EC Number   |
Recommended Name  |
Application |
|---|
    1.1.1.1 | alcohol dehydrogenase |
degradation |
direct conversion of switchgrass to ethanol without conventional pretreatment of the biomass is accomplished by deletion of lactate dehydrogenase and heterologous expression of a Clostridium thermocellum bifunctional acetaldehyde/alcohol dehydrogenase in Caldicellulosiruptor bescii. Whereas wild-type Caldicellulosiruptor bescii lacks the ability to make ethanol, 70% of the fermentation products in the engineered strain are ethanol (12.8 mM ethanol directly from 2% wt/vol switchgrass) with decreased production of acetate by 38% compared with wild-type |
| 1.1.1.1 | alcohol dehydrogenase |
degradation |
expression of AdhB gene in an ldh deletion mutant of Caldicellulosiruptor bescii leads to ethanol production at 75°C, near the ethanol boiling point. The AdhB expressing strain produces ethanol (1.4 mM on Avicel, 0.4 mM on switchgrass) as well as acetate (13.0 mM on Avicel, 15.7 mM on switchgrass). The addition of 40 mM MOPS to the growth medium increases the maximal growth yield of C. bescii by approximately twofold |
| 1.1.1.1 | alcohol dehydrogenase |
degradation |
expression of AdhB gene in an ldh deletion mutant of Caldicellulosiruptor bescii leads to ethanol production at 75°C, near the ethanol boiling point. The AdhE expressing strain produce ethanol (2.3 mM on Avicel, 1.6 mM on switchgrass) and acetate (12.3 mM on Avicel, 15.1 mM on switchgrass). The addition of 40 mM MOPS to the growth medium increases the maximal growth yield of C. bescii by approximately twofold |
| 1.1.1.159 | 7alpha-hydroxysteroid dehydrogenase |
degradation |
new integrated chemo-enzymatic synthesis of ursodeoxycholic acid starting from sodium cholate by 7alpha- and 12alpha-hydroxysteroid dehydrogenases |
| 1.1.1.176 | 12alpha-hydroxysteroid dehydrogenase |
degradation |
new integrated chemo-enzymatic synthesis of ursodeoxycholic acid starting from sodium cholate by 7alpha- and 12alpha-hydroxysteroid dehydrogenases |
| 1.1.1.203 | uronate dehydrogenase |
degradation |
development of a simple and specific assay for D-glucuronate using Udh, stability in solution and high activity of Udh, as well as its relatively easy purification method, provide researchers with an alternative method to study D-glucuronate-related metabolism |
| 1.1.1.211 | long-chain-3-hydroxyacyl-CoA dehydrogenase |
degradation |
when gene encoding 3-hydroxyacyl-CoA dehydrogenase is deleted, it is possible to produce medium-chain-length polyhydroxyalkanoates containing only two different monomer structures |
| 1.1.1.27 | L-lactate dehydrogenase |
degradation |
direct conversion of switchgrass to ethanol without conventional pretreatment of the biomass is accomplished by deletion of lactate dehydrogenase and heterologous expression of a Clostridium thermocellum bifunctional acetaldehyde/alcohol dehydrogenase. Whereas wild-type Caldicellulosiruptor bescii lacks the ability to make ethanol, 70% of the fermentation products in the engineered strain are ethanol (12.8 mM ethanol directly from 2% wt/vol switchgrass) with decreased production of acetate by 38% compared with wild-type |
| 1.1.1.284 | S-(hydroxymethyl)glutathione dehydrogenase |
degradation |
the enzyme is useful in elimination of formaldehyde, a toxic mutagen mediating apoptosis in cells, from consumers goods and environment |
| 1.1.1.284 | S-(hydroxymethyl)glutathione dehydrogenase |
degradation |
a Saccharomyces cerevisiae mutant lacking the gene for S-hydroxymethylglutathione dehydrogenase and expressing FldA is able to degrade 4 mM formaldehyde within 30 h |
| 1.1.1.90 | aryl-alcohol dehydrogenase |
degradation |
the enzyme is active in toluene degradtion in a reactor, containing the fungus Paecilomyces variotii strain CBS115145, for biofiltration of toluene |
| 1.1.3.13 | alcohol oxidase |
degradation |
the purified enzyme is able to decolorize textile dyes, Red HE7B (57.5%) and Direct Blue GLL (51.09%) within 15 h at 0.04 nm/ml concentration |
| 1.1.3.9 | galactose oxidase |
degradation |
the enzyme can be used for oxygen removal |
| 1.1.99.18 | cellobiose dehydrogenase (acceptor) |
degradation |
CDH is able to produce a sufficient amount of H2O2 to decolorize anthocyanins within 2 h |
| 1.1.99.29 | pyranose dehydrogenase (acceptor) |
degradation |
lignocellulose degradation |
| 1.10.3.2 | laccase |
degradation |
mineralization of organochlorine from toxic chlorophenols |
| 1.10.3.2 | laccase |
degradation |
enzyme shows dye-decolourizing activity against several anthraquinone dyes, azo dyes, polymeric dyes and others |
| 1.10.3.2 | laccase |
degradation |
use of enzyme in biodegradation of endocrine-disrupting chemicals such as bisphenol A and nonylphenol |
| 1.10.3.2 | laccase |
degradation |
use of enzyme to decolourize textile dye |
| 1.10.3.2 | laccase |
degradation |
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 |
degradation |
degradation of synthetic dyes from wastewater using biological treatment |
| 1.10.3.2 | laccase |
degradation |
eliminating toxic compounds (biogenic amines) present in fermented food and beverages |
| 1.10.3.2 | laccase |
degradation |
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatmen |
| 1.10.3.2 | laccase |
degradation |
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment |
| 1.10.3.2 | laccase |
degradation |
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 |
degradation |
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. The enzyme alone can decolourize 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 |
degradation |
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 |
degradation |
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 |
degradation |
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 |
degradation |
bisphenol A degradation |
| 1.10.3.2 | laccase |
degradation |
decolorization of industrial dyes. Evans blue decolorization and detoxification |
| 1.10.3.2 | laccase |
degradation |
degradation of endocrine disrupting compounds |
| 1.10.3.2 | laccase |
degradation |
degradation of lignin |
| 1.10.3.2 | laccase |
degradation |
deinking of old newspaper, indigo carmine decolorization |
| 1.11.1.10 | chloride peroxidase |
degradation |
rapid and efficient enzymatic decolorization of anthraquinone (alizarin red) and triphenylmethane dyes (crystal violet). The chromophoric groups are destructed and the dye molecules are broken-down into small pieces. The enzyme shows strong toleration to the typical salt species NaCl, NaNO3, and Na2SO4 |
| 1.11.1.13 | manganese peroxidase |
degradation |
biomimmetic decrosslinking with enzyme or metal complex-catalyzed reactions will enable the development of new devulcanizing strategies for the safe disposal and recycling of waste vulcanized rubber products |
| 1.11.1.13 | manganese peroxidase |
degradation |
lingnin-degrading enzymes possess oxidative activity against phenolic compoundss, which can be used for bioremediation, biobleaching, and biofuel production |
| 1.11.1.13 | manganese peroxidase |
degradation |
Mn peroxidases are of much interest biotechnologically because of their potentially applications in bioremdeial waste treatment and in catalyzing difficult chemical transfromations |
| 1.11.1.13 | manganese peroxidase |
degradation |
various aspects of the biotechnological uses of these fungi have been studied regarding the nonspecific ligninolytic system of white-red fungi such as the degradation of industrial textile dye effluents and various xenobiotics |
| 1.11.1.13 | manganese peroxidase |
degradation |
enzyme is able to detoxify aflatoxin B1. Maximum elimination of 86.0% of aflatoxin B1 is observed after 48 h in a reaction mixture containing 5 nkat of enzyme, and the addition of Tween 80 enhances elimination. The treatment of aflatoxin B1 by 20 nkat MnP reduces the mutagenic activity by 69.2%. Analysis suggests that aflatoxin B1 is first oxidized to aflatoxin B1-8,9-epoxide and then hydrolyzed to aflatoxin B1-8,9-dihydrodiol |
| 1.11.1.13 | manganese peroxidase |
degradation |
crude enzyme is able to degrade the antibiotics tetracycline and oxytetracycline. 72.5% of 50 mg/l of tetracycline and 84.3% of 50 mg/l oxytetracycline is degraded by 40 U/l of amnganese peroxidase, within 4 h. With the pH at 3.0-4.8, the temperature at 37-40°C, the Mn2+ concentration between 0.1 and 0.4 mM, the H2O2 concentration of 0.2 mM, and the enzyme-substrate ratio above 2.0 U/mg, the degradation rate reaches the highest |
| 1.11.1.13 | manganese peroxidase |
degradation |
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 |
| 1.11.1.14 | lignin peroxidase |
degradation |
degradation of different recalcitrant compounds, removal of toxic dyes |
| 1.11.1.14 | lignin peroxidase |
degradation |
the electroenzymatic method using in situ-generated hydrogen peroxide is effective for oxidation of veratryl alcohol by lignin peroxidase. The method may be easily applied to biodegradation systems |
| 1.11.1.14 | lignin peroxidase |
degradation |
enzyme shows marked dye-decolorization efficiency and stability toward denaturing, oxidizing, and bleaching agents, and compatibility with EcoVax and Dipex as laundry detergents for 48 h at 40°C |
| 1.11.1.14 | lignin peroxidase |
degradation |
LiPH8 showing high acid stability will be a crucial player in biomass valorization using selective depolymerization of lignin |
| 1.11.1.14 | lignin peroxidase |
degradation |
the enzyme can be used for PVC films biodegradation. Fungal metabolites are playing an immense role in developing various sustainable waste treatment processes. Production and characterization of a fungal lignin peroxidase with a potential to degrade polyvinyl chloride, method optimization, overview |
| 1.11.1.14 | lignin peroxidase |
degradation |
the partially purified LiP is able to degrade toxic synthetic polymer polyvinyl chloride (PVC) films, resulting in a 31% weight reduction of the films. LiP can effectively transform an endocrine disruptive hormone known as 17beta-estradiol (E2), which is considered a pollutant once released into the environment. Veratryl alcohol facilitates the enhanced removal and transformation of E2 by LiP and can perhaps also remove other closely related endocrine-disrupting impurities |
| 1.11.1.16 | versatile peroxidase |
degradation |
versatile peroxidase presents particular interest due to its catalytic versatility including the degradation of compounds that other peroxidases are not able to oxidize directly, versatile peroxidase versatility permits its application in Mn3+-mediated or Mn-independent reactions on both low and high redox-potential aromatic substrates and dyes, versatile peroxidase can be used to reoxidize Mn-containing polyoxometalates, which are efficient oxidizers in paper pulp delignification |
| 1.11.1.16 | versatile peroxidase |
degradation |
in presence of H2O2 and Mn2+, a cell-free subpernatant is capable to decolorize commercial azo dyes acid black 1 and reactive black 5, reaching efficiencies between 15 and 95%. For all assays performed with 33 microM Mn2+, the initial rate of the decolorization process is dependent on the dosage of H2O2 |
| 1.11.1.16 | versatile peroxidase |
degradation |
the allosteric behaviour of the VP enzyme promotes a high level of regulation of activity during the breakdown of model and industrial ligninolytic substrates, such as effluent from a pulp and paper plant, and fouled membrane solids extracted from a ground water treatment membrane |
| 1.11.1.19 | dye decolorizing peroxidase |
degradation |
DyP is a promising enzyme for the decolorizing treatment of dye-contaminated water |
| 1.11.1.19 | dye decolorizing peroxidase |
degradation |
degradation of lignin derivatives |
| 1.11.1.6 | catalase |
degradation |
application of KatA for elimination of H2O2 after cotton fabrics bleaching leads to less consumption of water, steam and electric power by 25%, 12% and 16.7% respectively without productivity and quality loss of cotton fabrics |
| 1.11.1.7 | peroxidase |
degradation |
enzyme can decolorize dyes, such as Aniline Blue, Reactive Black 5, and Reactive Blue 19 but not Congo Red |
| 1.13.11.1 | catechol 1,2-dioxygenase |
degradation |
because of broad spectrum of dioxygenases types that Stenotrophomonas maltophilia KB2 can exhibit, this strain appears to be very powerful and useful tool in the biotreatment of wastewaters and in soil decontamination |
| 1.13.11.15 | 3,4-dihydroxyphenylacetate 2,3-dioxygenase |
degradation |
comparison of binding sites and affinities using substrates chlorsulfon and metsulfuron-methyl. Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum and Arthrobacter globiformis are more effective in binding than catechol 2,3-dioxygenase from Pseudomonas putida. B. fuscum and A. globiformis have more potential than P. putida to remediate chlorsulfuron and metsulfuronmethyl |
| 1.13.11.2 | catechol 2,3-dioxygenase |
degradation |
because of broad spectrum of dioxygenases types that Stenotrophomonas maltophilia KB2 can exhibit, this strain appears to be very powerful and useful tool in the biotreatment of wastewaters and in soil decontamination |
| 1.13.11.2 | catechol 2,3-dioxygenase |
degradation |
the enzyme can be used for bioremediation of oil-polluted sites |
| 1.13.11.2 | catechol 2,3-dioxygenase |
degradation |
the enzyme can be used for the biodegradation of crude oil |
| 1.13.11.2 | catechol 2,3-dioxygenase |
degradation |
comparison of binding sites and affinities using substrates chlorsulfon and metsulfuron-methyl. Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum and Arthrobacter globiformis are more effective in binding than catechol 2,3-dioxygenase from Pseudomonas putida. B. fuscum and A. globiformis have more potential than P. putida to remediate chlorsulfuron and metsulfuronmethyl |
| 1.13.11.2 | catechol 2,3-dioxygenase |
degradation |
strain is able to degrade a solution containing benzene, toluene, ethylbenzene, and xylene at 7% NaCl (w/v) and pH 9 |
| 1.13.11.3 | protocatechuate 3,4-dioxygenase |
degradation |
because of broad spectrum of dioxygenases types that Stenotrophomonas maltophilia KB2 can exhibit, this strain appears to be very powerful and useful tool in the biotreatment of wastewaters and in soil decontamination |
| 1.13.11.37 | hydroxyquinol 1,2-dioxygenase |
degradation |
degradation of mixtures of phenolic compounds by Arthrobacter chlorophenolicus A6 |
| 1.13.11.37 | hydroxyquinol 1,2-dioxygenase |
degradation |
the highly purified Ar 1,2-HQD can be used as a key enzyme in the biodegradation of aromatic hydrocarbon contaminants |
| 1.13.11.39 | biphenyl-2,3-diol 1,2-dioxygenase |
degradation |
strain is able to degrade a solution containing benzene, toluene, ethylbenzene, and xylene at 7% NaCl (w/v) and pH 9 |
| 1.13.11.39 | biphenyl-2,3-diol 1,2-dioxygenase |
degradation |
the strain is able to completely degrade 280 microM of phenanthrene, 40% of 50 microM pyrene or 28% of 40 microM benzo[a]pyrene, each supplemented in M9 medium, within 7 days. The strain harbors genes which code for 2,3-dihydroxybiphenyl 1,2-dioxygenase (bphC), 4-nitrophenol 2-monooxygenase component B (npcB) as well as oxygenase component (nphA1), 4-hydroxybenzoate 3-monooxygenase (phbH), extradiol dioxygenase (edo), and naphthalene dioxygenase (ndo) |
| 1.13.11.39 | biphenyl-2,3-diol 1,2-dioxygenase |
degradation |
the strain is able to consume diphenyl ether and biphenyl from heat transfer fluid of thermo-solar plants (about 90% of total heat transfer fluid consumed after 1 day). The strain almost completely degrades 2,000 ppm heat transfer fluid after 5-day culture, and tolerates and grows in the presence of 150,000 ppm heat transfer fluid. When either biphenyl or diphenyl ether is used as sole carbon source, degradation is also effective |
| 1.13.11.55 | sulfur oxygenase/reductase |
degradation |
enzyme in the sulfur-oxidation pathway |
| 1.13.11.55 | sulfur oxygenase/reductase |
degradation |
initial enzyme in the sulfur-oxidation pathway |
| 1.13.11.56 | 1,2-dihydroxynaphthalene dioxygenase |
degradation |
the metabolic pathways of dibenzofuran and dibenzothiophene are controlled by naphthalene-degrading enzymes. Strain JB cannot grow on dibenzofuran or dibenzothiophen as the sole carbon source. 1,2-dihydroxynaphthalene dioxygenase may be responsible for the ring cleavage of 1,2-dihydroxydibenzofuran and 1,2-dihydroxydibenzothiophene to form 2-hydroxy-4-(3'-oxo-3'H-benzofuran-20-yliden)but-2-enoic acid and 4-[2-(3hydroxy)-thianaphthenyl]-2-oxo-3-butenoic acid |
| 1.13.11.87 | endo-cleaving rubber dioxygenase |
degradation |
enzyme exerts a synergistic effect on the efficiency of polyisoprene cleavage by rubber oxidase RoxA, EC 1.13.11.85 |
| 1.13.11.87 | endo-cleaving rubber dioxygenase |
degradation |
the enzyme has great potential for polyethylene and polypropylene degradation |
| 1.14.12.11 | toluene dioxygenase |
degradation |
stable isotopes could serve as a diagnostic for detecting aerobic biodegradation of TCE by toluene oxygenases at contaminated sites. There are no significant differences in fractionation among the enzymes toluene 3-monoxygenase, toluene 4-monooxygenase, and toluene 2,3-dioxygenase for compounds trichloroethene and cis-1,2-dichloroethene |
| 1.14.12.22 | carbazole 1,9a-dioxygenase |
degradation |
expression of genes CarAacd in dibenzothiophene degrader Rhodococcus erythropolis results in a strain capable of efficiently degrading dibenzothiophene and carbazole simultaneously. About 37% of the carbazole present, 0.8% by weight, is removed after treatment for 24 h.The recombinant strain can also degrade various alkylated derivatives of carbazole and dibenzothiophene in FS4800 crude oil by just a one-step bioprocess |
| 1.14.13.2 | 4-hydroxybenzoate 3-monooxygenase |
degradation |
in soil conditions, Phomopsis liquidambari effectively decomposes 99% of the available 4-hydroxybenzoic acid within 48 h. 4-Hydroxybenzoic acid hydroxylase activity is present in a high level early at 20 h, followed by 3,4-dihydroxybenzoic acid decarboxylase which reaches its highest relative activity at 24 h, and finally catechol 1,2-dioxygenase exhibits peak activity at 32 h |
| 1.14.13.20 | 2,4-dichlorophenol 6-monooxygenase |
degradation |
immobilized enzyme exhibits great potential for application in bioremediation |
| 1.14.13.227 | propane 2-monooxygenase |
degradation |
Rhodococcus sp. strain RHA1 can constitutively degrade N-nitrosodimethylamine. Activity toward this water contaminant is enhanced by approximately 500fold after growth on propane. Growth on propane elicits the upregulation of gene clusters associated with the oxidation of propane and the oxidation of substituted benzenes |
| 1.14.13.231 | tetracycline 11a-monooxygenase |
degradation |
addition of Escherichia coli overexpressing TetX to soil bacterial enrichment cultures along with varying levels of tetracycline affects community-wide tetracycline resistance levels. Soil microbial communities develop lower levels of tetracycline resistance upon exposure to 25 microg/ml of tetracycline when an Escherichia coli expressing TetX is present (6% of cultivable bacteria are resistant to 40 microg/ml tetracycline). In the absence of TetX activity, a similar tetracycline exposure selects for greater levels of resistant bacteria in the soil microbial community (90% of cultivable bacteria are resistant to 40 microg/ml tetracycline) |
| 1.14.13.243 | toluene 2-monooxygenase |
degradation |
coexpression of subunit TomA3 mutant V106A and an engineered epoxide hydrolase EchA from Agrobacterium radiobacter AD1, enhances the degradation of cis-dichloroethylene |
| 1.14.13.243 | toluene 2-monooxygenase |
degradation |
expression in Pseudomonas fluorescens for removal of trichloroethylene from soils. Closed microcosms containing the constitutive monooxygenase-expressing microorganism, soil, and wheat degrade an average of 63% of the initial trichloroethylene in 4 days (20.6 nmol of trichloroethylene/day and plant), compared to 9% of the initial trichloroethylene removed by microcosms containing wild-type Pseudomonas fluorescens 2-79 inoculated wheat, uninoculated wheat, or sterile soil |
| 1.14.13.244 | phenol 2-monooxygenase (NADH) |
degradation |
strain is able to degrade phenol at levels to 15 mM at a rate of 0.85 micromol/h |
| 1.14.13.25 | methane monooxygenase (soluble) |
degradation |
sMMO can be used for biodegradation of mixtures of chlorinated solvents, i.e., trichloroethylene, trans-dichloroethylene, and vinyl chloride. If the concentrations are increased to 0.1 mM, sMMO-expressing cells grow slower and degrade less of these pollutants in a shorter amount of time than pMMO |
| 1.14.13.50 | pentachlorophenol monooxygenase |
degradation |
pentachlorophenol is a chloroaromatic pesticide used to protect lumber, and an environmental pollutant, Sphingobium chlorophenolicum is a microorganism that can degrade the agent to 3-oxoadipate using 5 catalytic enzymes, pentachlorophenol 4-monooxygenase catalyzes the first and rate-limiting step |
| 1.14.13.7 | phenol 2-monooxygenase (NADPH) |
degradation |
phenol degradation, among kinetic parameters of growth, the maximum specific growth rate significantly affects the rate of contaminant degradation and is therefore an important parameter to characterise microbes in biological reatment systems |
| 1.14.15.26 | toluene methyl-monooxygenase |
degradation |
presence of chlorinated toluenes induces expression of enzymes of the xylene degradation sequence. Conjugative transfer of the TOL plasmid from Pseudomonas putida strain PaW1 to Pseudomonas sp. strain B13 and Pseudomonas cepacia strain JH230 allows the isolation of hybrid strains capable of growing in the presence of 3-chloro-, 4-chloro- and 3,5-dichlorotoluene |
| 1.14.15.3 | alkane 1-monooxygenase |
degradation |
formation of specific bacterial communities with reduced diversity after three week incubation of seawater with heptane, hexadecane, diesel fuel or crude oil. The isolates belong to well-known oil-degrading strains from the phyla Proteobacteria and Actinobacteria, whereas the genera Pseudomonas and Rhodococcus are represented with the biggest number of strains |
| 1.14.15.3 | alkane 1-monooxygenase |
degradation |
strain SJTD-1 efficiently mineralizes medium- and long-chain n-alkanes (C12-C30) as its sole carbon source within seven days, showing optimal growth on n-hexadecane, followed by n-octadecane, and n-eicosane. In 36 h, 500 mg/l of tetradecane, hexadecane, and octadecane are transformed completely; and 2 g/l n-hexadecane is degraded to undetectable levels within 72 h |
| 1.14.18.3 | methane monooxygenase (particulate) |
degradation |
pMMO can be used for biodegradation of mixtures of chlorinated solvents, i.e., trichloroethylene, trans-dichloroethylene, and vinyl chloride. If the concentrations are increased to 0.1 mM, pMMO-expressing cells grow faster and degrade more of these pollutants in a shorter amount of time than sMMO |
| 1.14.99.53 | lytic chitin monooxygenase |
degradation |
presence of lytic polysaccharide monooxygenase CBP21 facilitates the degradation of chitin substrates (colloidal chitin, beta-chitin, and alpha-chitin) by Chi92 |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
degradation |
design of dockerin-fused lytic polysaccharide monooxygenases. The resulting chimeras exhibit activity levels on microcrystalline cellulose similar to that of the wild-type enzymes. The dockerin moieties of the chimeras are functional and specifically bind to their corresponding cohesin partner. The chimeric lytic polysaccharide monooxygenases are able to self-assemble in designer cellulosomes alongside an endo- and an exo-cellulase also converted to the cellulosomal mode. The resulting complexes show a 1.7fold increase in the release of soluble sugars from cellulose, compared with the free enzymes, and a 2.6fold enhancement compared with free cellulases without lytic polysaccharide monooxygenase enhancement |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
degradation |
treatment with CelS2 reduces nonproductive binding of cellobiohydrolase onto cellulose surface |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
degradation |
cellulose conversion by cellobiohydrolase Cel7A from Trichoderma longibrachiatum alone is enhanced from 46 to 54% by the addition of isoform AA9A. Conversion by a mixture of Cel7A, endoglucanase, and beta-glucosidase is increased from 79 to 87% using pretreated bacterial microcrystalline cellulose with AA9A for 72 h. Individual AA9A molecules exhibit intermittent random movement along, across, and penetrating into the ribbon-like microfibril structure of bacterial microcrystalline cellulose, concomitant with the release of a small amount of oxidized sugars and the splitting of large cellulose ribbons into fibrils with smaller diameters |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
degradation |
in combination with endoglucanase and beta-glucosidase, Cel61A shows the ability to release more than 36% of the pretreated soy spent flake glucose |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
degradation |
in combination with endoglucanase and beta-glucosidase, Pte6 shows the ability to release more than 36% of the pretreated soy spent flake glucose |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
degradation |
in presence of a Trichoderma reesei CL847 cocktail composed of mainly cellulases and xylanases, a boost of glucose release from poplar and pine is observed upon addition of AA14B enzyme to the cocktail |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
degradation |
in presence of a Trichoderma reesei CL847 cocktail composed of mainly cellulases and xylanases, a boost of glucose release from poplar and pine is observed upon addition of AA14B enzyme to the cocktail. Addition of AA14A to a GH11 xylanase increases the release of xylooligomers from birchwood cellulosic fibers by 40% |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
degradation |
In the presence of an electron source, LPMO increases the activity of a commercial cellulase on filter paper, and the xylanase activity of xylanase Xyn10A on beechwood xylan. Mixtures of 60% Celluclast 1.5 L, 20% Xyn10A and 20% LPMO increase the total reducing sugar production from pretreated wheat straw by 54%, while the conversions of glucan to glucose and xylan to xylose are increased by 40 and 57%, respectively |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
degradation |
lytic polysaccharide monooxygenase is able to cleave cellulose acetates with a degree of acetylation of up to 1.4 |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
degradation |
oxidative activity of Cel61A displays a synergistic effect capable of boosting endoglucanase activity, and thereby substrate depolymerization of soy cellulose, by 27% |
