EC Number   |
Recommended Name |
Application |
|---|
   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 |
| 1.14.13.25 | 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 |
| 1.14.13.245 | 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 |
 1.14.14.1 | 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 |
| 1.20.9.1 | arsenate reductase (azurin) |
environmental protection |
important implications for biomediation of arsenite contaminated soils and groud water |
| 1.97.1.9 | 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 |
| 2.1.1.201 | 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 |
| 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 |
| 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 |
| 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 |
| 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. |
| 2.8.4.1 | 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 |
| 3.1.1.1 | 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 |
| 3.1.1.3 | triacylglycerol lipase |
environmental protection |
degradation of lipid wastes, bioremediation and bioaugumentation, removal of solid and water pollution by hydrocarbons, oils and lipids |
| 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 |
| 3.1.1.8 | cholinesterase |
environmental protection |
the enzyme may be employed as a biological indicator for assessing pesticide contamination |
| 3.1.1.74 | cutinase |
environmental protection |
application of cutinase for degradationof dihexyl phthalate in the dihexyl phthalate-contaminated environments may be possible |
| 3.1.1.88 | 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 |
| 3.1.1.88 | pyrethroid hydrolase |
environmental protection |
the mutant enzyme A171V/D256N is an ideal candidate for the biodegradation of pyrethroids (widely used as insecticides) |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
environmental protection |
a dual enzyme system composed of a polyester hydrolase and a carboxylesterase enhances the biocatalytic degradation of polyethylene terephthalate films. Since the enzymatic PET hydrolysis is inhibited by the degradation intermediate 4-[(2-hydroxyethoxy)carbonyl]benzoate, a dual enzyme system consisting of a polyester hydrolase and the immobilized carboxylesterase TfCa from Thermobifida fusca KW3 is employed for the hydrolysis of PET films at 60°C. HPLC analysis of the reaction products obtained after 24 h of hydrolysis shows an increased amount of soluble products with a lower proportion of 4-[(2-hydroxyethoxy)carbonyl]benzoate in the presence of the immobilized carboxylesterase TfCa. The results indicate a continuous hydrolysis of the inhibitory 4-[(2-hydroxyethoxy)carbonyl]benzoate by the immobilized carboxylesterase TfCa and demonstrate its advantage as a second biocatalyst in combination with a polyester hydrolase for an efficient degradation oft PET films |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
environmental protection |
bioconversion of plastics |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
environmental protection |
Tat-independent secretion of polyethylene terephthalate hydrolase PETase in Bacillus subtilis 168 mediated by its native signal peptide. Widespread utilization of polyethylene terephthalate (PET) has caused critical environmental pollution. The enzymatic degradation of PET is a promising solution to this problem. PETase, which exhibits much higher PET hydrolytic activity than other enzymes, is successfully secreted into extracellular milieu from Bacillus subtilis 168 under the direction of its native signal peptide (named SPPETase) |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
environmental protection |
the enzyme can offer an important contribution towards a future sustainable closed loop plastic recycling industry |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
environmental protection |
the enzyme is a potential tool to solve the issue of polyester plastic pollution |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
environmental protection |
the investigation of structure/function relationships can be used to guide further protein engineering to more effectively depolymerize PET and other synthetic polymers, thus informing a biotechnological strategy to help remediate the environmental scourge of plastic accumulation in nature |
| 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 |
| 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 |
| 3.1.8.1 | 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 3.5.1.4 | 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) |
| 3.5.1.56 | N,N-dimethylformamidase |
environmental protection |
the enzyme activity is useful to treat industrial effluent containing dimethylformamide obtained from pharmaceutical industry |
| 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 |
| 3.5.5.7 | Aliphatic nitrilase |
environmental protection |
Candida guilliermondii UFMG-Y65 might be useful for the bioremediation of environments contaminated with nitriles |
| 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 |
| 3.8.1.2 | (S)-2-haloacid dehalogenase |
environmental protection |
detoxification of halogenated herbicides, solvents and other xenobiotic compounds by immobilized enzyme |
| 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 |
| 3.8.1.5 | 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 |
| 3.8.1.5 | 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 |
| 3.8.1.5 | haloalkane dehalogenase |
environmental protection |
haloalkane dehalogenases are key enzymes for the degradation of halogenated aliphatic pollutants |
| 3.8.1.5 | 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 |
| 3.8.1.5 | haloalkane dehalogenase |
environmental protection |
organisms producing this enzyme are of great interest as bioremediants, the enzyme has also been shown to have uses in combating chemical warfare where it can act against toxic agents like mustard gas |
| 3.8.1.5 | 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 |
| 3.8.1.5 | haloalkane dehalogenase |
environmental protection |
enzyme DadB and its host, Alcanivorax dieselolei strain B-5, are of potential use for biocatalysis and bioremediation applications |
| 3.8.1.5 | haloalkane dehalogenase |
environmental protection |
HLD-containing bacteria are interesting as a cleanup technology for toxic haloalkane wastes produced from industries such as plastics and pesticides manufacture |
| 3.8.1.5 | haloalkane dehalogenase |
environmental protection |
DhaA displayed on the surface of Bacillus subtilis spores retains enzymatic activity, which suggests that it can be used effectively in applications including bioremediation of contaminated environments |
| 3.8.1.5 | haloalkane dehalogenase |
environmental protection |
potential biocatalyst for bioremediation/biosensing of mixed pollutants |
| 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 |
| 3.13.1.1 | UDP-sulfoquinovose synthase |
environmental protection |
the enzyme is useful in biodesulfurization, in which microorganisms selectively remove sulfur atoms from organosulfur compounds, a viable technology to complement the traditional hydrodesulfurization of fuels |
| 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 |
| 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 |
| 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 |
| 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 |
| 4.2.1.24 | porphobilinogen synthase |
environmental protection |
the enzyme can be used as a biomarker for Pb2+ contamination |
| 4.2.1.24 | porphobilinogen synthase |
environmental protection |
in free-living bird species, a decrease is observed in ALAD activity in Griffon vultures and Eagle owls exposed to Pb. Negative relationships are found between ALAD ratio or ALAD activity and logarithmic blood Pb levels in Griffon vultures and Eagle owls, and these relationships are stronger in areas with the highest Pb exposure. ALAD activity in Slender-billed gull and Audouin's gull species may be considerably normal, since very low blood Pb concentrations and no correlations are found |
| 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 |
