EC Number   |
Recommended Name  |
Application |
|---|
    3.8.1.2 | (S)-2-haloacid dehalogenase |
environmental protection |
detoxification of halogenated herbicides, solvents and other xenobiotic compounds by immobilized enzyme |
| 1.3.1.42 | 12-oxophytodienoate reductase |
environmental protection |
2,4,6-trinitrotoluene detoxofication, use of plants to remove environmental pollutants |
| 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 |
| 3.3.2.14 | 2,4-dinitroanisole O-demethylase |
environmental protection |
the immobilized enzyme can be used as biocatalyst for detection and destruction of the insensitive explosive, 2,4-dinitroanisole (DNAN), with a wide spectrum of applications ranging from national security and demilitarization to environmental monitoring and restoration |
| 3.7.1.8 | 2,6-dioxo-6-phenylhexa-3-enoate hydrolase |
environmental protection |
potential enzyme resource for the biodegradation of biphenyl, bioremediation of the environmental pollution caused by biphenyl/polychlorinated biphenyls |
| 2.1.1.201 | 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase |
environmental protection |
BoCOQ5-2 methyltransferase is a facilitator of selenium volatilization, biologically based selenium volatilization is a particular area of interest for its potential in making detoxification of selenium pollution highly effective |
| 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 |
| 1.1.1.51 | 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 |
| 4.1.2.43 | 3-hexulose-6-phosphate synthase |
environmental protection |
formaldehyde is thought to be the cause of sick house syndrome, transgenic plants harboring the ribulose monophosphate pathway could be useful to improve air pollution in the indoor 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 |
| 1.13.11.27 | 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 |
| 7.2.2.2 | ABC-type Cd2+ transporter |
environmental protection |
overexpression of this fungal transporter in plants can be useful for phytoremediation of lead and cadmium polluted soils |
| 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 |
| 3.1.1.7 | acetylcholinesterase |
environmental protection |
pesticide and organophosphate analysis in different soil samples using the enzyme in a photometric assay, overview |
| 3.1.1.7 | acetylcholinesterase |
environmental protection |
the enzyme activity in the gill tissue of Crassostrea hongkongensis may be used as a biomarker in monitoring organophosphate contamination in the marine fauna of South China |
| 4.2.1.3 | aconitate hydratase |
environmental protection |
use of enzyme as biomarker of oxidative damage. Exposure of oysters to Cd2+ results in elevated production of reactive oxygen species and enzyme inhibition, which is particualrly pronounced at elevated temperature |
| 1.8.99.2 | adenylyl-sulfate reductase |
environmental protection |
the gene apsA is used for quantitative determination of the organism in wastewater, overview |
| 1.8.4.9 | adenylyl-sulfate reductase (glutathione) |
environmental protection |
APR2 can be exploited for engineering heavy metal-tolerant plants in phytoremediation |
| 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 |
| 3.5.5.7 | Aliphatic nitrilase |
environmental protection |
Candida guilliermondii UFMG-Y65 might be useful for the bioremediation of environments contaminated with nitriles |
| 3.1.3.1 | alkaline phosphatase |
environmental protection |
monthly analysis of the activities of particulate and soluble phosphatase for 1 year in the coastal ecosystems of the North Western Mediterranean Sea. The mean contribution of the particulate activity increases from 56% at an methyl umbelliferyl phosphate concentration of 30 microM to 77% at 0.04 microM. This particulate activity is negatively correlated with the dissolved inorganic phosphorus concentrations, dissolved organic phosphorus and total dissolved phosphorus concentrations when the activities are related to the seawater volume, chlorophyll a or the protein concentration |
| 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 |
| 4.99.1.2 | alkylmercury lyase |
environmental protection |
detoxification of organomercury compounds is of critical importance. The bioorganometallic chemistry of mercury in a sulfur-rich coordination environment is studied in order emulate the structure and function of MerB. One of the three non-structural cysteine residues of MerB that are crucial for enzymatic activity is required to coordinate [HgR]+ in a linear manner, a second cysteine is required to activate the Hg-alkyl group toward protolytic cleavage, and the third cysteine is required to effect the cleavage reaction. |
| 4.99.1.2 | alkylmercury lyase |
environmental protection |
transgenic merB plants express high levels of MerB protein and show some evidence of higher resistance to the organic mercury than wild-type plants, in order to be useful in eastern cottonwood trees to degrade methylmercury at mercury contaminated aquatic sites, merB should be combined with other genes such as merA |
| 4.99.1.2 | alkylmercury lyase |
environmental protection |
a new transgenic tobacco plant for phytoremediation of CH3Hg+ pollution: The new ppk/merT/merB-transgenic tobacco plant, which contains the integrated bacterial merB gene encoding MerB, has the ability to tolerate and accumulate high levels of Hg2+ inside the plant cells from simulated soils, probably via a chelation mechanism of polyP with Hg2+, without releasing mercury vapor into the atmosphere |
| 4.99.1.2 | alkylmercury lyase |
environmental protection |
A recombinant whole-cell bacterial sensor for highly selective and sensitive detection of bioavailable methylmercury in the environment is constructed. The biosensor carries luciferase gene as a reporter under control of a very selective Hg2+-inducible part of the mer-operon from Pseudomonas K-62 plasmid pMR26. A merB gene encoding organomercurial lyase which cleaves the C-Hg bond of methylmercury to give Hg2+ is coexpressed in the sensor. |
| 3.5.1.4 | amidase |
environmental protection |
convenient treatment of acetonitrile-containing wastes using the tandem combination of nitrile hydratase (Rhodococcus pyridinivorans S85-2) and amidase-producing microorganisms (Brevundimonas diminuta AM10-C-1) |
| 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 |
| 1.7.1.B3 | aromatic nitroreductase [NADPH] |
environmental protection |
NfsA has potential applications in the biodegradation of nitroaromatic environment pollutants, e.g. explosives |
| 1.20.9.1 | arsenate reductase (azurin) |
environmental protection |
important implications for biomediation of arsenite contaminated soils and groud water |
| 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 |
| 3.1.8.1 | aryldialkylphosphatase |
environmental protection |
the enzyme is involved in detoxification of organophosphorus pesticides and chemical warfare agents sarin and VX |
| 3.1.8.1 | aryldialkylphosphatase |
environmental protection |
the enzyme is used for the detoxification of organophosphate pesticides and related chemical warfare agents such as VX and sarin |
| 3.1.8.1 | aryldialkylphosphatase |
environmental protection |
enzymes showing phosphotriesterase activity are capable of hydrolysing organophosphate phosphotriesters, a class of synthetic compounds employed worldwide both as insecticides and chemical warfare agents. Thermostable enzymes able to hydrolyse organophosphate phosphotriesters are considered good candidates for the set-up of efficient detoxification tools |
| 3.1.8.1 | aryldialkylphosphatase |
environmental protection |
enzymes showing phosphotriesterase activity are capable of hydrolysing the organophosphate phosphotriesters, a class of synthetic compounds employed worldwide both as insecticides and chemical warfare agents. Thermostable enzymes able to hydrolyse organophosphate phosphotriesters are considered good candidates for the set-up of efficient detoxification tools |
| 3.1.8.1 | aryldialkylphosphatase |
environmental protection |
thermostable phosphotriesterase-like lactonases (PLLs) are able to degrade organophosphates and can be potentially employed as bioremediation tools and bioscavengers |
| 3.1.8.1 | aryldialkylphosphatase |
environmental protection |
thermostable phosphotriesterase-like lactonases (PLLs) are able to degrade organophosphates and can be potentially employed as bioremediation tools and bioscavengers. The enzyme is employable in cleaning organophosphates from different surfaces like glass, tissues, and fruits, also in presence of surfactants and even when dissolved in tap water |
| 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 |
| 2.7.4.1 | ATP-polyphosphate phosphotransferase |
environmental protection |
bacterial microcompartment-directed polyphosphate kinase promotes stable polyphosphate accumulation in Escherichia coli. Specific application of this process to polyphosphate is of potential application for biological phosphate removal |
| 2.7.4.1 | ATP-polyphosphate phosphotransferase |
environmental protection |
E245K mutation leads to very high polyphosphate accumulation in vivo but is not different from the wild type in either activity or chain length of polyphosphate produced in vitro. Polyphosphate accumulation by bacteria is important in biotechnology applications, e.g. to enhanced biological phosphate removal (EBPR) from wastewater |
| 3.8.1.8 | atrazine chlorohydrolase |
environmental protection |
bioremidiation, use of enhanced expression of a modified bacterial atrazine chlorohydrolase, p-AtzA, in transgenic grasses, tall fescue or Festuca arundinacea, ryegrass or Lolium perenne, and switchgrass or Panicum virgatum, and the legume alfalfa, Medicago sativa, for the biodegradation of atrazine |
| 3.8.1.8 | atrazine chlorohydrolase |
environmental protection |
biodegradation by cells encapsulated in silica gel is an economical and environmentally friendly method for the removal of toxic chemicals from the environment. Recombinant Escherichia coli expressing atrazine chlorohydrolase are encapsulated in organically modified silica gels composed of TEOS, silica nanoparticles, and either phenyltriethoxysilane or methyltriethoxysilane. The optimized PTES and MTES gels have atrazine biodegradation rates of 0.041 and 0.047 mol/ml gel, respectively. The rates are approximately 80% higher than that measured in the TEOS gel. Optimized hydrophobic gel material design can be used to enhance both removal and biodegradation of hydrophobic chemicals like atrazine |
| 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) |
| 1.16.3.2 | 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 |
| 1.8.5.4 | 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 |
| 4.1.99.11 | benzylsuccinate synthase |
environmental protection |
toluene is a widespread contaminant and can be degraded under anoxic conditions, catalyzed by benzylsuccinate synthase |
| 4.1.99.11 | benzylsuccinate synthase |
environmental protection |
enzyme BSS and the growing number of additional fumarate-adding enzymes have become model cases for environmental processes in contaminated soils and deep anoxic subsediment habitats, and their isotopic preferences and conserved sequences serving as templates for molecular probes are employed as tools for monitoring these processes in situ |
| 3.2.1.23 | beta-galactosidase |
environmental protection |
the presence of coliforms in polluted water is determined enzymatically in situ by directly monitoring the activity of B-GAL through the hydrolysis of the yellow chromogenic subtrate, chlorophenol red beta-D-galactopyranoside, which produces a red chlorophenol red product, assay evaluation, overview |
| 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 |
| 1.11.1.18 | bromide peroxidase |
environmental protection |
CPO carries out a wide variety of oxidative reactions, changing the environmental impacts of organic matters |
| 4.2.1.1 | carbonic anhydrase |
environmental protection |
the enzyme can be useful in biomimetic sequestration of CO2 into CaCO3 as a biological catalyst |
| 4.2.1.1 | carbonic anhydrase |
environmental protection |
carbon dioxide absorption into carbonate solutions, promoted by the enzyme carbonic anhydrase, is proposed as potential technology for CO2 capture. The use of solid CA-based biocat-alysts allows the enzyme recovery and reuse under continuous operating conditions typical of industrial applications |
| 4.2.1.1 | carbonic anhydrase |
environmental protection |
recombinant engineered mASCA enzyme exhibits high production yield and sufficient stabilities against relatively high temperature and alkaline pH, which are required conditions for the development of more efficient enzymatic CCS systems. Carbon capture and storage (CCS) is a technology that can capture up to 90% of the carbon dioxide (CO2) emissions produced from the use of fossil fuels in electricity generation and industrial processes, preventing the carbon dioxide from entering the atmosphere. mASCA has the potential to play an important role in CCS systems, particularly in an enzyme-based CO2 capture system that requires large amounts of CA enzyme |
| 4.2.1.1 | carbonic anhydrase |
environmental protection |
the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview |
| 3.1.1.1 | carboxylesterase |
environmental protection |
use of enzyme to remove permethrin- and bifenthrin-associated toxicity to Ceriodaphna dubia and Hyalella axteca in a variety of matrices, including laboratory water, river water, river interstitial water, municipal effluent and seawater |
| 3.1.1.1 | carboxylesterase |
environmental protection |
the enzyme can efficiently hydrolyze a wide range of synthetic pyrethroids including fenpropathrin, permethrin, cypermethrin, cyhalothrin, deltamethrin and bifenthrin, which makes it a potential candidate for the detoxification of pyrethroids for the purpose of biodegradation |
| 3.1.1.1 | carboxylesterase |
environmental protection |
the catalytic efficiencies (kcat/Km) of Fluazifop-P-butyl carboxylesterase (FpbH) for different AOPP herbicides are higher than those of Cyhalofop-butyl esterase (ChbH) from Pseudomonas azotoformans and Fenoxaprop-ethyl hydrolase (FeH) from Rhodococcus sp.. FpbH differs from previously reported AOPP herbicide carboxylesterases and might be a good candidate enzyme for biodegradation, especially when diclofop-methyl and/or haloxyfop-P-methyl are the dominant pollutants |
| 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 |
| 3.2.1.4 | cellulase |
environmental protection |
cellulase producing haloarchael cells may be potentially utilized for the treatment of hypersaline waste water to remove cellulose |
| 3.2.1.14 | chitinase |
environmental protection |
chitin and chitinolytic bacteria addition can reduce the population of fungal plant pathogens in soil and enhance the growth of plants. In this biocontrol and environmental bioremediation, communities of soil bacteria and the addition of chitinous materials play an important role |
| 3.2.1.14 | chitinase |
environmental protection |
the enzyme is a good candidate for application in bioremedation of chitin wastes |
| 3.2.1.14 | chitinase |
environmental protection |
the enzyme is efficient in defense against metal(oid) pollution in environment. The timing of induced responses is likely to be important |
| 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 |
| 1.13.11.49 | 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 |
| 3.1.1.8 | cholinesterase |
environmental protection |
the enzyme may be employed as a biological indicator for assessing pesticide contamination |
| 2.8.4.1 | coenzyme-B sulfoethylthiotransferase |
environmental protection |
expression of methyl-coenzyme M reductase from an unculturable organism in Methanosarcina acetivorans to effectively run methanogenesis in reverse. Methanosarcina acetivorans cells heterologously producing methyl-coenzyme M reductase consume up to 9% of methane (corresponding to 109 micromol of methane) after 6 weeks of anaerobic growth on methane and utilize 10 mM FeCl3 as an electron acceptor. When incubated on methane for 5 days, high-densities of cells consume 15% methane (corresponding to 143 micromol of methane), and produce 10.3 mM acetate (corresponding to 52 micromol of acetate) |
| 2.8.4.1 | coenzyme-B sulfoethylthiotransferase |
environmental protection |
metabolization of methane can positively influence the environment |
| 3.1.1.74 | cutinase |
environmental protection |
application of cutinase for degradationof dihexyl phthalate in the dihexyl phthalate-contaminated environments may be possible |
| 4.2.1.104 | cyanase |
environmental protection |
potential biotechnological application in environmental detoxification |
| 4.2.1.104 | cyanase |
environmental protection |
cyanate and its derivatives are considered as environmental hazardous materials. Cyanate is released to the environment through many chemical industries and mining wastewater. Cyanase enzyme converts cyanate into CO2 and NH3 in a bicarbonate-dependent reaction. At low cyanate concentrations, the endogenous plant cyanases play a vital role in cyanate detoxification. But such cyanate biodegradation system is probably insufficient due to the excess cyanate concentrations at contaminated sites. Evaluation of transgenic plant resistance to cyanate stress. The enzyme is a candidate for developing novel ecofriendly phytoremediation systems for cyanate detoxification |
| 4.2.1.66 | cyanide hydratase |
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 |
| 3.5.2.15 | cyanuric acid amidohydrolase |
environmental protection |
cyanuric acid hydrolases are of industrial importance because of their use in aquatic recreational facilities to remove cyanuric acid, a stabilizer for the chlorine. Degradation of excess cyanuric acid is necessary to maintain chlorine disinfection in the waters |
| 3.5.2.15 | cyanuric acid amidohydrolase |
environmental protection |
di- and trichloroisocyanuric acids are widely used as water disinfection agents, but cyanuric acid accumulates with repeated additions and must be removed to maintain free hypochlorite for disinfection. The study describes the development of methods for using a cyanuric acid-degrading enzyme contained within nonliving cells that are encapsulated within a porous silica matrix |
| 3.5.2.15 | cyanuric acid amidohydrolase |
environmental protection |
di- and trichloroisocyanuric acids are widely used as water disinfection agents, but cyanuric acid accumulates with repeated additions and must be removed to maintain free hypochlorite for disinfection. The study describes the development of methods for using a cyanuric acid-degrading enzyme contained within nonliving cells that are encapsulated within a porous silica matrix. The optimum enzyme for these purposes was found to be the cyanuric acid hydrolase from Moorella thermoacetica. A water-recycling, flowthrough system is constructed and shown to be effective in removing 10 mM M cyanuric acid, a concentration well above that encountered in real-world disinfection processes |
| 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 |
| 2.5.1.47 | cysteine synthase |
environmental protection |
H2S is a major environmental pollutant, highly toxic to living organisms at high concentrations. Even at low concentrations, it causes an unpleasant odor from wetlands, especially from wastewater. Plants can utilize hydrogen sulfide as a sulfur source to synthesize cysteine. It is thus feasible to use aquatic plants, which possess high potential for sulfur assimilation, to remove hydrogen sulfide from the wetland. Transgenic rice plants over-expressing cysteine synthase exhibit 3fold elevated cysteine synthase activity, and incorporate more H2S into cysteine and glutathione than their wild type counterparts upon exposure to a high level of H2S. Overexpression of cysteine synthase in aquatic plants is a viable approach to remove H2S from polluted environments |
| 1.12.2.1 | cytochrome-c3 hydrogenase |
environmental protection |
enzyme might be useful in development of a mechanism to remove contaminating uranium from groundwaters |
| 3.1.8.2 | diisopropyl-fluorophosphatase |
environmental protection |
detoxification of nerve agent exposed environments |
| 3.1.8.2 | diisopropyl-fluorophosphatase |
environmental protection |
to detoxify nerve agent exposed environments, a decontamination solution known as DS2 is being used in conjunction with bleach |
| 3.1.8.2 | diisopropyl-fluorophosphatase |
environmental protection |
enzyme DFPase can be used as in vivo detoxifying agent for elimination of organophosphorus chemicals, used as pesticides and warfare nerve agent, e.g. sarin, soman, or tabun |
| 3.1.8.2 | diisopropyl-fluorophosphatase |
environmental protection |
the engineered bacterium, prepared with an N-terminal domain of the ice nucleation protein (InaV-N) as an anchoring motif on cell surface of expressing bacteria, can be used in the bioremediation of pesticide-contaminated environments |
| 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 |
| 2.8.3.16 | formyl-CoA transferase |
environmental protection |
bacterial oxalate-degrading function, microbiological processes are considered as the main oxalate sinks in natural environments, in soil oxalate from fungi, plant root exudates and decaying plant tissues display powerful metal chelating properties. Oxalate takes part in plant nutrition status by increasing the availability of phosphate and other poorly soluble micro-nutriments, through its ability to complex and remove excess metal cations. It also plays an important role in the detoxification of heavy metals in the vicinity of plant roots. |
| 2.3.2.15 | glutathione gamma-glutamylcysteinyltransferase |
environmental protection |
yeast cells expressing AtPCS can be used as an inexpensive sorbent for the removal of toxic arsenic |
| 3.1.4.46 | glycerophosphodiester phosphodiesterase |
environmental protection |
the enzyme might be useful in the bioremediation of soil, through the detoxification of organophosphate pesticides and products of the degradation of nerve agents |
| 3.8.1.3 | haloacetate dehalogenase |
environmental protection |
the enzyme has a great potential in lowing its energy barrier toward efluorination of per- or polyfluoropropionic acids. Future in silico and in vitro efforts focusing on the directed mutations and enzyme engineering are required to enable its efficient degradation toward perfluorocarboxylic acids |
| 3.8.1.5 | haloalkane dehalogenase |
environmental protection |
enzyme might be utilized for bioremediation of organohalide-contaminated industrial waste |
