1.1.1.50 3alpha-hydroxysteroid 3-dehydrogenase (Si-specific) environmental protection the mutant Comamonas testosteroni strain CT-GFP5-1 can be used as a sensitive biosensor system for steroid determination in the environment 1.1.1.51 3(or 17)beta-hydroxysteroid dehydrogenase environmental protection transcriptional repressor phaR knockout mutants have better ability to degrade steroids than wild-type Comamonas testosteroni ATCC11996 and might therefore be used in bioremediation 1.1.1.149 20alpha-hydroxysteroid dehydrogenase environmental protection diesel exhaust components are inhibitory on 20alpha-hydroxysteroid dehydrogenase in liver and lung cytosol, with little inhibition in kidney cytosol 1.1.1.284 S-(hydroxymethyl)glutathione dehydrogenase environmental protection the enzyme is useful in elimination of formaldehyde, a toxic mutagen mediating apoptosis in cells, from consumers goods and environment 1.1.2.3 L-lactate dehydrogenase (cytochrome) environmental protection the reductive pathway of the enzyme resulting in formation of less toxic Cr(III)-species is suggested to be the most important among possible mechanisms for chromate biodetoxification 1.1.2.8 alcohol dehydrogenase (cytochrome c) environmental protection potential application of Pseudomonas sp. strain J51 in the treatment of DES-contaminated freshwater and seawater environments 1.1.3.7 aryl-alcohol oxidase environmental protection the enzyme in white-rot fungi is useful in degradation of aromatic hydrocarbons in a historically contaminated soil 1.2.1.65 salicylaldehyde dehydrogenase environmental protection the ability to degrade acenaphthylene and other aromatic compounds makes this strain ideal candidate for application in remediation at the contaminated sites 1.3.1.32 maleylacetate reductase environmental protection further evolution to more catalytically active PcpE may be an important contributor to improved Sphingobium chlorophenolicum L-1-mediated bioremediation of pentachlorophenol 1.3.1.42 12-oxophytodienoate reductase environmental protection 2,4,6-trinitrotoluene detoxofication, use of plants to remove environmental pollutants 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 1.4.3.12 cyclohexylamine oxidase environmental protection as a potential biocatalyst, the enzyme is promising in controlling cyclohexylamine pollution and deracemization of chiral amines 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 1.6.5.5 NADPH:quinone reductase environmental protection NfsA has potential applications in the biodegradation of nitroaromatic environment pollutants, e.g. explosives 1.6.5.6 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 1.7.1.2 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 1.7.1.B3 aromatic nitroreductase [NADPH] environmental protection NfsA has potential applications in the biodegradation of nitroaromatic environment pollutants, e.g. explosives 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) 1.7.2.5 nitric oxide reductase (cytochrome c) environmental protection mantains global environmental homeostasis 1.7.2.5 nitric oxide reductase (cytochrome c) environmental protection removes cytotoxic nitrous oxide 1.7.2.8 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 1.8.4.9 adenylyl-sulfate reductase (glutathione) environmental protection APR2 can be exploited for engineering heavy metal-tolerant plants in phytoremediation 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 1.8.5.5 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 1.8.5.5 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 1.8.99.2 adenylyl-sulfate reductase environmental protection the gene apsA is used for quantitative determination of the organism in wastewater, overview 1.10.3.2 laccase environmental protection fast biodegradation of 2,4-dichlorophenol, a potent xenobiotic compound 1.10.3.2 laccase environmental protection laccase is capable of efficiently removing 2,4-dimethylphenol from water at very low enzyme concentrations and hence shows great potential for cost-effective industrial applications 1.10.3.2 laccase environmental protection LI1 shows activity over a broad range of pH and temperature, which may make it useful in the biodegradation of phenolic compounds present in wastewater from several industrial processes 1.10.3.2 laccase environmental protection the stability of this laccase against metal ions makes the enzyme an efficient agent in the treatment of wastewater containing heavy metals 1.10.3.2 laccase environmental protection cyanobacterial laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. Due to phototrophic mode of nutrition, short generation time and easy mass cultivation, Spirulina platensis laccase appears as good candidate for laccase production. The high yield of laccase in short production period are profitable for its industrial application. Pure Spirulina platensis laccase alone can efficiently decolorized anthraquinonic dye Reactive Blue 4 without any mediators which makes it cost effective and suitable candidate for decolorization of synthetic dyes and help in waste water treatment 1.10.3.2 laccase environmental protection degradation of synthetic dyes from wastewater using biological treatment 1.10.3.2 laccase environmental protection laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment 1.10.3.2 laccase environmental protection laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment, thermostable and acidophilic laccase that can efficiently decolorize several synthetic dyes without addition of an expensive redox mediator 1.10.3.2 laccase environmental protection laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. The enzyme alone can decolorize indigo carmine partially after 60-min incubation at 45°C. Decolorization is much more efficient in the presence of syringaldehyde. Nearly 90 % decolorization is observed within 20 min 1.10.3.2 laccase environmental protection laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. The enzyme can also be considered as a candidate for treating industrial effluent containing malachite green 1.10.3.2 laccase environmental protection laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. The enzyme is effective in the decolorization of bromothymol blue, evans blue, methyl orange, and malachite green with decolorizationefficiencies of 50%-85% 1.10.3.2 laccase environmental protection laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. Two anthraquinonic dyes (reactive blue 4 and reactive yellow brown) and two azo dyes (reactive red 11 and reactive brilliant orange) can be partially decolorized by purified laccase in the absence of a mediator. The decolorization process is efficiently promoted when methylsyringate is present, with more than 90 % of color removal occurring in 3 h at pH 7.0 or 9.0 1.10.3.2 laccase environmental protection laccase can be efficiently used to decolorize synthetic dye and is a suitable candidate for the treatment of wastewater from industrial effluents 1.10.3.2 laccase environmental protection laccase can be efficiently used to decolorize synthetic dye and is a suitable candidate for the treatment of wastewater from industrial effluents. The wide pH- and thermostability attributes of immobilized laccase make them suitable for environmental applications 1.10.3.2 laccase environmental protection sensitive, rapid, and precise determination of phenols and their derivatives is important in environmental control and protection. An amperometric principle-based biosensor, employing immobilized laccase enzyme from Trametes versicolor, is developed for the detection of disubstituted methyl and methoxy phenols (industrial effluents). Evaluation of the influence of different enzyme immobilization techniques, on nylon membrane, on the performances of laccase-based Clark-type electrodes. The analytical properties and operating stabilities of the resulting biosensors are tested with different disubstituted methyl and methoxy derivatives of phenol substrates. Co-cross-linking method is superior to the other methods of immobilization in terms of sensitivity, limit of detection, response time, and operating stability. In co-cross-linking method of immobilization, laccase is mixed with bovine serum albumin as protein-based stabilizing agent and glutaraldehyde as crosslinking agent 1.10.3.2 laccase environmental protection the enzyme has potential for application in the treatment of contaminated water with low pH values and high phenolic content 1.10.3.2 laccase environmental protection the enzyme is potentially useful for industrial and environmental applications such as textile finishing and wastewater treatment. It decolorizes structurally different dyes and a real textile effluent 1.10.3.2 laccase environmental protection decolorization of industrial dyes with different chemical structures and decolorization of industrial wastewaters 1.10.3.2 laccase environmental protection decolorization of industrial dyes. Evans blue decolorization and detoxification 1.10.3.2 laccase environmental protection deinking of old newspaper, indigo carmine decolorization 1.10.3.2 laccase environmental protection good application prospect in wastewater treatment and dye degradation. error-prone PCR is a feasible method to improve the degradation activity of laccase for environmental pollutants, which provide a basis for the application of laccase on dye degradation and other environmental pollutants 1.10.3.2 laccase environmental protection laccases are very important in removing environmental pollutants, detoxification from wastewater 1.10.3.2 laccase environmental protection laccases are very important in removing environmental pollutants. Detoxification from wastewater 1.10.3.2 laccase environmental protection potential for industrial wastewater treatments 1.10.3.2 laccase environmental protection the enzyme is able to decolorize efficiently a variety of chemical dyes, thus, being potentially applicable in textile and environmental industries 1.10.3.2 laccase environmental protection the enzyme is an ideal candidate for lots of biotechnological and industrial applications due to its stability in the extreme conditions 1.10.3.2 laccase environmental protection the immobilized laccase transforms diclofenac to 4-OH diclofenac. The immobilized laccase can be used to transform or degrade several recalcitrant compounds from industrial effluents 1.10.3.2 laccase environmental protection the surface display laccase (SDL) biocatalyst, where the enzyme laccase is displayed on the surface of biological cells through synthetic biology, provides a biocatalytic material for removal of emerging contaminants from wastewater 1.10.3.2 laccase environmental protection treating waste water containing synthetic dyes 1.11.1.7 peroxidase environmental protection biodegradation of toxic and carcinogenic phenolic contaminants and related compounds in industrial effluents. Calotropis procera is a drought-resistant local plant that grows wild in the natural habitat of Nigerian throughout the year. Calotropis procera root could be an environmentally sustainable source of peroxidase for a low technological solution for phenol remediation 1.11.1.7 peroxidase environmental protection the removal of textile dyes from wastewater by using plant peroxidases offers environmentally effective solutions 1.11.1.10 chloride peroxidase environmental protection chloroperoxidase shows oxidative dehalogenation activity and is significantly more robust than other peroxidases and functions under harsher reaction conditions compared to other biocatalysts. Expanding the scope of reactivity achieved by the enzyme may be beneficial for industrial and biotechnological functions in the future. This considerable extension of already known activities could lead to the use of the enzyme as a biocatalyst in the field of bioremediation and a broader understanding of both how peroxidases and cytochrome P450s react with halogenated organic substrates 1.11.1.10 chloride peroxidase environmental protection this enzyme may by employed to treat contaminated soil or water prior to discharge 1.11.1.10 chloride peroxidase environmental protection amino modified magnetic halloysite nanotube supporting chloroperoxidase immobilization is useful for enhanced stability, reusability, and efficient degradation of pesticide residue in wastewater. Degradation of mesotrione in wastewater by the immobilized CPO 1.11.1.10 chloride peroxidase environmental protection CPO carries out a wide variety of oxidative reactions, changing the environmental impacts of organic matters 1.11.1.13 manganese peroxidase environmental protection - 1.11.1.13 manganese peroxidase environmental protection thiol-mediated degradation of dimeric model compounds and of polymeric lignin by MnP has potential applications in the degradation of industrial lignins 1.11.1.13 manganese peroxidase environmental protection key enzyme for degradation of environmentally persistent xenobiotics such as pentachlorophenol and dioxins 1.11.1.13 manganese peroxidase environmental protection degradation of recalcitrant high-molecular-mass compounds, such as nylon and melanin, degradation of xenobiotic compounds, bioremediation, decolorization of wastewater 1.11.1.13 manganese peroxidase environmental protection polycyclic aromatic hydrocarbon degradation 1.11.1.13 manganese peroxidase environmental protection mediated system of degradation is potentially valuable for degradation of synthetic polymers and of environmental pollutants 1.11.1.13 manganese peroxidase environmental protection degradation of recalcitrant pollutants 1.11.1.13 manganese peroxidase environmental protection as to denim bleaching, sodium hypochlorite treatment is primarily used and this gives rise to problems such as chemical injuries, denim yellowness and reduced denim strength. To ensure the low-cost and ecofriendly advantages, denim biobleaching using oxidizing enzymes such as manganese peroxidases (MnPs) and laccases is an ideal alternative. In the presence of MnPs, denim bleaching by laccases is greatly enhanced. Usage of recombinant white-rot fungi MnP in denim bleaching and PAH degradation 1.11.1.13 manganese peroxidase environmental protection fibrous bed culture of Bacillus velezensis strain Al-Dhabi 140 might be an efficient strain for tetracycline removal from artificial wastewater, even from natural wastewater 1.11.1.13 manganese peroxidase environmental protection manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes 1.11.1.13 manganese peroxidase environmental protection the enzyme can degrade sulfamethoxazole (SMX), a broad-spectrum antibiotic (one non-phenolic compound) that has been widely used as a growth promoter in the breeding industry. SMX has been widely detected in effluents, soils, and surface waters in China. SMX is a persistent and polar organic compound in effluent with a half-life time of 17.8 days. More seriously, the SMX in aquatic environments may accelerate the spread of sul genes (antibiotic resistance genes (ARGs)) in microbial populations, and this would have detrimental effects on the ecosystem balance 1.11.1.14 lignin peroxidase environmental protection use of Phanerochaete chrysosporium and its enzyme lignin peroxidase in the degradation of environmental pollutants such as dye. High efficient degradation of dyes with lignin peroxidase coupled with glucose oxidase 1.11.1.14 lignin peroxidase environmental protection decolorization of textile dyes 1.11.1.14 lignin peroxidase environmental protection the enzyme shows the potential to be applied in the treatment of textile effluents (decolorization of dyes). The results from the selection of dyes such as methylene blue, malachite green and methyl orange show that the enzyme is able to remove a higher content of methylene blue (14%) compared to the other two dyes (3-8%). The optimization with the OFAT method determined the operating conditions of the decolorization of methylene blue dye at temperature 55°C, pH 5.0 (in 50 mM sodium acetate buffer) with H2O2 concentration 4.0 mM. The addition of veratryl alcohol to the reaction mixture has no affect on decolorization of dye 1.11.1.14 lignin peroxidase environmental protection a high and sustainable lignin peroxidase activity is achieved via in situ release of H2O2 by a co-immobilized glucose oxidase. The present co-immobilization system is demonstrated to be very effective for lignin peroxidase mediated dye decolourization 1.11.1.14 lignin peroxidase environmental protection lignin peroxidase enzyme production using sewage treatment plant sludge as a major substrate seems to be a promising and encouraging alternative for better sludge management. This is a new environmental biotechnological approach for the biodegradation of sludge, which, in addition to producing lignin peroxidase, would reduce treatment and production costs through the use of an environmentally friendly process 1.11.1.14 lignin peroxidase environmental protection lignin peroxidase has a applicable potential for the degradation of sulfonated azo dyes 1.11.1.14 lignin peroxidase environmental protection removal of four catechols (1,2-dihydroxybenzene), 4-chlorocatechol (4-CC), 4,5-dichlorocatechol (4,5-DCC) and 4-methylcatechol (4-MC) typical pollutants in wastewater derived from oil and paper industries 1.11.1.14 lignin peroxidase environmental protection the enzyme is able to decolorize synthetic dyes 1.11.1.16 versatile peroxidase environmental protection the enzyme immobilized on yeast cell wall fragments can be used for longterm bioremediation of environments contaminated with azo dyes 1.11.1.16 versatile peroxidase environmental protection versatile peroxidases form an attractive ligninolytic enzyme group due to their dual oxidative ability to oxidize Mn(II) and also phenolic and nonphenolic aromatic compounds, and can be used in programs for phytoremediation 1.11.1.18 bromide peroxidase environmental protection CPO carries out a wide variety of oxidative reactions, changing the environmental impacts of organic matters 1.12.2.1 cytochrome-c3 hydrogenase environmental protection enzyme might be useful in development of a mechanism to remove contaminating uranium from groundwaters 1.13.11.1 catechol 1,2-dioxygenase environmental protection in gasoline contaminated environments, aromatic hydrocarbon degrading Rhodococcus populations can be identified based upon the detection and sequence analysis of catechol 1,2-dioxygenase gene. Rhodococcus species are important members of the bacterial community involved in the degradation of aromatic contaminants and their specific detection can help assess functions and activities in the contaminated environments 1.13.11.2 catechol 2,3-dioxygenase environmental protection C23O appears to be very powerful and useful tools in the biotreatment of wastewaters and soil decontamination 1.13.11.2 catechol 2,3-dioxygenase environmental protection the enzyme also showed resistance to most of the metal ions, surfactants and organic solvents, being a promising biocatalyst for biodegradation of aromatic compounds in complex environments 1.13.11.3 protocatechuate 3,4-dioxygenase environmental protection the purified enzyme can be used in bioremediation of polluted groundwater or soil contaminated with various aromatic compounds ranging from monocyclic to polycyclic 1.13.11.3 protocatechuate 3,4-dioxygenase environmental protection the enzyme could play a significant role in 2,4,6-trinitrotoluene (TNT) degradation 1.13.11.27 4-hydroxyphenylpyruvate dioxygenase environmental protection the enzyme can be used for enzyme-based sensors for monitoring herbicides used in agriculture, i.e. mesotrione. Compared to the standard sensors, biosensors have assorted advantages, such as practicality, quick response, low cost, and high sensitivity. A nanobiosensor is developed based on HPPD for mesotrione detection 1.13.11.49 chlorite O2-lyase environmental protection bacteria with Cld play significant roles in the bioremediation of industrially contaminated sites and also in wastewater treatment 1.13.11.49 chlorite O2-lyase environmental protection the enzyme from Nitrospira defluvii is an interesting candidate for bioremediation of chlorite 1.13.11.50 acetylacetone-cleaving enzyme environmental protection biodegradation by the enzyme of the widely used industrial chemical acetylacetone, i.e. 2,4-pentanedione, which has toxic effects, in a membrane bioreactor, determination of operational stability of the enzyme in the reactor at different temperatures, simulations 1.14.13.7 phenol 2-monooxygenase (NADPH) environmental protection the enzyme is useful in degradation of industrial pollutants 1.14.13.7 phenol 2-monooxygenase (NADPH) environmental protection application for enzyme-based remediation of phenolic wastewater or in phenolic biosensor, kinetic properties. Remediation of phenols at its anthropogenic source before it enters into the environmental ecosystem. Microbial degradation has gained attention for treatment of phenols owing to its ability of complete mineralization and cost effectiveness 1.14.13.20 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 4.2.1.84 nitrile hydratase environmental protection degradation of nitrile waste 4.2.1.84 nitrile hydratase environmental protection NHase is used in two-step degradation (including amidase, EC 3.5.1.4) of acetonitrile-containing waste 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 4.2.2.2 pectate lyase environmental protection alkaline pectate lyases play an important role in mild and eco-friendly bioscouring pretreatment processes in the textile industry. So far, only a few pectate lyases can be applied in industrial-scale production, and many of them exhibit high production cost, low activity, and/or do not meet the treatment requirements. Recombinant PelB has with promising properties for use in bioscouring in the textile pretreatment process and is a potential enzyme for industrial applications 4.2.2.2 pectate lyase environmental protection biotechnological applications of microbial pectate lyases in plant fiber processing are considered as environmentally friendly. As such, they become promising substitutes for conventional chemical degumming process 4.2.2.2 pectate lyase environmental protection the conventional degumming process of ramie with alkaline treatment at high temperature causes severe environmental pollution. Pectate lyases can be used to remove pectin from ramie in a degumming process with reduced environmental pollution and energy consumption 4.2.3.27 isoprene synthase environmental protection analysis of in vivo isoprene emission. The in vivo rate constant of IspS obeys the Arrhenius law, with an activation energy of 42.8 kJ per mol. Steady-state isoprene emission has a significantly lower temperature optimum than IspS and higher activation energy. The reversible temperature-dependent decrease in the rate of isoprene emission between 35°C and 44°C is caused by decreases in dimethylallyl diphosphate concentration, possibly reflecting reduced pools of energetic metabolites generated in photosynthesis, particularly of ATP. Strong control of isoprene temperature responses by the dimethylallyl diphosphate pool implies that transient temperature responses under fluctuating conditions in the field are driven by initial dimethylallyl diphosphate pool size as well as temperature-dependent modifications in dimethylallyl diphosphate pool size during temperature transients 4.2.3.27 isoprene synthase environmental protection isoprene emission patterns in transgenic tobacco plants are remarkably similar to naturally emitting plants under a wide variety of conditions. Emissions correlate with photosynthetic rates in developing and mature leaves, and with the amount of isoprene synthase protein in mature leaves. Isoprene synthase protein levels do not change under short-term increase in heat/light, despite an increase in emissions under these conditions. A robust circadian pattern can be observed in emissions from long-day plants. Substrate supply and changes in enzyme kinetics rather than changes in isoprene synthase levels or post-translational regulation of activity seem to be the primary controls on isoprene emission in mature transgenic tobacco leaves 4.2.3.27 isoprene synthase environmental protection regulation of isoprene emission. Upon darkening a leaf, isoprene emission falls nearly to zero but then increases for several min before falling back to nearly zero. Time of appearance of this burst of isoprene is highly temperature dependent, occurring sooner at higher temperatures. During a rapid temperature switch from 30°C to 40°C, isoprene emission increases transiently with concomitant increase in isoprene synthase activity, while dimethylallyl diphosphate level stays constant during the switch. One h after switching to 40!, the amount of dimethylallyl diphosphate falls but the rate constant for isoprene synthase remains constant, indicating that the high temperature falloff in isoprene emission results from a reduction in the supply of dimethylallyl diphosphate rather than from changes in isoprene synthase activity 4.4.1.11 methionine gamma-lyase environmental protection enzyme is not an important source of volatile methanethiol 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. 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