EC Number   |
Recommended Name |
Application  |
|---|
   1.1.1.50 | 3alpha-hydroxysteroid 3-dehydrogenase (Si-specific) |
environmental protection |
the mutant Comamonas testosteroni strain CT-GFP5-1 can be used as a sensitive biosensor system for steroid determination in the environment |
 1.1.1.51 | 3(or 17)beta-hydroxysteroid dehydrogenase |
environmental protection |
transcriptional repressor phaR knockout mutants have better ability to degrade steroids than wild-type Comamonas testosteroni ATCC11996 and might therefore be used in bioremediation |
| 1.1.1.149 | 20alpha-hydroxysteroid dehydrogenase |
environmental protection |
diesel exhaust components are inhibitory on 20alpha-hydroxysteroid dehydrogenase in liver and lung cytosol, with little inhibition in kidney cytosol |
| 1.1.1.284 | S-(hydroxymethyl)glutathione dehydrogenase |
environmental protection |
the enzyme is useful in elimination of formaldehyde, a toxic mutagen mediating apoptosis in cells, from consumers goods and environment |
| 1.1.2.3 | L-lactate dehydrogenase (cytochrome) |
environmental protection |
the reductive pathway of the enzyme resulting in formation of less toxic Cr(III)-species is suggested to be the most important among possible mechanisms for chromate biodetoxification |
| 1.1.2.8 | alcohol dehydrogenase (cytochrome c) |
environmental protection |
potential application of Pseudomonas sp. strain J51 in the treatment of DES-contaminated freshwater and seawater environments |
| 1.1.3.7 | aryl-alcohol oxidase |
environmental protection |
the enzyme in white-rot fungi is useful in degradation of aromatic hydrocarbons in a historically contaminated soil |
| 1.2.1.65 | salicylaldehyde dehydrogenase |
environmental protection |
the ability to degrade acenaphthylene and other aromatic compounds makes this strain ideal candidate for application in remediation at the contaminated sites |
| 1.3.1.32 | maleylacetate reductase |
environmental protection |
further evolution to more catalytically active PcpE may be an important contributor to improved Sphingobium chlorophenolicum L-1-mediated bioremediation of pentachlorophenol |
| 1.3.1.42 | 12-oxophytodienoate reductase |
environmental protection |
2,4,6-trinitrotoluene detoxofication, use of plants to remove environmental pollutants |
| 1.3.3.5 | bilirubin oxidase |
environmental protection |
BOX can be used to decolorize synthetic dyes from effluents, especially for anthraquinonic dyes |
| 1.3.3.5 | bilirubin oxidase |
environmental protection |
the BOD from Magnaporthe oryzae is efficient in decolorizing textile dyes such as Remazol brilliant Blue R, making it useful for environmentally friendly industrial applications |
| 1.4.3.12 | cyclohexylamine oxidase |
environmental protection |
as a potential biocatalyst, the enzyme is promising in controlling cyclohexylamine pollution and deracemization of chiral amines |
| 1.5.1.37 | FAD reductase (NADH) |
environmental protection |
strain X1 Fre can effectively dehalogenate dihalophenols, which can be useful for the treatment of dihalophenols in wastewaters and remediation of DCP-contaminated environments |
| 1.6.5.5 | NADPH:quinone reductase |
environmental protection |
NfsA has potential applications in the biodegradation of nitroaromatic environment pollutants, e.g. explosives |
| 1.6.5.6 | p-benzoquinone reductase (NADPH) |
environmental protection |
the strain WBC3, also possessing 4-nitrophenyl 4-monooxygenase activity through PnpA, has a potential in bioremediation of the environment polluted by both 4-nitrocatechol and 4-nitrophenol |
| 1.7.1.2 | Nitrate reductase [NAD(P)H] |
environmental protection |
hexahydro-1,3,5-trinitro-1,3,5-triazine is widely used for military and commercial purposes due to its high explosive properties. Hexahydro-1,3,5-trinitro-1,3,5-triazine and its degradation products are toxic, mutagenic and carcinogenic to humans and other biological systems. The biotransformation of hexahydro-1,3,5-trinitro-1,3,5-triazine by NAD(P)H nitrate reductase from Aspergillus niger under anaerobic conditions |
| 1.7.1.B3 | aromatic nitroreductase [NADPH] |
environmental protection |
NfsA has potential applications in the biodegradation of nitroaromatic environment pollutants, e.g. explosives |
| 1.7.1.6 | azobenzene reductase |
environmental protection |
potential for the treatment of azo dye contaminated wastewater |
| 1.7.1.6 | azobenzene reductase |
environmental protection |
generation of a coupled enzyme system constructed with azoreductase and glucose 1-dehydrogenase for removal of methyl red, evaluation, overview |
| 1.7.1.6 | azobenzene reductase |
environmental protection |
Geobacter sulfurreducens useful for the decontamination of environments polluted with azo dyes. The contribution of extracellular respiration to pollutants reduction will broaden the environmental applications |
| 1.7.1.6 | azobenzene reductase |
environmental protection |
utilization of azo-dye degrading organisms is essential for developing bioremediation strategies in waste-water treatment plants |
| 1.7.1.6 | azobenzene reductase |
environmental protection |
anthropogenic activity has converted chromium (Cr), an element found in rocks, soils, plants, and animals, into a dangerous environmental pollutant. The activity of the pure oxidoreductase YhdA can be used for efficient bioremediation of Cr(VI) |
| 1.7.2.5 | nitric oxide reductase (cytochrome c) |
environmental protection |
mantains global environmental homeostasis |
| 1.7.2.5 | nitric oxide reductase (cytochrome c) |
environmental protection |
removes cytotoxic nitrous oxide |
| 1.7.2.8 | hydrazine dehydrogenase |
environmental protection |
the application of anammox to nitrogen removal would lead to a reduction of operational costs of up to 90%. The process targets wastewaters that contain much ammonium and little organic material, such as sludge digestor effluents. Anammox would replace the conventional denitrification step completely and would also save half of the nitrification aeration costs |
| 1.8.4.9 | adenylyl-sulfate reductase (glutathione) |
environmental protection |
APR2 can be exploited for engineering heavy metal-tolerant plants in phytoremediation |
| 1.8.5.4 | bacterial sulfide:quinone reductase |
environmental protection |
anaerobic treatment of sulphate rich wastewater results in high amount of sulfide in liquid phase and gaseous phase. Sulfide is malodorous in gaseous phase and toxic even at very low concentrations in liquid phase and causes objectionable environmental issues. Sulfide present in the up-flow anaerobic sludge blanket (UASB)-treated post tanning wastewater is oxidized into elemental sulfur using sulfide:quinone oxidoreductase (SQR) immobilized on functionalized carbon-silica matrix (FCSM) in a packed bed reactor. Optimum conditions for immobilization of SQR onto FCSM are pH, 7.0, 40°C, and 10mg/g SQR during 240 min. The immobilization of SQR onto FCSM obeys the Langmuir isotherm model. The maximum sulfide oxidation is 99% at HRT of 15 h with residual sulfide of 2.4 mg/l. The formation of elemental Sulphur is confirmed by XRD studies |
| 1.8.5.5 | thiosulfate reductase (quinone) |
environmental protection |
Escherichia coli expressing thiosulfate reductase genes (phsABC) from Salmonella typhimurium is able to remove significant amounts of heavy metals from the medium within 24 h: 99% of zinc up to 500 microM, 99% of lead up to 200 microM, 99% of 100 icroM and 91% of 200 icroM cadmium. In a mixture of 100 microM each of cadmium, lead, and zinc, the strain removes 99% of the total metals from solution within 10 h. Cadmium is removed first, lead second, and zinc last |
| 1.8.5.5 | thiosulfate reductase (quinone) |
environmental protection |
Escherichia coli strains harboring thiosulfate reductase gene phsABC expression constructs show higher thiosulfate reductase activity and produce significantly more sulfide than the control strains under both aerobic and anaerobic conditions. The most effecitve expression construct produces thiosulfate reductase at the highest level and removes the most cadmium from solution under anaerobic conditions: 98% of all concentrations up to 150 microM and 91% of 200 microM. The metal removed from solution precipitates as a complex of cadmium and sulfur, most likely cadmium sulfide |
| 1.8.99.2 | adenylyl-sulfate reductase |
environmental protection |
the gene apsA is used for quantitative determination of the organism in wastewater, overview |
| 1.10.3.2 | laccase |
environmental protection |
fast biodegradation of 2,4-dichlorophenol, a potent xenobiotic compound |
| 1.10.3.2 | laccase |
environmental protection |
laccase is capable of efficiently removing 2,4-dimethylphenol from water at very low enzyme concentrations and hence shows great potential for cost-effective industrial applications |
| 1.10.3.2 | laccase |
environmental protection |
LI1 shows activity over a broad range of pH and temperature, which may make it useful in the biodegradation of phenolic compounds present in wastewater from several industrial processes |
| 1.10.3.2 | laccase |
environmental protection |
the stability of this laccase against metal ions makes the enzyme an efficient agent in the treatment of wastewater containing heavy metals |
| 1.10.3.2 | laccase |
environmental protection |
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 |
environmental protection |
degradation of synthetic dyes from wastewater using biological treatment |
| 1.10.3.2 | laccase |
environmental protection |
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment |
| 1.10.3.2 | laccase |
environmental protection |
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 |
environmental protection |
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. The enzyme alone can decolorize 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 |
environmental protection |
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. The enzyme can also be considered as a candidate for treating industrial effluent containing malachite green |
| 1.10.3.2 | laccase |
environmental protection |
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 |
environmental protection |
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 |
environmental protection |
laccase can be efficiently used to decolorize synthetic dye and is a suitable candidate for the treatment of wastewater from industrial effluents |
| 1.10.3.2 | laccase |
environmental protection |
laccase can be efficiently used to decolorize synthetic dye and is a suitable candidate for the treatment of wastewater from industrial effluents. The wide pH- and thermostability attributes of immobilized laccase make them suitable for environmental applications |
| 1.10.3.2 | laccase |
environmental protection |
sensitive, rapid, and precise determination of phenols and their derivatives is important in environmental control and protection. An amperometric principle-based biosensor, employing immobilized laccase enzyme from Trametes versicolor, is developed for the detection of disubstituted methyl and methoxy phenols (industrial effluents). Evaluation of the influence of different enzyme immobilization techniques, on nylon membrane, on the performances of laccase-based Clark-type electrodes. The analytical properties and operating stabilities of the resulting biosensors are tested with different disubstituted methyl and methoxy derivatives of phenol substrates. Co-cross-linking method is superior to the other methods of immobilization in terms of sensitivity, limit of detection, response time, and operating stability. In co-cross-linking method of immobilization, laccase is mixed with bovine serum albumin as protein-based stabilizing agent and glutaraldehyde as crosslinking agent |
| 1.10.3.2 | laccase |
environmental protection |
the enzyme has potential for application in the treatment of contaminated water with low pH values and high phenolic content |
| 1.10.3.2 | laccase |
environmental protection |
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 |
environmental protection |
decolorization of industrial dyes with different chemical structures and decolorization of industrial wastewaters |
| 1.10.3.2 | laccase |
environmental protection |
decolorization of industrial dyes. Evans blue decolorization and detoxification |
| 1.10.3.2 | laccase |
environmental protection |
deinking of old newspaper, indigo carmine decolorization |
| 1.10.3.2 | laccase |
environmental protection |
good application prospect in wastewater treatment and dye degradation. error-prone PCR is a feasible method to improve the degradation activity of laccase for environmental pollutants, which provide a basis for the application of laccase on dye degradation and other environmental pollutants |
| 1.10.3.2 | laccase |
environmental protection |
laccases are very important in removing environmental pollutants, detoxification from wastewater |
| 1.10.3.2 | laccase |
environmental protection |
laccases are very important in removing environmental pollutants. Detoxification from wastewater |
| 1.10.3.2 | laccase |
environmental protection |
potential for industrial wastewater treatments |
| 1.10.3.2 | laccase |
environmental protection |
the enzyme is able to decolorize efficiently a variety of chemical dyes, thus, being potentially applicable in textile and environmental industries |
| 1.10.3.2 | laccase |
environmental protection |
the enzyme is an ideal candidate for lots of biotechnological and industrial applications due to its stability in the extreme conditions |
| 1.10.3.2 | laccase |
environmental protection |
the immobilized laccase transforms diclofenac to 4-OH diclofenac. The immobilized laccase can be used to transform or degrade several recalcitrant compounds from industrial effluents |
| 1.10.3.2 | laccase |
environmental protection |
the surface display laccase (SDL) biocatalyst, where the enzyme laccase is displayed on the surface of biological cells through synthetic biology, provides a biocatalytic material for removal of emerging contaminants from wastewater |
| 1.10.3.2 | laccase |
environmental protection |
treating waste water containing synthetic dyes |
| 1.11.1.7 | peroxidase |
environmental protection |
biodegradation of toxic and carcinogenic phenolic contaminants and related compounds in industrial effluents. Calotropis procera is a drought-resistant local plant that grows wild in the natural habitat of Nigerian throughout the year. Calotropis procera root could be an environmentally sustainable source of peroxidase for a low technological solution for phenol remediation |
| 1.11.1.7 | peroxidase |
environmental protection |
the removal of textile dyes from wastewater by using plant peroxidases offers environmentally effective solutions |
| 1.11.1.10 | chloride peroxidase |
environmental protection |
chloroperoxidase shows oxidative dehalogenation activity and is significantly more robust than other peroxidases and functions under harsher reaction conditions compared to other biocatalysts. Expanding the scope of reactivity achieved by the enzyme may be beneficial for industrial and biotechnological functions in the future. This considerable extension of already known activities could lead to the use of the enzyme as a biocatalyst in the field of bioremediation and a broader understanding of both how peroxidases and cytochrome P450s react with halogenated organic substrates |
| 1.11.1.10 | chloride peroxidase |
environmental protection |
this enzyme may by employed to treat contaminated soil or water prior to discharge |
| 1.11.1.10 | chloride peroxidase |
environmental protection |
amino modified magnetic halloysite nanotube supporting chloroperoxidase immobilization is useful for enhanced stability, reusability, and efficient degradation of pesticide residue in wastewater. Degradation of mesotrione in wastewater by the immobilized CPO |
| 1.11.1.10 | chloride peroxidase |
environmental protection |
CPO carries out a wide variety of oxidative reactions, changing the environmental impacts of organic matters |
| 1.11.1.13 | manganese peroxidase |
environmental protection |
- |
| 1.11.1.13 | manganese peroxidase |
environmental protection |
thiol-mediated degradation of dimeric model compounds and of polymeric lignin by MnP has potential applications in the degradation of industrial lignins |
| 1.11.1.13 | manganese peroxidase |
environmental protection |
key enzyme for degradation of environmentally persistent xenobiotics such as pentachlorophenol and dioxins |
| 1.11.1.13 | manganese peroxidase |
environmental protection |
degradation of recalcitrant high-molecular-mass compounds, such as nylon and melanin, degradation of xenobiotic compounds, bioremediation, decolorization of wastewater |
| 1.11.1.13 | manganese peroxidase |
environmental protection |
polycyclic aromatic hydrocarbon degradation |
| 1.11.1.13 | manganese peroxidase |
environmental protection |
mediated system of degradation is potentially valuable for degradation of synthetic polymers and of environmental pollutants |
| 1.11.1.13 | manganese peroxidase |
environmental protection |
degradation of recalcitrant pollutants |
| 1.11.1.13 | manganese peroxidase |
environmental protection |
as to denim bleaching, sodium hypochlorite treatment is primarily used and this gives rise to problems such as chemical injuries, denim yellowness and reduced denim strength. To ensure the low-cost and ecofriendly advantages, denim biobleaching using oxidizing enzymes such as manganese peroxidases (MnPs) and laccases is an ideal alternative. In the presence of MnPs, denim bleaching by laccases is greatly enhanced. Usage of recombinant white-rot fungi MnP in denim bleaching and PAH degradation |
| 1.11.1.13 | manganese peroxidase |
environmental protection |
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 |
| 1.11.1.13 | manganese peroxidase |
environmental protection |
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes |
| 1.11.1.13 | manganese peroxidase |
environmental protection |
the enzyme can degrade sulfamethoxazole (SMX), a broad-spectrum antibiotic (one non-phenolic compound) that has been widely used as a growth promoter in the breeding industry. SMX has been widely detected in effluents, soils, and surface waters in China. SMX is a persistent and polar organic compound in effluent with a half-life time of 17.8 days. More seriously, the SMX in aquatic environments may accelerate the spread of sul genes (antibiotic resistance genes (ARGs)) in microbial populations, and this would have detrimental effects on the ecosystem balance |
| 1.11.1.14 | lignin peroxidase |
environmental protection |
use of Phanerochaete chrysosporium and its enzyme lignin peroxidase in the degradation of environmental pollutants such as dye. High efficient degradation of dyes with lignin peroxidase coupled with glucose oxidase |
| 1.11.1.14 | lignin peroxidase |
environmental protection |
decolorization of textile dyes |
| 1.11.1.14 | lignin peroxidase |
environmental protection |
the enzyme shows the potential to be applied in the treatment of textile effluents (decolorization of dyes). The results from the selection of dyes such as methylene blue, malachite green and methyl orange show that the enzyme is able to remove a higher content of methylene blue (14%) compared to the other two dyes (3-8%). The optimization with the OFAT method determined the operating conditions of the decolorization of methylene blue dye at temperature 55°C, pH 5.0 (in 50 mM sodium acetate buffer) with H2O2 concentration 4.0 mM. The addition of veratryl alcohol to the reaction mixture has no affect on decolorization of dye |
| 1.11.1.14 | lignin peroxidase |
environmental protection |
a high and sustainable lignin peroxidase activity is achieved via in situ release of H2O2 by a co-immobilized glucose oxidase. The present co-immobilization system is demonstrated to be very effective for lignin peroxidase mediated dye decolourization |
| 1.11.1.14 | lignin peroxidase |
environmental protection |
lignin peroxidase enzyme production using sewage treatment plant sludge as a major substrate seems to be a promising and encouraging alternative for better sludge management. This is a new environmental biotechnological approach for the biodegradation of sludge, which, in addition to producing lignin peroxidase, would reduce treatment and production costs through the use of an environmentally friendly process |
| 1.11.1.14 | lignin peroxidase |
environmental protection |
lignin peroxidase has a applicable potential for the degradation of sulfonated azo dyes |
| 1.11.1.14 | lignin peroxidase |
environmental protection |
removal of four catechols (1,2-dihydroxybenzene), 4-chlorocatechol (4-CC), 4,5-dichlorocatechol (4,5-DCC) and 4-methylcatechol (4-MC) typical pollutants in wastewater derived from oil and paper industries |
| 1.11.1.14 | lignin peroxidase |
environmental protection |
the enzyme is able to decolorize synthetic dyes |
| 1.11.1.16 | versatile peroxidase |
environmental protection |
the enzyme immobilized on yeast cell wall fragments can be used for longterm bioremediation of environments contaminated with azo dyes |
| 1.11.1.16 | versatile peroxidase |
environmental protection |
versatile peroxidases form an attractive ligninolytic enzyme group due to their dual oxidative ability to oxidize Mn(II) and also phenolic and nonphenolic aromatic compounds, and can be used in programs for phytoremediation |
| 1.11.1.18 | bromide peroxidase |
environmental protection |
CPO carries out a wide variety of oxidative reactions, changing the environmental impacts of organic matters |
| 1.12.2.1 | cytochrome-c3 hydrogenase |
environmental protection |
enzyme might be useful in development of a mechanism to remove contaminating uranium from groundwaters |
| 1.13.11.1 | catechol 1,2-dioxygenase |
environmental protection |
in gasoline contaminated environments, aromatic hydrocarbon degrading Rhodococcus populations can be identified based upon the detection and sequence analysis of catechol 1,2-dioxygenase gene. Rhodococcus species are important members of the bacterial community involved in the degradation of aromatic contaminants and their specific detection can help assess functions and activities in the contaminated environments |
| 1.13.11.2 | catechol 2,3-dioxygenase |
environmental protection |
C23O appears to be very powerful and useful tools in the biotreatment of wastewaters and soil decontamination |
| 1.13.11.2 | catechol 2,3-dioxygenase |
environmental protection |
the enzyme also showed resistance to most of the metal ions, surfactants and organic solvents, being a promising biocatalyst for biodegradation of aromatic compounds in complex environments |
| 1.13.11.3 | protocatechuate 3,4-dioxygenase |
environmental protection |
the purified enzyme can be used in bioremediation of polluted groundwater or soil contaminated with various aromatic compounds ranging from monocyclic to polycyclic |
| 1.13.11.3 | protocatechuate 3,4-dioxygenase |
environmental protection |
the enzyme could play a significant role in 2,4,6-trinitrotoluene (TNT) degradation |
| 1.13.11.27 | 4-hydroxyphenylpyruvate dioxygenase |
environmental protection |
the enzyme can be used for enzyme-based sensors for monitoring herbicides used in agriculture, i.e. mesotrione. Compared to the standard sensors, biosensors have assorted advantages, such as practicality, quick response, low cost, and high sensitivity. A nanobiosensor is developed based on HPPD for mesotrione detection |
| 1.13.11.49 | chlorite O2-lyase |
environmental protection |
bacteria with Cld play significant roles in the bioremediation of industrially contaminated sites and also in wastewater treatment |
| 1.13.11.49 | chlorite O2-lyase |
environmental protection |
the enzyme from Nitrospira defluvii is an interesting candidate for bioremediation of chlorite |
| 1.13.11.50 | acetylacetone-cleaving enzyme |
environmental protection |
biodegradation by the enzyme of the widely used industrial chemical acetylacetone, i.e. 2,4-pentanedione, which has toxic effects, in a membrane bioreactor, determination of operational stability of the enzyme in the reactor at different temperatures, simulations |
| 1.14.13.7 | phenol 2-monooxygenase (NADPH) |
environmental protection |
the enzyme is useful in degradation of industrial pollutants |
| 1.14.13.7 | phenol 2-monooxygenase (NADPH) |
environmental protection |
application for enzyme-based remediation of phenolic wastewater or in phenolic biosensor, kinetic properties. Remediation of phenols at its anthropogenic source before it enters into the environmental ecosystem. Microbial degradation has gained attention for treatment of phenols owing to its ability of complete mineralization and cost effectiveness |
