known for 1.1.1.284Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.284S-(hydroxymethyl)glutathione dehydrogenase degradation the enzyme is useful in elimination of formaldehyde, a toxic mutagen mediating apoptosis in cells, from consumers goods and environment
Show all pathways known for 1.1.1.284Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.284S-(hydroxymethyl)glutathione dehydrogenase degradation a Saccharomyces cerevisiae mutant lacking the gene for S-hydroxymethylglutathione dehydrogenase and expressing FldA is able to degrade 4 mM formaldehyde within 30 h
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.9galactose oxidase degradation the enzyme can be used for oxygen removal
Show all pathways known for 1.1.3.13Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.13alcohol oxidase degradation the purified enzyme is able to decolorize textile dyes, Red HE7B (57.5%) and Direct Blue GLL (51.09%) within 15 h at 0.04 nm/ml concentration
Show all pathways known for 1.1.99.18Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.18cellobiose dehydrogenase (acceptor) degradation CDH is able to produce a sufficient amount of H2O2 to decolorize anthocyanins within 2 h
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.29pyranose dehydrogenase (acceptor) degradation lignocellulose degradation
Show all pathways known for 1.2.1.5Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.5aldehyde dehydrogenase [NAD(P)+] degradation degradation of polyethylene glycols, PEGs
Show all pathways known for 1.2.1.26Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.262,5-dioxovalerate dehydrogenase degradation involved in an alternative pathway of D-glucarate metabolism
Show all pathways known for 1.2.1.28Display the reaction diagram Show all sequences 1.2.1.28benzaldehyde dehydrogenase (NAD+) degradation in cells of Acinetobacter sp. AG1 isolated from the River Elbe a combined action of benzylalcohol and benzaldehyde dehydrogenase induced after growth with benzylbenzoate does produce benzoate from benzylalcohol, which is a mechanism to quantitatively eliminate the anthropogenic marker compound benzylbenzoate under aerobic conditions
Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.36retinal dehydrogenase degradation ALDH1A1 appears to be the major if not the only enzyme responsible for the oxidation of 3-deoxyglucosone to 2-keto-3-deoxygluconate
Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.36retinal dehydrogenase degradation urinary excretion of 2-keto-3-deoxygluconate amounts to 16.7 micromol/g creatinine in humans, indicating that 3-deoxyglucosone may be quantitatively a more important substrate than retinaldehyde for ALDH1A1
Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.46formaldehyde dehydrogenase degradation physiological significance of dlFalDH in the formaldehyde metabolism in Hyphomicrobium zavarzinii ZV 580 cultured on C1 compounds
Show all pathways known for 1.2.1.72Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.72erythrose-4-phosphate dehydrogenase degradation coupling of a transketolase reaction (using Leishmania mexicana transketolase) that converts D-fructose 6-phosphate to D-erythrose 4-phosphate, which can then be converted to 4-phosphate D-erythronate using E4PD, whereby D-ribose 5-phosphate and D-glyceraldehyde 3-phosphate can both be used as ketol acceptor substrates in the reaction
Display the word mapDisplay the reaction diagram Show all sequences 1.2.3.1aldehyde oxidase degradation aldehyde oxidase plays a critical role in nitrite reduction, and this process is regulated by pH, oxygen tension, nitrite, and reducing substrate concentrations
Display the word mapDisplay the reaction diagram Show all sequences 1.2.3.1aldehyde oxidase degradation the enzyme plays a dual role in the metabolism of physiologically important endogenous compounds and the biotransformation of xenobiotics. Simple qualitative method using density functional theory to predict the product of aldehyde oxidase metabolism by examining the energetics of likely tetrahedral intermediates resulting from nucleophilic attack on carbon
Show all pathways known for 1.2.7.6Display the word mapDisplay the reaction diagram Show all sequences 1.2.7.6glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) degradation Pyrobaculum aerophilum contains a modified Embden-Meyerhof pathway, in which GAPOR replaces the GAPDH/phosphoglycerate kinase couple of the conventional Embden–Meyerhof pathway
Show all pathways known for 1.2.7.6Display the word mapDisplay the reaction diagram Show all sequences 1.2.7.6glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) degradation the major physiological role of GAPOR in Methanococcus maripaludis most likely involves only nonoptimal growth conditions
Display the word mapDisplay the reaction diagram Show all sequences 1.2.98.1formaldehyde dismutase degradation resting Escherichia coli cells transformed with the formaldehyde dismutase gene degrade high concentrations of formaldehyde and produce formic acid and methanol that are molar equivalents of one-half of the degraded formaldehyde. The lyophilized cells of the recombinant Escherichia coli also degrade high concentrations of formaldehyde
Show all pathways known for 1.3.3.6Display the word mapDisplay the reaction diagram Show all sequences 1.3.3.6acyl-CoA oxidase degradation ACO activity in Beauveria bassiana depends on the carbon source used for growth and the chain length of the substrate utilized for the oxidation reaction
Show all pathways known for 1.4.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.2glutamate dehydrogenase degradation at high salinity glutamate seems to be preferentially produced through the process catalyzed by NADH-GDH, whereas GS-catalysis might be the main glutamate synthesis pathway under low salinity
Show all pathways known for 1.4.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.2glutamate dehydrogenase degradation clarification of the in vivo direction of the reaction catalyzed by GDH isoenzyme 1, the enzyme catabolizes L-glutamate in roots, and does not assimilate NH4+ in source leaves
Display the word mapDisplay the reaction diagram Show all sequences 1.5.3.23glyphosate oxidoreductase degradation in Ochrobactrum sp., glyphosate (3 mM) degradation is induced by phosphate starvation, and is completed within 60 h. The bacterium grows even in the presence of glyphosate concentrations as high as 200 mM
Display the word mapDisplay the reaction diagram Show all sequences 1.5.3.23glyphosate oxidoreductase degradation inoculating glyphosate-treated soil samples with Pseudomonas sp. strains GA07, GA09 and GC04 results in a 2-3 times higher rate of glyphosate removal than that in non-inoculated soil. The degradation kinetics follows a first-order model. Glyphosate breakdown in strain GA09 is catalyzed both by C-P lyase and glyphosate oxidoreductase. Strains GA07 and GC04 degrade glyphosate only via glyphosate oxidoreductase, but no further metabolite is detected
Display the word mapDisplay the reaction diagram Show all sequences 1.5.3.23glyphosate oxidoreductase degradation upon cultivation at initial pH 6.0, incubation temperature 35°C, glyphosate concentration 6 g/l, inoculation amount 5% and incubation time 5 days, strain CB4 utilizes 94.47% of glyphosate. The strain degrades glyphosate concentrations up to 12 g/l
Display the word mapDisplay the reaction diagram Show all sequences 1.6.2.4NADPH-hemoprotein reductase degradation coexpression of CPR and P450 cytochromes CYP6AE14 or CYP9A12 of Helicoverpa armigera in Pichia pastoris. CYP6AE14 is not involved in gossipol degradation, but CYP9A12 takes part in gossipol metabolism
Show all pathways known for 1.6.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.6.5.2NAD(P)H dehydrogenase (quinone) degradation TcpB is acting as a quinone reductase for 6-chlorohydroxyquinone reduction during 2,4,6-trichlorophenol degradation, a toxic pollutant
Display the reaction diagram Show all sequences 1.7.1.B4azobenzene reductase [NADH] degradation strain is able to decolorize azo dyes up to 1000 mg /l in 24 h under aerobic conditions. Cell extracts show NADH dependent oxygen-insensitive azoreductase activity
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.6azobenzene reductase degradation potential for the treatment of azo dye contaminated wastewater
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.6azobenzene reductase degradation expression of enzyme gene AzoA in Escherichia coli induces a higher rate of dye reduction with increases of 2fold for methyl red, 4fold for ponceau BS and 2.6fold for orange II compared to noninduced cells, respectively
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.6azobenzene reductase degradation the optimum medium contains dye at 200 mg per l, 1.14 mM NADH, glucose at 2.07 g per l, and peptone at 6.44 g per l for the decolorization of Orange II up to 87% in 48 hr
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.14nitric oxide reductase [NAD(P)+, nitrous oxide-forming] degradation p450nor gene is present in all fungal isolates analyzed that produce N2O from NO2, whereas nirK encoding the NO-forming NO2 reductase, is amplified in only 13 to 74% of the N2O-forming isolates
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.16nitrobenzene nitroreductase degradation the strain can use nitrobenzene as the sole carbon and nitrogen source for growth, and completely degrade 300 mg nitrobenzene per litre within 14 h, at 20-35°C and pH 7.0-9.0. Strain 1 can also degrade aniline and phenol
Show all pathways known for 1.7.2.4Display the word mapDisplay the reaction diagram Show all sequences 1.7.2.4nitrous-oxide reductase degradation plays a critical enviromental role in preventing release into the atmosphere of the potent greenhouse gas nitrous oxide
Show all pathways known for 1.8.1.4Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.4dihydrolipoyl dehydrogenase degradation conservation of the Cys-45 residue in human E3 is essential to the efficient catalytic function of the enzyme
Show all pathways known for 1.8.1.4Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.4dihydrolipoyl dehydrogenase degradation decreased activity of DLDH induced by valproic acid metabolites may, at least in part, account for the impaired rate of oxygen consumption and ATP synthesis in mitochondria if 2-oxoglutarate or glutamate are used as respiratory substrates, thus limiting the flux of these substrates through the citric acid cycle
Show all pathways known for 1.8.1.4Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.4dihydrolipoyl dehydrogenase degradation DLD is required for hamster acrosome reaction
Show all pathways known for 1.8.1.4Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.4dihydrolipoyl dehydrogenase degradation N286 and D320 play a role in the catalytic function of the E3
Show all pathways known for 1.8.1.4Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.4dihydrolipoyl dehydrogenase degradation S456 and E431 form a catalytic dyad in the DLD monomer, whereas H450, by forming a hydrogen bond with E431, may decrease the ability of E431 to polarize the hydroxyl group of S456
Show all pathways known for 1.8.1.4Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.4dihydrolipoyl dehydrogenase degradation shows flavin reductase activity with moderate diaphorase activity
Show all pathways known for 1.8.1.4Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.4dihydrolipoyl dehydrogenase degradation shows NADH-dependent tellurite reductase activity in vitro
Show all pathways known for 1.8.1.4Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.4dihydrolipoyl dehydrogenase degradation shows strong diaphorase activity
Show all pathways known for 1.8.1.4Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.4dihydrolipoyl dehydrogenase degradation T148 is not important to E3 catalytic function, whereas R281 plays a role in the catalytic function of E3
Display the reaction diagram Show all sequences 1.8.1.21dissimilatory dimethyldisulfide reductase degradation application of strain in a two-stage biotrickling filter for simultaneous treatment of hydrogen sulfide, methanethiol, dimethyl sulfide and dimethyl disulfide. The first biofilter is inoculated with Acidithiobacillus thiooxidans and the second one with Thiobacillus thioparus. For separate feeds of reduced sulfur compounds, the elimination capacity order is dimethyl disulfide > dimethyl sulfide > methanethiol
Display the word mapDisplay the reaction diagram Show all sequences 1.10.3.2laccase degradation mineralization of organochlorine from toxic chlorophenols
Display the word mapDisplay the reaction diagram Show all sequences 1.10.3.2laccase degradation enzyme shows dye-decolourizing activity against several anthraquinone dyes, azo dyes, polymeric dyes and others
Display the word mapDisplay the reaction diagram Show all sequences 1.10.3.2laccase degradation use of enzyme in biodegradation of endocrine-disrupting chemicals such as bisphenol A and nonylphenol
Display the word mapDisplay the reaction diagram Show all sequences 1.10.3.2laccase degradation use of enzyme to decolourize textile dye
Display the word mapDisplay the reaction diagram Show all sequences 1.10.3.2laccase degradation cyanobacterial laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. Due to phototrophic mode of nutrition, short generation time and easy mass cultivation, Spirulina platensis laccase appears as good candidate for laccase production. The high yield of laccase in short production period are profitable for its industrial application. Pure Spirulina platensis laccase alone can efficiently decolorized anthraquinonic dye Reactive Blue 4 without any mediators which makes it cost effective and suitable candidate for decolorization of synthetic dyes and help in waste water treatment
Display the word mapDisplay the reaction diagram Show all sequences 1.10.3.2laccase degradation degradation of synthetic dyes from wastewater using biological treatment
Display the word mapDisplay the reaction diagram Show all sequences 1.10.3.2laccase degradation eliminating toxic compounds (biogenic amines) present in fermented food and beverages
Display the word mapDisplay the reaction diagram Show all sequences 1.10.3.2laccase degradation laccase can be efficiently used to decolorize synthetic dye and help in waste water treatmen
Display the word mapDisplay the reaction diagram Show all sequences 1.10.3.2laccase degradation laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment
Display the word mapDisplay the reaction diagram Show all sequences 1.10.3.2laccase degradation laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment, thermostable and acidophilic laccase that can efficiently decolorize several synthetic dyes without addition of an expensive redox mediator
Display the word mapDisplay the reaction diagram Show all sequences 1.10.3.2laccase degradation laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. The enzyme alone can decolourize indigo carmine partially after 60-min incubation at 45 °C. Decolorization is much more efficient in the presence of syringaldehyde. Nearly 90 % decolorization is observed within 20 min
Display the word mapDisplay the reaction diagram Show all sequences 1.10.3.2laccase degradation laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. The enzyme is effective in the decolorization of bromothymol blue, evans blue, methyl orange, and malachite green with decolorizationefficiencies of 50%-85%
Display the word mapDisplay the reaction diagram Show all sequences 1.10.3.2laccase degradation laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. Two anthraquinonic dyes (reactive blue 4 and reactive yellow brown) and two azo dyes (reactive red 11 and reactive brilliant orange) can be partially decolorized by purified laccase in the absence of a mediator. The decolorization process is efficiently promoted when methylsyringate is present, with more than 90 % of color removal occurring in 3 h at pH 7.0 or 9.0
Display the word mapDisplay the reaction diagram Show all sequences 1.10.3.2laccase degradation the enzyme is potentially useful for industrial and environmental applications such as textile finishing and wastewater treatment. It decolorizes structurally different dyes and a real textile effluent
Display the word mapDisplay the reaction diagram Show all sequences 1.10.3.2laccase degradation bisphenol A degradation
Display the word mapDisplay the reaction diagram Show all sequences 1.10.3.2laccase degradation decolorization of industrial dyes. Evans blue decolorization and detoxification
Display the word mapDisplay the reaction diagram Show all sequences 1.10.3.2laccase degradation degradation of endocrine disrupting compounds
Display the word mapDisplay the reaction diagram Show all sequences 1.10.3.2laccase degradation degradation of lignin
Display the word mapDisplay the reaction diagram Show all sequences 1.10.3.2laccase degradation deinking of old newspaper, indigo carmine decolorization
Show all pathways known for 1.11.1.6Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.6catalase degradation application of KatA for elimination of H2O2 after cotton fabrics bleaching leads to less consumption of water, steam and electric power by 25%, 12% and 16.7% respectively without productivity and quality loss of cotton fabrics
Show all pathways known for 1.11.1.7Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.7peroxidase degradation enzyme can decolorize dyes, such as Aniline Blue, Reactive Black 5, and Reactive Blue 19 but not Congo Red
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.10chloride peroxidase degradation rapid and efficient enzymatic decolorization of anthraquinone (alizarin red) and triphenylmethane dyes (crystal violet). The chromophoric groups are destructed and the dye molecules are broken-down into small pieces. The enzyme shows strong toleration to the typical salt species NaCl, NaNO3, and Na2SO4
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.13manganese peroxidase degradation biomimmetic decrosslinking with enzyme or metal complex-catalyzed reactions will enable the development of new devulcanizing strategies for the safe disposal and recycling of waste vulcanized rubber products
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.13manganese peroxidase degradation lingnin-degrading enzymes possess oxidative activity against phenolic compoundss, which can be used for bioremediation, biobleaching, and biofuel production
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.13manganese peroxidase degradation Mn peroxidases are of much interest biotechnologically because of their potentially applications in bioremdeial waste treatment and in catalyzing difficult chemical transfromations
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.13manganese peroxidase degradation various aspects of the biotechnological uses of these fungi have been studied regarding the nonspecific ligninolytic system of white-red fungi such as the degradation of industrial textile dye effluents and various xenobiotics
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.13manganese peroxidase degradation enzyme is able to detoxify aflatoxin B1. Maximum elimination of 86.0% of aflatoxin B1 is observed after 48 h in a reaction mixture containing 5 nkat of enzyme, and the addition of Tween 80 enhances elimination. The treatment of aflatoxin B1 by 20 nkat MnP reduces the mutagenic activity by 69.2%. Analysis suggests that aflatoxin B1 is first oxidized to aflatoxin B1-8,9-epoxide and then hydrolyzed to aflatoxin B1-8,9-dihydrodiol
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.13manganese peroxidase degradation crude enzyme is able to degrade the antibiotics tetracycline and oxytetracycline. 72.5% of 50 mg/l of tetracycline and 84.3% of 50 mg/l oxytetracycline is degraded by 40 U/l of amnganese peroxidase, within 4 h. With the pH at 3.0-4.8, the temperature at 37-40°C, the Mn2+ concentration between 0.1 and 0.4 mM, the H2O2 concentration of 0.2 mM, and the enzyme-substrate ratio above 2.0 U/mg, the degradation rate reaches the highest
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.13manganese peroxidase degradation fibrous bed culture of Bacillus velezensis strain Al-Dhabi 140 might be an efficient strain for tetracycline removal from artificial wastewater, even from natural wastewater
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.14lignin peroxidase degradation degradation of different recalcitrant compounds, removal of toxic dyes
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.14lignin peroxidase degradation the electroenzymatic method using in situ-generated hydrogen peroxide is effective for oxidation of veratryl alcohol by lignin peroxidase. The method may be easily applied to biodegradation systems
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.14lignin peroxidase degradation enzyme shows marked dye-decolorization efficiency and stability toward denaturing, oxidizing, and bleaching agents, and compatibility with EcoVax and Dipex as laundry detergents for 48 h at 40°C
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.14lignin peroxidase degradation LiPH8 showing high acid stability will be a crucial player in biomass valorization using selective depolymerization of lignin
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.14lignin peroxidase degradation the enzyme can be used for PVC films biodegradation. Fungal metabolites are playing an immense role in developing various sustainable waste treatment processes. Production and characterization of a fungal lignin peroxidase with a potential to degrade polyvinyl chloride, method optimization, overview
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.14lignin peroxidase degradation the partially purified LiP is able to degrade toxic synthetic polymer polyvinyl chloride (PVC) films, resulting in a 31% weight reduction of the films. LiP can effectively transform an endocrine disruptive hormone known as 17beta-estradiol (E2), which is considered a pollutant once released into the environment. Veratryl alcohol facilitates the enhanced removal and transformation of E2 by LiP and can perhaps also remove other closely related endocrine-disrupting impurities
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.16versatile peroxidase degradation versatile peroxidase presents particular interest due to its catalytic versatility including the degradation of compounds that other peroxidases are not able to oxidize directly, versatile peroxidase versatility permits its application in Mn3+-mediated or Mn-independent reactions on both low and high redox-potential aromatic substrates and dyes, versatile peroxidase can be used to reoxidize Mn-containing polyoxometalates, which are efficient oxidizers in paper pulp delignification
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.16versatile peroxidase degradation in presence of H2O2 and Mn2+, a cell-free subpernatant is capable to decolorize commercial azo dyes acid black 1 and reactive black 5, reaching efficiencies between 15 and 95%. For all assays performed with 33 microM Mn2+, the initial rate of the decolorization process is dependent on the dosage of H2O2
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.16versatile peroxidase degradation the allosteric behaviour of the VP enzyme promotes a high level of regulation of activity during the breakdown of model and industrial ligninolytic substrates, such as effluent from a pulp and paper plant, and fouled membrane solids extracted from a ground water treatment membrane
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.19dye decolorizing peroxidase degradation DyP is a promising enzyme for the decolorizing treatment of dye-contaminated water
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.19dye decolorizing peroxidase degradation degradation of lignin derivatives
Show all pathways known for 1.13.11.1Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.1catechol 1,2-dioxygenase degradation because of broad spectrum of dioxygenases’ types that Stenotrophomonas maltophilia KB2 can exhibit, this strain appears to be very powerful and useful tool in the biotreatment of wastewaters and in soil decontamination
Show all pathways known for 1.13.11.2Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.2catechol 2,3-dioxygenase degradation because of broad spectrum of dioxygenases’ types that Stenotrophomonas maltophilia KB2 can exhibit, this strain appears to be very powerful and useful tool in the biotreatment of wastewaters and in soil decontamination
Show all pathways known for 1.13.11.2Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.2catechol 2,3-dioxygenase degradation the enzyme can be used for bioremediation of oil-polluted sites
Show all pathways known for 1.13.11.2Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.2catechol 2,3-dioxygenase degradation the enzyme can be used for the biodegradation of crude oil
Show all pathways known for 1.13.11.2Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.2catechol 2,3-dioxygenase degradation comparison of binding sites and affinities using substrates chlorsulfon and metsulfuron-methyl. Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum and Arthrobacter globiformis are more effective in binding than catechol 2,3-dioxygenase from Pseudomonas putida. B. fuscum and A. globiformis have more potential than P. putida to remediate chlorsulfuron and metsulfuronmethyl
Show all pathways known for 1.13.11.2Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.2catechol 2,3-dioxygenase degradation strain is able to degrade a solution containing benzene, toluene, ethylbenzene, and xylene at 7% NaCl (w/v) and pH 9
Show all pathways known for 1.13.11.3Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.3protocatechuate 3,4-dioxygenase degradation because of broad spectrum of dioxygenases’ types that Stenotrophomonas maltophilia KB2 can exhibit, this strain appears to be very powerful and useful tool in the biotreatment of wastewaters and in soil decontamination
Show all pathways known for 1.13.11.15Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.153,4-dihydroxyphenylacetate 2,3-dioxygenase degradation comparison of binding sites and affinities using substrates chlorsulfon and metsulfuron-methyl. Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum and Arthrobacter globiformis are more effective in binding than catechol 2,3-dioxygenase from Pseudomonas putida. B. fuscum and A. globiformis have more potential than P. putida to remediate chlorsulfuron and metsulfuronmethyl
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