EC Number   |
Recommended Name  |
Application |
|---|
   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 |
| 1.1.1.50 | 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 |
| 1.1.2.3 | 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 |
| 1.10.3.2 | 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 |
| 1.11.1.10 | 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 |
| 1.11.1.7 | 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 |
| 1.12.2.1 | 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 |
| 1.13.11.27 | 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 |
| 1.13.11.3 | 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 |
| 1.13.11.49 | 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 |
| 1.14.13.20 | 2,4-dichlorophenol 6-monooxygenase |
environmental protection |
2,4-dichlorophenoxy acetic acid (2,4-D) is of particular concern, as this synthetic auxin has been the most utilized herbicide in the past 50 years. It is prevalent in agricultural fields and has been widely applied in cereal crops to control broadleaved weeds. It inhibits the growth of leaf weeds by accumulating in the plant root. 2,4-D accumulated crops, on consumption, result in gastrointestinal haemorrhage, direct myocardial toxicity, CNS depression, renal failure, and other disorders. The bacterium Bacillus licheniformis strain SL10 finds potential application in the remediation of 2,4-dichlorophenol |
| 1.14.13.20 | 2,4-dichlorophenol 6-monooxygenase |
environmental protection |
immobilized enzyme exhibits great potential for application in bioremediation |
| 1.14.13.245 | assimilatory dimethylsulfide S-monooxygenase |
environmental protection |
Acinetobacter sp. 20B grown on dimethyl sulfide degrades up to 25% of 1.5 mg trichloroethylene/l, respectively. Escherichia coli harboring the DMS monooxygenase genes from strain 20B alone, or in combination with the cumene dioxygenase genes from Pseudomonas fluorescens IP01, degrades up to 50% and 88% of 75 mg TCE/l, respectively. The growth rates of the E. coli recombinants remain nearly unaffected by TCE at least up to 150 mg/l |
| 1.14.13.25 | methane monooxygenase (soluble) |
environmental protection |
pulping wastewater still contains massive refractory organics after biotreatment, with high colority, low biodegradability, and lasting biotoxicity. To eliminate refractory organics in pulping wastewater, a methanotrophic co-metabolic system in a gas cycle Sequencing Batch Biofilm Reactor (gcSBBR) seeded by soil at a ventilation opening of coal mine is quickly built on the 92nd day. The removal rate of COD, colority and TOC is 53.28%, 50.59% and 51.60%, respectively. Analysis of 3D-EEM indicates that glycolated protein-like, melanoidin-like or lignocellulose-like, and humic acid-like decrease by 7.85%, 5.02% and 1.74%, respectively |
| 1.14.13.50 | pentachlorophenol monooxygenase |
environmental protection |
PCP-decontamination of soil and water, degradation of 3,5-dibromophenol derived in soil from the herbicide bromoxynil, i.e. 3,5-dibromo-4-hydroxybenzonitrile |
| 1.14.13.50 | pentachlorophenol monooxygenase |
environmental protection |
development of biological methods for the decontamination of halophenol-polluted sites |
| 1.14.13.50 | pentachlorophenol monooxygenase |
environmental protection |
bioaugmentation of groundwater with known Sphingobium chlorophenolicum L-1, amendment of nutrients, and air sparging result in an enhanced degradation of pentachlorophenol and hence bioremediation of PCP-contaminated groundwater. The amendments to the site undergoing air sparging may result in more effective and less time-consuming bioremediation of pentachlorophenol-contaminated groundwater without adding significantly high cost and labor |
| 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 |
| 1.14.14.1 | unspecific monooxygenase |
environmental protection |
the enzyme is of great importance commercially not only from the point of view of herbicide resistance but also in terms of ecotoxicology |
| 1.14.14.20 | phenol 2-monooxygenase (FADH2) |
environmental protection |
strain UPV-1 is able to grow on phenol as the sole carbon and energy source, removing, concomitantly, the formaldehyde present in phenolic industrial wastewaters |
| 1.14.14.28 | long-chain alkane monooxygenase |
environmental protection |
the thermophilic soluble monomeric LadA is an ideal candidate for treatment of environmental oil pollutions |
| 1.14.15.3 | alkane 1-monooxygenase |
environmental protection |
the enzyme has a tremendous biotechnological potential as a biocatalyst and promising application in the bioremediation of oil-contaminated environments |
| 1.14.18.1 | tyrosinase |
environmental protection |
the integration of cyanide hydratase and tyrosinase open up new possibilities for the bioremediation of wastewaters with complex pollution. Almost full degradation of free cyanide in the model and the real coking wastewaters is achieved by using a recombinant cyanide hydratase in the first step. The removal of cyanide, a strong inhibitor of tyrosinase, enables an effective degradation of phenols by this enzyme in the second step. Phenol is completely removed from a real coking wastewater within 20 h and cresols are removed by 66% under the same conditions |
| 1.14.18.3 | methane monooxygenase (particulate) |
environmental protection |
gene pmoA, which encodes the key subunit of the pMMO enzyme is commonly used as functional biomarker for surveying aerobic methane or ammonia oxidizers in the environment |
| 1.14.99.39 | ammonia monooxygenase |
environmental protection |
identification of organic oxidation products and comparison of the reactivities of monohalogenated ethanes and n-chlorinated C1 to C4 alkanes for oxidation by whole cells of Nitrosomonas europaea. The dehalogenating potential of the ammonia monooxygenase in Nitrosomonas europaea may have practical applications for the detoxification of contaminated soil and groundwater |
| 1.14.99.39 | ammonia monooxygenase |
environmental protection |
gene amoA, which encodes the key subunit of the AMO enzyme is commonly used as functional biomarker for surveying aerobic methane or ammonia oxidizers in the environment |
| 1.15.1.1 | superoxide dismutase |
environmental protection |
Cu/Zn superoxide dismutase might be used as a bioindicator of the aquatic environmental pollution and cellular stress in pearl oyster |
| 1.16.1.1 | mercury(II) reductase |
environmental protection |
application of the immobilized mercuric reductase for continuous treatment of Hg(II)-containing water in a fixed bed reactor |
| 1.16.1.1 | mercury(II) reductase |
environmental protection |
detoxification of mercury by immobilized mercuric reductase |
| 1.16.1.1 | mercury(II) reductase |
environmental protection |
the organism can potentially be used for bioremediation in marine environments |
| 1.16.1.1 | mercury(II) reductase |
environmental protection |
enzyme MerA is a promising candidate for Hg2+ bioremediation |
| 1.16.3.2 | bacterial non-heme ferritin |
environmental protection |
thermostable ferritin can be used in production of clean drinking water and process water. Thermostable ferritin is an excellent system for rapid phosphate and arsenate removal from aqueous solutions down to residual concentrations at the picomolar level |
| 1.17.1.4 | xanthine dehydrogenase |
environmental protection |
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin |
| 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 |
| 1.20.9.1 | arsenate reductase (azurin) |
environmental protection |
important implications for biomediation of arsenite contaminated soils and groud water |
