EC Number   |
Recommended Name |
Application |
|---|
    1.1.1.1 | alcohol 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 |
| 1.1.1.1 | alcohol 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 |
| 1.1.1.1 | alcohol 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 |
| 1.1.1.27 | L-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 |
| 1.1.1.90 | aryl-alcohol dehydrogenase |
degradation |
the enzyme is active in toluene degradtion in a reactor, containing the fungus Paecilomyces variotii strain CBS115145, for biofiltration of toluene |
| 1.1.1.159 | 7alpha-hydroxysteroid dehydrogenase |
degradation |
new integrated chemo-enzymatic synthesis of ursodeoxycholic acid starting from sodium cholate by 7alpha- and 12alpha-hydroxysteroid dehydrogenases |
| 1.1.1.176 | 12alpha-hydroxysteroid dehydrogenase |
degradation |
new integrated chemo-enzymatic synthesis of ursodeoxycholic acid starting from sodium cholate by 7alpha- and 12alpha-hydroxysteroid dehydrogenases |
| 1.1.1.203 | uronate 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 |
| 1.1.1.211 | long-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 |
| 1.1.1.284 | S-(hydroxymethyl)glutathione dehydrogenase |
degradation |
the enzyme is useful in elimination of formaldehyde, a toxic mutagen mediating apoptosis in cells, from consumers goods and environment |
| 1.1.1.284 | S-(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 |
| 1.1.3.9 | galactose oxidase |
degradation |
the enzyme can be used for oxygen removal |
| 1.1.3.13 | alcohol 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 |
| 1.1.99.18 | cellobiose dehydrogenase (acceptor) |
degradation |
CDH is able to produce a sufficient amount of H2O2 to decolorize anthocyanins within 2 h |
| 1.1.99.29 | pyranose dehydrogenase (acceptor) |
degradation |
lignocellulose degradation |
| 1.2.1.5 | aldehyde dehydrogenase [NAD(P)+] |
degradation |
degradation of polyethylene glycols, PEGs |
| 1.2.1.26 | 2,5-dioxovalerate dehydrogenase |
degradation |
involved in an alternative pathway of D-glucarate metabolism |
| 1.2.1.28 | benzaldehyde 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 |
| 1.2.1.36 | retinal 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 |
| 1.2.1.36 | retinal 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 |
| 1.2.1.46 | formaldehyde dehydrogenase |
degradation |
physiological significance of dlFalDH in the formaldehyde metabolism in Hyphomicrobium zavarzinii ZV 580 cultured on C1 compounds |
| 1.2.1.72 | erythrose-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 |
| 1.2.3.1 | aldehyde 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 |
| 1.2.3.1 | aldehyde 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 |
| 1.2.7.6 | glyceraldehyde-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 EmbdenMeyerhof pathway |
| 1.2.7.6 | glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) |
degradation |
the major physiological role of GAPOR in Methanococcus maripaludis most likely involves only nonoptimal growth conditions |
| 1.2.98.1 | formaldehyde 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 |
| 1.3.3.6 | acyl-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 |
| 1.4.1.2 | glutamate 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 |
| 1.4.1.2 | glutamate 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 |
| 1.5.3.23 | glyphosate 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 |
| 1.5.3.23 | glyphosate 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 |
| 1.5.3.23 | glyphosate 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 |
| 1.6.2.4 | NADPH-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 |
| 1.6.5.2 | NAD(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 |
| 1.7.1.B4 | azobenzene 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 |
| 1.7.1.6 | azobenzene reductase |
degradation |
potential for the treatment of azo dye contaminated wastewater |
| 1.7.1.6 | azobenzene 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 |
| 1.7.1.6 | azobenzene 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 |
| 1.7.1.14 | nitric 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 |
| 1.7.1.16 | nitrobenzene 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 |
| 1.7.2.4 | nitrous-oxide reductase |
degradation |
plays a critical enviromental role in preventing release into the atmosphere of the potent greenhouse gas nitrous oxide |
| 1.8.1.4 | dihydrolipoyl dehydrogenase |
degradation |
conservation of the Cys-45 residue in human E3 is essential to the efficient catalytic function of the enzyme |
| 1.8.1.4 | dihydrolipoyl 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 |
| 1.8.1.4 | dihydrolipoyl dehydrogenase |
degradation |
DLD is required for hamster acrosome reaction |
| 1.8.1.4 | dihydrolipoyl dehydrogenase |
degradation |
N286 and D320 play a role in the catalytic function of the E3 |
| 1.8.1.4 | dihydrolipoyl 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 |
| 1.8.1.4 | dihydrolipoyl dehydrogenase |
degradation |
shows flavin reductase activity with moderate diaphorase activity |
| 1.8.1.4 | dihydrolipoyl dehydrogenase |
degradation |
shows NADH-dependent tellurite reductase activity in vitro |
| 1.8.1.4 | dihydrolipoyl dehydrogenase |
degradation |
shows strong diaphorase activity |
| 1.8.1.4 | dihydrolipoyl dehydrogenase |
degradation |
T148 is not important to E3 catalytic function, whereas R281 plays a role in the catalytic function of E3 |
| 1.8.1.21 | dissimilatory 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 |
| 1.10.3.2 | laccase |
degradation |
mineralization of organochlorine from toxic chlorophenols |
| 1.10.3.2 | laccase |
degradation |
enzyme shows dye-decolourizing activity against several anthraquinone dyes, azo dyes, polymeric dyes and others |
| 1.10.3.2 | laccase |
degradation |
use of enzyme in biodegradation of endocrine-disrupting chemicals such as bisphenol A and nonylphenol |
| 1.10.3.2 | laccase |
degradation |
use of enzyme to decolourize textile dye |
| 1.10.3.2 | laccase |
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 |
| 1.10.3.2 | laccase |
degradation |
degradation of synthetic dyes from wastewater using biological treatment |
| 1.10.3.2 | laccase |
degradation |
eliminating toxic compounds (biogenic amines) present in fermented food and beverages |
| 1.10.3.2 | laccase |
degradation |
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatmen |
| 1.10.3.2 | laccase |
degradation |
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment |
| 1.10.3.2 | laccase |
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 |
| 1.10.3.2 | laccase |
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 |
| 1.10.3.2 | laccase |
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% |
| 1.10.3.2 | laccase |
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 |
| 1.10.3.2 | laccase |
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 |
| 1.10.3.2 | laccase |
degradation |
bisphenol A degradation |
| 1.10.3.2 | laccase |
degradation |
decolorization of industrial dyes. Evans blue decolorization and detoxification |
| 1.10.3.2 | laccase |
degradation |
degradation of endocrine disrupting compounds |
| 1.10.3.2 | laccase |
degradation |
degradation of lignin |
| 1.10.3.2 | laccase |
degradation |
deinking of old newspaper, indigo carmine decolorization |
| 1.11.1.6 | catalase |
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 |
| 1.11.1.7 | peroxidase |
degradation |
enzyme can decolorize dyes, such as Aniline Blue, Reactive Black 5, and Reactive Blue 19 but not Congo Red |
| 1.11.1.10 | chloride 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 |
| 1.11.1.13 | manganese 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 |
| 1.11.1.13 | manganese peroxidase |
degradation |
lingnin-degrading enzymes possess oxidative activity against phenolic compoundss, which can be used for bioremediation, biobleaching, and biofuel production |
| 1.11.1.13 | manganese peroxidase |
degradation |
Mn peroxidases are of much interest biotechnologically because of their potentially applications in bioremdeial waste treatment and in catalyzing difficult chemical transfromations |
| 1.11.1.13 | manganese 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 |
| 1.11.1.13 | manganese 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 |
| 1.11.1.13 | manganese 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 |
| 1.11.1.13 | manganese 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 |
| 1.11.1.14 | lignin peroxidase |
degradation |
degradation of different recalcitrant compounds, removal of toxic dyes |
| 1.11.1.14 | lignin 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 |
| 1.11.1.14 | lignin 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 |
| 1.11.1.14 | lignin peroxidase |
degradation |
LiPH8 showing high acid stability will be a crucial player in biomass valorization using selective depolymerization of lignin |
| 1.11.1.14 | lignin 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 |
| 1.11.1.14 | lignin 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 |
| 1.11.1.16 | versatile 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 |
| 1.11.1.16 | versatile 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 |
| 1.11.1.16 | versatile 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 |
| 1.11.1.19 | dye decolorizing peroxidase |
degradation |
DyP is a promising enzyme for the decolorizing treatment of dye-contaminated water |
| 1.11.1.19 | dye decolorizing peroxidase |
degradation |
degradation of lignin derivatives |
| 1.13.11.1 | catechol 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 |
| 1.13.11.2 | catechol 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 |
| 1.13.11.2 | catechol 2,3-dioxygenase |
degradation |
the enzyme can be used for bioremediation of oil-polluted sites |
| 1.13.11.2 | catechol 2,3-dioxygenase |
degradation |
the enzyme can be used for the biodegradation of crude oil |
| 1.13.11.2 | catechol 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 |
| 1.13.11.2 | catechol 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 |
| 1.13.11.3 | protocatechuate 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 |
| 1.13.11.15 | 3,4-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 |
