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Search term: environmental protection

Results 1 - 100 of 159 > >>
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
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
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
alcohol dehydrogenase (cytochrome c)
environmental protection
potential application of Pseudomonas sp. strain J51 in the treatment of DES-contaminated freshwater and seawater environments
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
BOX can be used to decolorize synthetic dyes from effluents, especially for anthraquinonic dyes
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
NADPH:quinone reductase
environmental protection
NfsA has potential applications in the biodegradation of nitroaromatic environment pollutants, e.g. explosives
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
aromatic nitroreductase [NADPH]
environmental protection
NfsA has potential applications in the biodegradation of nitroaromatic environment pollutants, e.g. explosives
azobenzene reductase
environmental protection
utilization of azo-dye degrading organisms is essential for developing bioremediation strategies in waste-water treatment plants
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
azobenzene reductase
environmental protection
potential for the treatment of azo dye contaminated wastewater
azobenzene reductase
environmental protection
generation of a coupled enzyme system constructed with azoreductase and glucose 1-dehydrogenase for removal of methyl red, evaluation, overview
nitric oxide reductase (cytochrome c)
environmental protection
mantains global environmental homeostasis
nitric oxide reductase (cytochrome c)
environmental protection
removes cytotoxic nitrous oxide
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
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
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
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
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
laccase
environmental protection
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment
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
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%
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
laccase
environmental protection
degradation of synthetic dyes from wastewater using biological treatment
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
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
laccase
environmental protection
the enzyme has potential for application in the treatment of contaminated water with low pH values and high phenolic content
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
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
-
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
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
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
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
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
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
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
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
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
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
enzyme MerA is a promising candidate for Hg2+ bioremediation
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
xanthine dehydrogenase
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
arsenate reductase (azurin)
environmental protection
important implications for biomediation of arsenite contaminated soils and groud water
selenate reductase
environmental protection
the organism is part of an enrichment of a bacterial assemblage from a mine impacted natural marsh sediment that is capable of simultaneous selenate reduction and denitrification, overview
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
Results 1 - 100 of 159 > >>