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Search term: environmental protection

Results 1 - 100 of 124 > >>
EC Number
Application
Commentary
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
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
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
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
aryl-alcohol oxidase
environmental protection
the enzyme in white-rot fungi is useful in degradation of aromatic hydrocarbons in a historically contaminated soil
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
12-oxophytodienoate reductase
environmental protection
2,4,6-trinitrotoluene detoxofication, use of plants to remove environmental pollutants; 2,4,6-trinitrotoluene detoxofication, use of plants to remove environmental pollutants; 2,4,6-trinitrotoluene detoxofication, use of plants to remove environmental pollutants
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
bilirubin oxidase
environmental protection
BOX can be used to decolorize synthetic dyes from effluents, especially for anthraquinonic dyes
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
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
azobenzene reductase
environmental protection
potential for the treatment of azo dye contaminated wastewater
nitric oxide reductase (cytochrome c)
environmental protection
removes cytotoxic nitrous oxide
nitric oxide reductase (cytochrome c)
environmental protection
mantains global environmental homeostasis
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
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
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
adenylyl-sulfate reductase
environmental protection
the gene apsA is used for quantitative determination of the organism in wastewater, overview
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
laccase
environmental protection
fast biodegradation of 2,4-dichlorophenol, a potent xenobiotic compound
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
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
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 enzye 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
chloride peroxidase
environmental protection
this enzyme may by employed to treat contaminated soil or water prior to discharge
manganese peroxidase
environmental protection
key enzyme for degradation of environmentally persistent xenobiotics such as pentachlorophenol and dioxins
manganese peroxidase
environmental protection
degradation of recalcitrant high-molecular-mass compounds, such as nylon and melanin, degradation of xenobiotic compounds, bioremediation, decolorization of wastewater
manganese peroxidase
environmental protection
mediated system of degradation is potentially valuable for degradation of synthetic polymers and of environmental pollutants
manganese peroxidase
environmental protection
polycyclic aromatic hydrocarbon degradation
manganese peroxidase
environmental protection
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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
manganese peroxidase
environmental protection
degradation of recalcitrant pollutants
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
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
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
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
lignin peroxidase
environmental protection
lignin peroxidase has a applicable potential for the degradation of sulfonated azo dyes
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
lignin peroxidase
environmental protection
decolorization of textile dyes
lignin peroxidase
environmental protection
the enzyme is able to decolorize synthetic dyes
cytochrome-c3 hydrogenase
environmental protection
enzyme might be useful in development of a mechanism to remove contaminating uranium from groundwaters
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
catechol 2,3-dioxygenase
environmental protection
C23O appears to be very powerful and useful tools in the biotreatment of wastewaters and soil decontamination
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
chlorite O2-lyase
environmental protection
bacteria with Cld play significant roles in the bioremediation of industrially contaminated sites and also in wastewater treatment
chlorite O2-lyase
environmental protection
the enzyme from Nitrospira defluvii is an interesting candidate for bioremediation of chlorite
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
phenol 2-monooxygenase (NADPH)
environmental protection
the enzyme is useful in degradation of industrial pollutants
pentachlorophenol monooxygenase
environmental protection
development of biological methods for the decontamination of halophenol-polluted sites
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
dimethyl-sulfide 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
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
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; 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
long-chain alkane monooxygenase
environmental protection
the thermophilic soluble monomeric LadA is an ideal candidate for treatment of environmental oil pollutions
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
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
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
mercury(II) reductase
environmental protection
detoxification of mercury by immobilized mercuric reductase
mercury(II) reductase
environmental protection
application of the immobilized mercuric reductase for continuous treatment of Hg(II)-containing water in a fixed bed reactor
mercury(II) reductase
environmental protection
the organism can potentially be used for bioremediation in marine environments
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
arsenate reductase (azurin)
environmental protection
important implications for biomediation of arsenite contaminated soils and groud water
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
glutathione gamma-glutamylcysteinyltransferase
environmental protection
yeast cells expressing AtPCS can be used as an inexpensive sorbent for the removal of toxic arsenic
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
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.; 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.; 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.
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.; 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.
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.
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)
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
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
triacylglycerol lipase
environmental protection
degradation of lipid wastes, bioremediation and bioaugumentation, removal of solid and water pollution by hydrocarbons, oils and lipids
acetylcholinesterase
environmental protection
pesticide and organophosphate analysis in different soil samples using the enzyme in a photometric assay, overview
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
cholinesterase
environmental protection
the enzyme may be employed as a biological indicator for assessing pesticide contamination
cutinase
environmental protection
application of cutinase for degradationof dihexyl phthalate in the dihexyl phthalate-contaminated environments may be possible
pyrethroid hydrolase
environmental protection
the engineered Sphingobium sp. strain BA3 is more useful in bioremidation of pyrethroid insecticides-contaminated environment than the wild-type strain JZ-2, overview
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
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
aryldialkylphosphatase
environmental protection
the enzyme is involved in detoxification of organophosphorus pesticides and chemical warfare agents sarin and VX
aryldialkylphosphatase
environmental protection
the enzyme is used for the detoxification of organophosphate pesticides and related chemical warfare agents such as VX and sarin
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
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
diisopropyl-fluorophosphatase
environmental protection
to detoxify nerve agent exposed environments, a decontamination solution known as DS2 is being used in conjunction with bleach
diisopropyl-fluorophosphatase
environmental protection
detoxification of nerve agent exposed environments
cellulase
environmental protection
cellulase producing haloarchael cells may be potentially utilized for the treatment of hypersaline waste water to remove cellulose
chitinase
environmental protection
the enzyme is a good candidate for application in bioremedation of chitin wastes
chitinase
environmental protection
the nezyme is efficient in defense against metal(oid) pollution in environment. The timing of induced responses is likely to be important
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
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
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)
N,N-dimethylformamidase
environmental protection
the enzyme activity is useful to treat industrial effluent containing dimethylformamide obtained from pharmaceutical industry
Aliphatic nitrilase
environmental protection
Candida guilliermondii UFMG-Y65 might be useful for the bioremediation of environments contaminated with nitriles
cadmium-transporting ATPase
environmental protection
overexpression of this fungal transporter in plants can be useful for phytoremediation of lead and cadmium polluted soils
(S)-2-haloacid dehalogenase
environmental protection
detoxification of halogenated herbicides, solvents and other xenobiotic compounds by immobilized enzyme
haloalkane dehalogenase
environmental protection
haloalkane dehalogenases are key enzymes for the degradation of halogenated aliphatic pollutants
haloalkane dehalogenase
environmental protection
because the halogenated substrates are often environmentally toxic industrial byproducts, the enzyme has been suggested to be an useful catalyst for biodegradation and bioremediation
haloalkane dehalogenase
environmental protection
LinB catalyses the conversion of a broad range of halogenated alkanes to their corresponding alcohols which makes it of particular interest for biomediation purposes
haloalkane dehalogenase
environmental protection
haloalkane dehalogenases are exploited for clean-up of groundwater contaminated by halogenated compounds, removal of the side-products from chemical synthesis, and biosensors detecting halogenated contaminants in the environment
haloalkane dehalogenase
environmental protection
DhaA is capable of degrading 1,2,3-trichloropropane, TCP, an industrial waste product that is toxic, extremely recalcitrant to biodegradation, and expensive to dispose of by physical or chemical methods
haloalkane dehalogenase
environmental protection
enzyme DadB and its host, Alcanivorax dieselolei strain B-5, are of potential use for biocatalysis and bioremediation applications
Results 1 - 100 of 124 > >>