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 1.1.1.27 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 1.1.1.90 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 1.1.1.159 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 1.1.1.284 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 1.1.3.9 galactose oxidase degradation the enzyme can be used for oxygen removal 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 1.1.99.18 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 1.2.1.5 aldehyde dehydrogenase [NAD(P)+] degradation degradation of polyethylene glycols, PEGs 1.2.1.26 2,5-dioxovalerate dehydrogenase degradation involved in an alternative pathway of D-glucarate metabolism 1.2.1.28 benzaldehyde dehydrogenase (NAD+) degradation in cells of Acinetobacter sp. AG1 isolated from the River Elbe a combined action of benzylalcohol and benzaldehyde dehydrogenase induced after growth with benzylbenzoate does produce benzoate from benzylalcohol, which is a mechanism to quantitatively eliminate the anthropogenic marker compound benzylbenzoate under aerobic conditions 1.2.1.36 retinal dehydrogenase degradation ALDH1A1 appears to be the major if not the only enzyme responsible for the oxidation of 3-deoxyglucosone to 2-keto-3-deoxygluconate 1.2.1.36 retinal dehydrogenase degradation urinary excretion of 2-keto-3-deoxygluconate amounts to 16.7 micromol/g creatinine in humans, indicating that 3-deoxyglucosone may be quantitatively a more important substrate than retinaldehyde for ALDH1A1 1.2.1.46 formaldehyde dehydrogenase degradation physiological significance of dlFalDH in the formaldehyde metabolism in Hyphomicrobium zavarzinii ZV 580 cultured on C1 compounds 1.2.1.72 erythrose-4-phosphate dehydrogenase degradation coupling of a transketolase reaction (using Leishmania mexicana transketolase) that converts D-fructose 6-phosphate to D-erythrose 4-phosphate, which can then be converted to 4-phosphate D-erythronate using E4PD, whereby D-ribose 5-phosphate and D-glyceraldehyde 3-phosphate can both be used as ketol acceptor substrates in the reaction 1.2.3.1 aldehyde oxidase degradation aldehyde oxidase plays a critical role in nitrite reduction, and this process is regulated by pH, oxygen tension, nitrite, and reducing substrate concentrations 1.2.3.1 aldehyde oxidase degradation the enzyme plays a dual role in the metabolism of physiologically important endogenous compounds and the biotransformation of xenobiotics. Simple qualitative method using density functional theory to predict the product of aldehyde oxidase metabolism by examining the energetics of likely tetrahedral intermediates resulting from nucleophilic attack on carbon 1.2.7.6 glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) degradation Pyrobaculum aerophilum contains a modified Embden-Meyerhof pathway, in which GAPOR replaces the GAPDH/phosphoglycerate kinase couple of the conventional Embden–Meyerhof pathway 1.2.7.6 glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) degradation the major physiological role of GAPOR in Methanococcus maripaludis most likely involves only nonoptimal growth conditions 1.2.98.1 formaldehyde dismutase degradation resting Escherichia coli cells transformed with the formaldehyde dismutase gene degrade high concentrations of formaldehyde and produce formic acid and methanol that are molar equivalents of one-half of the degraded formaldehyde. The lyophilized cells of the recombinant Escherichia coli also degrade high concentrations of formaldehyde 1.3.3.6 acyl-CoA oxidase degradation ACO activity in Beauveria bassiana depends on the carbon source used for growth and the chain length of the substrate utilized for the oxidation reaction 1.4.1.2 glutamate dehydrogenase degradation at high salinity glutamate seems to be preferentially produced through the process catalyzed by NADH-GDH, whereas GS-catalysis might be the main glutamate synthesis pathway under low salinity 1.4.1.2 glutamate dehydrogenase degradation clarification of the in vivo direction of the reaction catalyzed by GDH isoenzyme 1, the enzyme catabolizes L-glutamate in roots, and does not assimilate NH4+ in source leaves 1.5.3.23 glyphosate oxidoreductase degradation in Ochrobactrum sp., glyphosate (3 mM) degradation is induced by phosphate starvation, and is completed within 60 h. The bacterium grows even in the presence of glyphosate concentrations as high as 200 mM 1.5.3.23 glyphosate oxidoreductase degradation inoculating glyphosate-treated soil samples with Pseudomonas sp. strains GA07, GA09 and GC04 results in a 2-3 times higher rate of glyphosate removal than that in non-inoculated soil. The degradation kinetics follows a first-order model. Glyphosate breakdown in strain GA09 is catalyzed both by C-P lyase and glyphosate oxidoreductase. Strains GA07 and GC04 degrade glyphosate only via glyphosate oxidoreductase, but no further metabolite is detected 1.5.3.23 glyphosate oxidoreductase degradation upon cultivation at initial pH 6.0, incubation temperature 35°C, glyphosate concentration 6 g/l, inoculation amount 5% and incubation time 5 days, strain CB4 utilizes 94.47% of glyphosate. The strain degrades glyphosate concentrations up to 12 g/l 1.6.2.4 NADPH-hemoprotein reductase degradation coexpression of CPR and P450 cytochromes CYP6AE14 or CYP9A12 of Helicoverpa armigera in Pichia pastoris. CYP6AE14 is not involved in gossipol degradation, but CYP9A12 takes part in gossipol metabolism 1.6.5.2 NAD(P)H dehydrogenase (quinone) degradation TcpB is acting as a quinone reductase for 6-chlorohydroxyquinone reduction during 2,4,6-trichlorophenol degradation, a toxic pollutant 1.7.1.B4 azobenzene reductase [NADH] degradation strain is able to decolorize azo dyes up to 1000 mg /l in 24 h under aerobic conditions. Cell extracts show NADH dependent oxygen-insensitive azoreductase activity 1.7.1.6 azobenzene reductase degradation potential for the treatment of azo dye contaminated wastewater 1.7.1.6 azobenzene reductase degradation expression of enzyme gene AzoA in Escherichia coli induces a higher rate of dye reduction with increases of 2fold for methyl red, 4fold for ponceau BS and 2.6fold for orange II compared to noninduced cells, respectively 1.7.1.6 azobenzene reductase degradation the optimum medium contains dye at 200 mg per l, 1.14 mM NADH, glucose at 2.07 g per l, and peptone at 6.44 g per l for the decolorization of Orange II up to 87% in 48 hr 1.7.1.14 nitric oxide reductase [NAD(P)+, nitrous oxide-forming] degradation p450nor gene is present in all fungal isolates analyzed that produce N2O from NO2, whereas nirK encoding the NO-forming NO2 reductase, is amplified in only 13 to 74% of the N2O-forming isolates 1.7.1.16 nitrobenzene nitroreductase degradation the strain can use nitrobenzene as the sole carbon and nitrogen source for growth, and completely degrade 300 mg nitrobenzene per litre within 14 h, at 20-35°C and pH 7.0-9.0. Strain 1 can also degrade aniline and phenol 1.7.2.4 nitrous-oxide reductase degradation plays a critical enviromental role in preventing release into the atmosphere of the potent greenhouse gas nitrous oxide 1.8.1.4 dihydrolipoyl dehydrogenase degradation conservation of the Cys-45 residue in human E3 is essential to the efficient catalytic function of the enzyme 1.8.1.4 dihydrolipoyl dehydrogenase degradation decreased activity of DLDH induced by valproic acid metabolites may, at least in part, account for the impaired rate of oxygen consumption and ATP synthesis in mitochondria if 2-oxoglutarate or glutamate are used as respiratory substrates, thus limiting the flux of these substrates through the citric acid cycle 1.8.1.4 dihydrolipoyl dehydrogenase degradation DLD is required for hamster acrosome reaction 1.8.1.4 dihydrolipoyl dehydrogenase degradation N286 and D320 play a role in the catalytic function of the E3 1.8.1.4 dihydrolipoyl dehydrogenase degradation S456 and E431 form a catalytic dyad in the DLD monomer, whereas H450, by forming a hydrogen bond with E431, may decrease the ability of E431 to polarize the hydroxyl group of S456 1.8.1.4 dihydrolipoyl dehydrogenase degradation shows flavin reductase activity with moderate diaphorase activity 1.8.1.4 dihydrolipoyl dehydrogenase degradation shows NADH-dependent tellurite reductase activity in vitro 1.8.1.4 dihydrolipoyl dehydrogenase degradation shows strong diaphorase activity 1.8.1.4 dihydrolipoyl dehydrogenase degradation T148 is not important to E3 catalytic function, whereas R281 plays a role in the catalytic function of E3 1.8.1.21 dissimilatory dimethyldisulfide reductase degradation application of strain in a two-stage biotrickling filter for simultaneous treatment of hydrogen sulfide, methanethiol, dimethyl sulfide and dimethyl disulfide. The first biofilter is inoculated with Acidithiobacillus thiooxidans and the second one with Thiobacillus thioparus. For separate feeds of reduced sulfur compounds, the elimination capacity order is dimethyl disulfide > dimethyl sulfide > methanethiol 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 1.11.1.6 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 1.11.1.10 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 1.13.11.1 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 1.13.11.2 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 1.13.11.15 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 1.13.11.37 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 1.14.13.7 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 1.14.13.20 2,4-dichlorophenol 6-monooxygenase degradation immobilized enzyme exhibits great potential for application in bioremediation 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 1.14.13.227 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 1.14.15.3 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 1.14.15.26 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 1.14.18.3 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% 1.14.99.54 lytic cellulose monooxygenase (C1-hydroxylating) degradation the intrinsic physicochemical characteristics of Kraft pulp fibers (e.g. cellulose accessibility/degree of polymerization/crystallinity/charge) are positively enhanced by the synergistic cooperation of endoglucanase, LPMO and xylanase. LPMO addition results in the oxidative cleavage of the pulps, increasing the negative charge on the cellulose fibers, although gross fiber properties (fiber length, width and morphology) are relatively unchanged. This improves cellulose nanofibrilliation while stabilizing the nanofibril suspension, without sacrificing nanocellulose thermostability 1.14.99.56 lytic cellulose monooxygenase (C4-dehydrogenating) degradation in combination with endoglucanase and beta-glucosidase, Cel61A shows the ability to release more than 36% of the pretreated soy spent flake glucose 1.14.99.56 lytic cellulose monooxygenase (C4-dehydrogenating) degradation in combination with endoglucanase and beta-glucosidase, Pte6 shows the ability to release more than 36% of the pretreated soy spent flake glucose 1.14.99.56 lytic cellulose monooxygenase (C4-dehydrogenating) degradation lytic polysaccharide monooxygenase is able to cleave cellulose acetates with a degree of acetylation of up to 1.4 1.14.99.56 lytic cellulose monooxygenase (C4-dehydrogenating) degradation oxidative activity of Cel61A displays a synergistic effect capable of boosting endoglucanase activity, and thereby substrate depolymerization of soy cellulose, by 27% 1.14.99.56 lytic cellulose monooxygenase (C4-dehydrogenating) degradation the intrinsic physicochemical characteristics of Kraft pulp fibers (e.g. cellulose accessibility/degree of polymerization/crystallinity/charge) are positively enhanced by the synergistic cooperation of endoglucanase, LPMO and xylanase. LPMO addition results in the oxidative cleavage of the pulps, increasing the negative charge on the cellulose fibers, although gross fiber properties (fiber length, width and morphology) are relatively unchanged. This improves cellulose nanofibrilliation while stabilizing the nanofibril suspension, without sacrificing nanocellulose thermostability 1.20.4.1 arsenate reductase (glutathione/glutaredoxin) degradation PvGrx5 has a role in regulating intracellular arsenite levels, by either directly or indirectly modulating the aquaglyceroporin 1.97.1.1 chlorate reductase degradation bacterial reduction of chlorate and perchlorate in water 1.97.1.1 chlorate reductase degradation (per)chlorate-reducing microorganisms are useful for bioremediation of soils and sediments 1.97.1.1 chlorate reductase degradation since the saturated hydrocarbon fraction is the most abundant in crude oil, its biodegradation is quantitatively most important in oil bioremediation 2.1.1.8 histamine N-methyltransferase degradation higher HMT activity seems to be linked to reduced histamine catabolism, percentage of catabolized histamine is not correlated to individual mannitol fluxes and appears to be independent of paracellular permeability 2.1.1.41 sterol 24-C-methyltransferase degradation active site of the yeast SMT has the necessary amino acids to generate products common to SMT catalysis of plants and protozoa, minor perturbations in the active site topography brought about by mutagenesis are sufficient to recognize new substrates 2.1.1.137 arsenite methyltransferase degradation Bacillus subtilis 168 expressing ArsM converts most of the inorganic As in the medium into dimethylarsenate and trimethylarsine oxide within 48 h and volatizes substantial amounts of dimethylarsine and trimethylarsine. The rate of As methylation and volatilization increases with temperature from 37 to 50°C. When inoculated into an As-contaminated organic manure composted at 50°C, the modified strain significantly enhances As volatilization 2.1.1.142 cycloartenol 24-C-methyltransferase degradation the amino acids of Region 1 provide a tight substrate orientation imposed by hydrophobic interactions between the sterol side chain and the SMT active site contacts and control the production and processing of the transmethylation pathways governed by the first and second C1-transfer activities 2.1.2.1 glycine hydroxymethyltransferase degradation essential for one-carbon metabolism 2.3.1.12 dihydrolipoyllysine-residue acetyltransferase degradation strain MM3 can grow on up to 250 microM pyrene in culture medium. With an initial cell density of 30000000 cells/ml, nearly 70% of 50 microM pyrene is degraded after 7 days of incubation. Nearly 20% increase in degradation of pyrene is observed with the use of 0.005% Tween 80. Dihydrolipoamide acetyltransferase accumulates during microalgal degradation of pyrene. The microalgal cells immobilized in calcium alginate completely degrade 50 microM of pyrene within 10 days in nonsterile soil slurry treated with 0.005% Tween 80 2.3.1.184 acyl-homoserine-lactone synthase degradation a significant positive correlation is observed between isoform LasI expression and polycyclic aromatic hydrocarbon degradation. Expression of isoform LasI increases with increase in biofilm growth, while the expression of isoform RhlI decreases during log phase of biofilm growth. Degradation of phenanthrene and pyrene by Pseudomonas aeruginosa N6P6 is affected by biofilm growth and LasI expression. The respective phenanthrene degradation for 15, 24, 48, and 72 h old biofilm after 7 days is 21.5, 54.2, 85.6, and 85.7%. The corresponding pyrene degradation is 15, 18.28, 47.56, and 46.48%, respectively, after 7 days 2.6.1.116 6-aminohexanoate aminotransferase degradation strain KI72 grows on a 6-aminohexanoate oligomer, a by-product of nylon-6 manufacturing, as a sole source of carbon and nitrogen 2.7.2.2 carbamate kinase degradation arginine is metabolized by the arginine deiminase pathway 3.1.1.1 carboxylesterase degradation use of enzyme in presence of oxime for detoxification of organophosphorous compounds 3.1.1.1 carboxylesterase degradation 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.B12 zearalenone hydrolase degradation effectively biological detoxification technology for ZEN degradation in agriculture and grain processing industry using enzyme ZHD. Biological detoxification of ZEN is more efficient, harmless, and specific compared to traditional methods 3.1.1.B12 zearalenone hydrolase degradation recombinant ZHD-P can be feasible for ZEN detoxification. The recombinant Escherichia coli cells expressing ZHD-P can be applied as a whole-cell biocatalyst for ZEN detoxification 3.1.1.B12 zearalenone hydrolase degradation zearalenone hydrolase (ZHD) is a lactone hydrolase with potential for the degradation of toxic and estrogenic zearalenone (ZEN). Importantly, ZHD does not damage cereal crops. ZHD catalyzes the cleavage of an ester bond in ZEN to form a non-toxic dihydroxyphenyl product with an open side chain with a subsequent loss of CO2, the product is non-estrogenic. Calculating the energy and electrostatic effects can provide a reference for the development of biodegradation technology in the field of environmental protection 3.1.1.20 tannase degradation TanSg1 is a tannase with potential industrial interest regarding the biodegradation of tannin waste or its bioconversion into biologically active products 3.1.1.32 phospholipase A1 degradation hydrolysis of nonpolar lipids, i.e. triacylglycerols, diacylglycerols and monoacylglycerols, when crude sunflower lecithin is treated with commercial product Lecitase VR Ultra. During the reaction, an acyl-migration phenomenon is observed. In 1 h of reaction the content of triacylglycerols decreases to 54%, while diacylglycerol and monoacylglycerol concentrations increase from 0.4 to 3.5 and from 1.9 to 6.5 g/100 g of crude lecithin, respectively. Along the reaction, different contents of glycerides can be achieved 3.1.1.42 chlorogenate hydrolase degradation use of yerba mate as source of chlorogenate and degradation by crude enzyme extract. Application to mass processing for a plant scale production of quinic acid 3.1.1.60 bis(2-ethylhexyl)phthalate esterase degradation di(2-ethylhexyl) phthalate, dibutyl phthalate, benzyl butyl phthalate and dipentyl phthalate can be almost completely degraded within four days in mineral salt medium under shaking conditions. 5.9% of the dimethyl phthalate and 42.9% of the diethyl phthalate present, are degraded under the same conditions. At temperatures of 10-50°C, strain B1811 is able to grow and utilize all the phthalate esters except for dimethylphthalate 3.1.1.60 bis(2-ethylhexyl)phthalate esterase degradation Fusarium culmorum degrades 95% of 1000 mg/l di(2-ethylhexyl) phthalate within 60 h of growth. Di(2-ethylhexyl) phthalate is fully metabolized wth butanediol as the final product 3.1.1.72 acetylxylan esterase degradation enzyme displays significant synergy with a xylanase, with a degree of synergy of 1.35 for the hydrolysis of delignified corn stover. Release of glucose is increased by 51% from delignified corn stover when 2 mg of a commercial cellulase is replaced by an equivalent amount of Axe 3.1.1.72 acetylxylan esterase degradation presence of the enzyme increases the activity of alpha-glucuronidases from families GH67 and GH115 on xylan by five and nine times, respectively 3.1.1.72 acetylxylan esterase degradation synergistic effect of AXE1 with xylanase on hemicellulose degradation. The amount of xylose released from acetylated birchwood xylan is increased by 1.4 fold when AXE1 is mixed with xylanase in a reaction cocktail 3.1.1.73 feruloyl esterase degradation capable of decolourising effluent from the paper industry, potential application in obtaining ferulic acid from agriculture waste materials produced by milling, brewing and sugar industries 3.1.1.73 feruloyl esterase degradation selective modification of xylans, degradation may be commercially important 3.1.1.73 feruloyl esterase degradation the esterase capable to release phenolic acids from intact polymers, degradation may be of interest for industries wishing to effect the controlled degradation of plant cell walls 3.1.1.73 feruloyl esterase degradation feruloyl esterase B is a tool for the release of phenolic compounds from agro-industrial by-products (coffe pulp, apple marc, wheat straw, sugar beet pulp and maite bran) 3.1.1.73 feruloyl esterase degradation feruloyl esterases A is a tool for the release of phenolic compounds from agro-industrial by-products (wheat straw, sugar beet pulp and maize bran) 3.1.1.73 feruloyl esterase degradation ferulic acid esterase activity in the enzymatic extracts of Aspergillus terreus grown on corn cob are higher than those after growth on vine trimming shoots. The enzymatic extracts produced on vine trimming shoots demonstrate a better performance for ferulic acid release from both corn cob (2.05 mg/g) and vine trimming shoots (0.19 mg/g), probably because of the higher xylanase/Fferulic acid esterase ratio determined in vine trimming extraxct 3.1.1.73 feruloyl esterase degradation maximum (76.8%) of total alkali-extractable ferulic acid is released from destarched wheat bran by the fungal enzyme system consisting of carboxymethyl cellulase, xylanase, beta-glucosidase, filter paper cellulase and ferulic acid esterase of Eupenicillium parvum 4-14 3.1.1.73 feruloyl esterase degradation the endo-1,4-xylanase XynC11 from Penicillium funiculosum (CAC15487)and the feruloyl esterase CE1 from Clostridium thermocellum effectively break down hemicellulose from pretreated sugarcane bagasse (up to 65%), along with the production of xylooligosaccharides GH11 and CE1 can improve biomasssaccharification by cellulases. Treatment with these two enzymes followed by a commercial cellulase cocktail increases saccharification of pretreated lignocellulose by 24% 3.1.1.73 feruloyl esterase degradation the hydrolysis of corn stalk and corncob by xylanase from Aspergillus niger can be significantly improved in concert with recombinant FaeA 3.1.1.73 feruloyl esterase degradation addition of a crude enzyme supernatant from high xylanase producing actinomycete strain Kitasatospora sp. ID06-480 and ethyl ferulate producing actinomycete strain Nonomuraea sp. ID06-094 to sugarcane bagasse hydrolysis with low-level loading of commercial enzyme Cellic® CTec2 enhances both the released amount of glucose and reducing sugars. High conversion yield of glucose from cellulose at 60.5% can be achieved after 72 h of saccharification 3.1.1.73 feruloyl esterase degradation low doses of enzyme (120 microg/g substrate) increases glucose yields released from corn stover, wheat bran, corn cob, and cassava stillage residues by 68.8%, 38.6%, 15.6%, and 20.0%, respectively 3.1.1.73 feruloyl esterase degradation enzyme acts synergistically with commercial xylanase by improving the release of xylooligosaccharides from wheat arabinoxylan 3.1.1.73 feruloyl esterase degradation overexpression in Hypocrea jecorina leads to a high level of feruloyl esterase produced under solid-state fermentation. The recombinant fungal enzyme system can release 52.2% of total ferulic acids from destarched wheat bran 3.1.1.73 feruloyl esterase degradation overexpression in Hypocrea jecorina leads to a high level of feruloyl esterase produced under solid-state fermentation. The recombinant fungal enzyme system can release 62.9% of total ferulic acids from destarched wheat bran 3.1.1.73 feruloyl esterase degradation presence of enzyme enhances the quantity of ferulic acid from destarched wheat bran in presence of xylanase 3.1.1.74 cutinase degradation efficient degradation of n-butyl benzyl phthalate by enzyme, degradation of 60% of initial amount within 7.5 h. Major product is 1,3-isobenzofurandione 3.1.1.74 cutinase degradation enzyme degrades 60% of initial 500 mg/l malathion within 0.5 h, major degradation product is malathion diacid 3.1.1.74 cutinase degradation enzyme shows significant degradation of dipropyl phthalate to non-toxic 1,3-isobenzofurandione, with 70% degradation of initial 500 mg/l within 2.5 h 3.1.1.74 cutinase degradation biotechnological applications of cutinases for synthetic polyester degradation 3.1.1.74 cutinase degradation enzyme decreases the turbidity of poly(methyl acrylate) and poly(ethyl acrylate) dispersions 3.1.1.74 cutinase degradation enzyme decreases the turbidity of poly(methyl acrylate) and poly(ethyl acrylate) dispersions. It favors the hydrolysis of poly(ethyl acrylate) over poly(methyl acrylate) 3.1.1.74 cutinase degradation enzyme is able to modify the surface of the polycaprolactone and polyethylene terephthalate synthetic polyesters 3.1.1.74 cutinase degradation enzyme shows an ink removal efficiency of 78.4% on laser-printed paper and 81.3% on newspaper at 30°C 3.1.1.74 cutinase degradation fusion of enzyme to the class II hydrophobins HFB4 and HFB7 or the pseudo-class I hydrophobin HFB9b. Upon fusion to HFB4 or HFB7, the hydrolysis of polyethylene terephthalate is enhanced over16fold over the level with the free enzyme 3.1.1.74 cutinase degradation surface hydrolysis of poly(ethylene terephthalate) fabric using recombinant cutinase. The optimal parameters are 40°C, pH 8, and 1.92 mg enzyme loading per gram of fabric 3.1.1.75 poly(3-hydroxybutyrate) depolymerase degradation development of biodegradable plastics such as poly(3-hydroxybutyrate) or poly(3-hydroxybutyrate-co-3-hydroxyvalerate) 3.1.1.75 poly(3-hydroxybutyrate) depolymerase degradation About 8.58 g/l (R)-3-hydroxybutanoate is obtained after 8 h of incubation using extracellular PHB. The optimal conditions are 50°C and pH 8. Presence of CaCO3 increases (R)-3-hydroxybutanoate yields to 23.97 g/l by stabilizing the pH of the reaction system 3.1.1.75 poly(3-hydroxybutyrate) depolymerase degradation strain is able to degrade polyhydroxybutanoate film provided as sole carbon source, and readily degrades both polyhydroxybutanoate film and polyhydroxybutanoate particles in agar suspensions 3.1.1.75 poly(3-hydroxybutyrate) depolymerase degradation strain is able to degrade polyhydroxybutanoate film provided as sole carbon source, even at pH 3.3-3.7, and readily degrades both polyhydroxybutanoate film and polyhydroxybutanoate particles in agar suspensions 3.1.1.75 poly(3-hydroxybutyrate) depolymerase degradation the enzyme shows high percentage of degradation with poly(3-hydroxybutanoate) films with pH 9 and at 40°C 3.1.1.75 poly(3-hydroxybutyrate) depolymerase degradation the extra-cellular fraction of Escherichia coli expressing PhaZ exhibits a high poly(3-hydroxybutanoate) degradation rate. It takes 35 h to completely degrade oly(3-hydroxybutanoate) films, while Caldimonas manganoxidans takes 81 h. The coexpression of putative periplasmic substrate binding protein ORFCma further improves the PHB degradation. The enzyme is also able to degrade poly(lactic acid) polycaprolactone, and poly(butylene succinate-co-adipate) 3.1.1.76 poly(3-hydroxyoctanoate) depolymerase degradation enzyme is able to degrade functionalized polyhydroxyalkanoate polymers containing thioester groups in the side chain, releasing functional thioester-based monomers and oligomers 3.1.1.88 pyrethroid hydrolase degradation 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 3.1.1.101 poly(ethylene terephthalate) hydrolase degradation a dual enzyme system consisting of the polyester hydrolase and the immobilized carboxylesterase TfCa from Thermobifida fusca KW3 can be employed for the hydrolysis of PET films at 60°C, resulting in an increased amount of soluble products with a lower proportion of mono-(2-hydroxyethyl)terephthalate in the presence of the immobilized TfCa 3.1.1.101 poly(ethylene terephthalate) hydrolase degradation a dual enzyme system consisting of the polyester hydrolase and the immobilized carboxylesterase TfCa from Thermobifida fusca KW3 can be employed for the hydrolysis of PET films at 60°C, resulting in an increased amount of soluble products with a lower proportion of mono-(2-hydroxyethyl)terephthalate in the presence of the immobilized TfCa. The dual enzyme system with LC-cutinase produces a 2.4fold higher amount of degradation products compared to Thermobifida fusca enzyme Cut2 after a reaction time of 24 h 3.1.1.101 poly(ethylene terephthalate) hydrolase degradation at 50°C, a maximum hydrolysis rate for poly(ethylene terephthalate) nanoparticles of 0.0033 per min is determined with 80 microg/ml of Tcur_1278. With 50 microg/ml of Tcur_1278, the hydrolysis rate increases 1.8fold at 55°C and 2.6fold at 60°C 3.1.1.101 poly(ethylene terephthalate) hydrolase degradation at 50°C, a maximum hydrolysis rate of poly(ethylene terephthalate) nanoparticles of 0.0059 per min is determined with 20 microg/ml of Tcur_0390 3.1.1.101 poly(ethylene terephthalate) hydrolase degradation biodegradability of PET is mainly influenced by the mobility of the polyester chains, which determine the affinity and accessibility of the ester bonds to the enzyme. The hydrolysis rates of enzymatic PET degradation are predominantly controlled by the efficient substrate adsorption rather than by the hydrolysis of the ester bonds. Nanoparticles prepared from PET samples of different crystallinity show a high proportion of amorphous domains and thus in the corresponding biodegradability 3.1.1.101 poly(ethylene terephthalate) hydrolase degradation enzyme shows good activity against commercial bottle-derived PET, which is highly crystallized and is was considerably active against PET film at low temperatures 3.1.1.101 poly(ethylene terephthalate) hydrolase degradation exchange of amino acid residues of TfCut2 involved in substrate binding with those present in LC-cutinase, UniProt ID G9BY57, from an uncultured bacterium, leads to enzyme variants with increased PET hydrolytic activity at 65°C. Variant causes a weight loss of PET films of more than 42% after 50 h of hydrolysis, corresponding to a 2.7fold increase compared to the wild type enzyme 3.1.1.101 poly(ethylene terephthalate) hydrolase degradation mutant D204C/E253C/D174R causes a weight loss of PET films of 25.0% at 70°C after a reaction time of 48 h, compared to 0.3% for wild-type 3.1.1.101 poly(ethylene terephthalate) hydrolase degradation the thermostability of the polyester hydrolase is sufficient to degrade semi-crystalline PET films at 65°C in the presence of 10 mM Ca2+ and 10 mM Mg2+ resulting in weight losses of up to 12.9% after a reaction time of 48 h 3.1.1.101 poly(ethylene terephthalate) hydrolase degradation 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 degradation bioconversion of plastics 3.1.1.101 poly(ethylene terephthalate) hydrolase degradation due to its low structural stability and solubility, it is difficult to apply standard laboratory-level Ideonella sakaiensis PETase expression and purification procedures in industry. To overcome this difficulty, the expression of IsPETase can be improved by using a secretion system. The extracellular enzyme is successfully produced using pET22b-SPMalE:IsPETase and pET22b-SPLamB:IsPETase expression systems. The secreted IsPETase has PET-degradation activity. The work will be used for development of a new Escherichia coli strain capable of degrading and assimilating PET in its culture medium 3.1.1.101 poly(ethylene terephthalate) hydrolase degradation enzymatic degradation of poly(ethylene terephthalate) (PET) is promising because this process is safer than conventional industrial approaches. Acceleration of enzymatic degradation of poly(ethylene terephthalate) is reached by surface coating with anionic surfactants 3.1.1.101 poly(ethylene terephthalate) hydrolase degradation 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 degradation the enzyme can offer an important contribution towards a future sustainable closed loop plastic recycling industry 3.1.1.101 poly(ethylene terephthalate) hydrolase degradation the enzyme is a potential tool to solve the issue of polyester plastic pollution 3.1.1.102 mono(ethylene terephthalate) hydrolase degradation enzyme shows good activity against commercial bottle-derived PET, which is highly crystallized and is considerably active against PET film at low temperatures 3.1.1.117 (4-O-methyl)-D-glucuronate---lignin esterase degradation fungal glucuronoyl esterases (FGEs) catalyze cleavage of the ester bond connecting a lignin alcohol to the xylan-bound 4-O-methyl-D-glucuronic acid of glucuronoxylans. Thus, FGEs are capable of degrading lignin-carbohydrate complexes and have potential for biotechnological applications toward woody biomass utilization 3.1.1.117 (4-O-methyl)-D-glucuronate---lignin esterase degradation Glucuronoyl esterases (GEs) catalyze the cleavage of ester linkages found between lignin and glucuronic acid moieties on glucuronoxylan in plant biomass. As such, GEs represent promising biochemical tools in industrial processing of these recalcitrant resources 3.1.2.20 acyl-CoA hydrolase degradation TEII can maintain effective polyketide biosynthesis by selectively removing the nonelongatable residues bound to acyl carrier proteins 3.1.8.1 aryldialkylphosphatase degradation the enzyme is used for the detoxification of organophosphate pesticides and realted chemical warfare agents such as VX and sarin 3.1.8.1 aryldialkylphosphatase degradation a series of substituted phenoxyalkyl pyridinium oximes enhance the degradation of surrogates of sarin (i.e. nitrophenyl isopropyl methylphosphonate, NIMP) and VX (i.e. nitrophenyl ethyl methylphosphonate, NEMP). Neither NIMP nor NEMP is hydrolyzed effectively by paraoxonase PON1 if one of these oximes is absent. In the presence of eight novel oximes, PON1-mediated degradation of both surrogates occurs 3.1.8.1 aryldialkylphosphatase degradation activity and stability of organophosphorus hydrolase are enhanced by interactions between the hydrophobic poly(propylene oxide) block of amphiphilic Pluronics and the enzyme. The strategy provides an efficient route to new formulations for decontaminating organophosphate neurotoxins 3.1.8.2 diisopropyl-fluorophosphatase degradation - 3.1.8.2 diisopropyl-fluorophosphatase degradation enzyme catalyse the hydrolysis of toxic organophosphorus cholinesterase-inhibiting compounds, including pesticides and chemical nerve agents 3.1.8.2 diisopropyl-fluorophosphatase degradation approach to the use of enzyme encapsulated within liposomes, to protect against and treat chemical poisoning 3.1.8.2 diisopropyl-fluorophosphatase degradation enzyme is capable of detoxifying chemical warfare agents by hydrolysis 3.1.8.2 diisopropyl-fluorophosphatase degradation use of enzyme for decomposition of soman in vitro 3.1.13.1 exoribonuclease II degradation RNA-binding domains of RNase II play a more important role in its exoribonuclease activity than they do in the activity of RNase R 3.1.21.1 deoxyribonuclease I degradation treatment of established 72 h biofilms with 100 microg per ml of DNase for 24 h induces incomplete Listeria monocytogenes biofilm dispersal, with about 25% biofilm remaining compared to control. Addition of proteinase K completely inhibits biofilm formation, and 72 h biofilms including those grown under stimulatory conditions are completely dispersed with 100 microg per ml proteinase K 3.1.21.1 deoxyribonuclease I degradation the degradation of extracellular DNA with enzymes such as DNase I is a rapid method to remove Campylobacter jejuni biofilms, and is likely to potentiate the activity of antimicrobial treatments and thus synergistically aid disinfection treatments 3.2.1.4 cellulase degradation cellulase is an industrially important enzyme for biomass saccharification at high temperature. beta-Glucan can be completely degraded to glucose at high temperature with a combination of the hyperthermophile Pyrococcus furiosus endocellulase (EGPf) and beta-glucosidase (BGLPf). beta-Glucans are polysaccharides of D-glucose monomers formed by beta(1->3),(1->4) mixed-linkage bonds. They occur most commonly as cellulose in plants, in the bran of cereal grains, the cell wall of baker's yeast, and in certain fungi, mushrooms, and bacteria 3.2.1.4 cellulase degradation a statistical optimization approach involving Plackett-Burman design and response surface methodology on submerged fermentation using cane molasses medium results in the production of 72410, 36420, 32420 and 5180 U/l of xylanase, endo-beta-1,4-glucanase, exo-beta-1,4-glucanase, and beta-glucosidase, respectively, i.e. more than fourfold improvements in production of xylanolytic and cellulolytic enzymes. Addition of microparticles engineers fungal morphology and enhances enzymes production. Maximum sugar yield of 578.12 and 421.79 mg/g substrate for waste tea cup and rice straw, respectively, are achieved after 24 h 3.2.1.4 cellulase degradation addition of Eg5A to cellobiase (i.e. cellobiohydrolase and beta-glucosidase) results in a 53% increasing saccharification of NaOH-pretreated barley straw, and the glucose release is 47% higher than with cellobiase treatment alone 3.2.1.4 cellulase degradation addition of isoform Eg5A to cellobiase (cellobiohydrolase and beta-glucosidase) results in a 53% increasing saccharification of NaOH-pretreated barley straw, whereas the glucose release is 47% higher than that cellobiase treatment alone 3.2.1.4 cellulase degradation after hydrolysis and fermentation of wheat straw a significant amount of active enzymes can be recovered by recycling the liquid phase. In the early stage of the process, enzyme adsorbs to the substrate, then gradually returning to the solution as the saccharification proceeds. The hydrolysis yield and enzyme recycling efficiency in consecutive recycling rounds can be increased by using high enzyme loadings and moderate temperatures. The amount of enzymes in the liquid phase increases with its thermostability and hydrolytic efficiency 3.2.1.4 cellulase degradation bioethanol production by Aspergillus fumigatus JCF at optimised growth conditions and Saccharomyces cerevisiae for simultaneous saccharification and fermentation. Using cotton seed as the substrate, maximum bioethanol concentration of 6.7 g/l can be achieved 3.2.1.4 cellulase degradation cellulase complex containing cellulolytic enzymes,endoglucanase CelE, EC 3.2.1.4, and beta-glucosidase BglA, EC 3.2.1.21, to completely degrade cellulose to glucose. The cellulases are displayed on the cell surface of Corynebacterium glutamicum by using themechanosensitive channel to anchor enzymes in the cytoplasmic membrane. The displayed cellulases complexes have a synergic effect on the direct conversion of biomass to reducing sugars leading to 3.1- to 6.0fold increase compared to the conversion by the secreted cellulases complexes. The displayed cellulases complexes increase the residual activities of cCelEand cBglA at 70°C from 28.3% and 24.3% in the secreted form to 65.1% and 82.8%, respectively 3.2.1.4 cellulase degradation during cultivation, consortium SV79 produces the maximum filter paper activity (FPase, 9.41 U/ml), carboxymethylcellulase activity (CMCase, 6.35 U/ml), and xylanase activity (4.28 U/ml) with sugarcane bagasse, spent mushroom substrate, and Sorbus anglica, respectively. The ethanol production using Miscanthus floridulus as substrate is up to 2.63 mM ethanol/g 3.2.1.4 cellulase degradation effect of nickel-cobaltite (NiCo2O4) nanoparticles on production and thermostability of the cellulase enzyme system. Maximum production of endoglucanase (211 IU/gds), beta-glucosidase (301 IU/gds), and xylanase (803 IU/gds) is achieved after 72 h without nanoparticles, while in the presence of 1 mM of nanoparticles, endoglucanase, beta-glucosidase, and xylanase activity increase by about 49, 53, and 19.8%, respectively, after 48 h of incubation. Crude enzyme is thermally stable for 7 h at 80°C in presence of nanoparticles, as against 4 h at the same temperature for control samples 3.2.1.4 cellulase degradation effects of microalgal biomass particle on the degree of enzymatic hydrolysis and bioethanol production by single enzyme hydrolysis (cellulase) and double enzyme hydrolysis (cellulase and cellobiase). The glucose yield from biomass in the smallest particle size range examined, i.e. 35 microm to 90 microm, is the highest, 134.73 mg glucose/g algae, while the yield from biomass in the larger particle size range from 295 microm to 425 microm is 75.45mg glucose/g algae. A similar trend is observed for bioethanol yield, with the highest yield of 0.47 g EtOH/g glucose obtained from biomass in the smallest particle size range 3.2.1.4 cellulase degradation enzyme extracts obtained from growing Acrophialophora nainiana on cellulose, dirty-cotton residue, sugarcane bagasse and banana stem can be used in the hydrolysis of sugarcane bagasse, untreated, pre-treated by steam explosion and pretreated by acid-catalysed steam explosion. The carbohydrase activity profile of the enzyme preparations varies significantly with the used carbon source. The highest enzyme activities, especially total cellulase (0.0132 IU) and xylanase (0.0774 IU) activities, are obtained with banana stem as the carbon source. On sugarcane bagasse, total cellulase activity on filter paper and pectinase activities are predominant. The exocellulase/endocellulase activity ratio (FPAsol/FPAinsol) of the cellulases produced varies between 1 and 4 depending on the substrate. The highest endocellulase activity (FPAinsol) content is obtained when grown on sugarcane bagasse 3.2.1.4 cellulase degradation hydrolysis of 2% carboxymethyl cellulose with purified enzyme at its optimum temperature and pH results in complete hydrolysis within 2 h yielding 18% cellotriose, 72% cellobiose and 10% glucose 3.2.1.4 cellulase degradation immobilization of enzyme on functionalized magnetic silica nanospheres using glutaraldehyde. Immobilized cellulase exhibits better resistance to high temperature and pH inactivation in comparison to free cellulase. Use of cross-linking agent leads to a greater amount of immobilized cellulase and better operational stability. The amount of immobilized cellulase with the cross-linking agent is 92 mg/g support. The activity of the immobilized cellulase is still 85.5% of the initial activity after 10 continuous uses 3.2.1.4 cellulase degradation mixtures of beta-xylosidase, xylanase, beta-glucosidase, and cellulase isolated from the metagenomic library of a long-term dry thermophilic methanogenic digester community retain high residual synergistic activities after incubation with cellulose, xylan, and steam-exploded corncob at 50°C for 72 h. About 55% dry weight of steam-exploded corncob is hydrolyzed to glucose and xylose by the synergistic action of the four enzymes at 50°C for 48 h 3.2.1.4 cellulase degradation preparation of functionalized magnetic nanospheres by co-condensation of tetraethylorthosilicate with aminosilanes 3-(2-aminoethylaminopropyl)-triethoxysilane (AEAPTES), 3-(2-aminoethy-laminopropyl)-trimethoxysilane (AEAPTMES) and 3-aminopropyltriethoxysilane (APTES) and use as supports for immobilization of cellulase. The magnetic nanospheres with core-shell morphologies exhibit higher capacity for cellulase immobilization than unfunctionalized magnetic nanospheres. AEAPTMES with methoxy groups is favored to be hydrolyzed and grafted on unfunctionalized magnetic nanospheres. AEAPTMES functionalized magnetic nanospheres with the highest zeta-potential (29 mV) exhibit 87% activity recovery, and the maximum amount of immobilized cellulase is112 mg/g support at concentration of initial cellulase of 8 mg/ml. Immobilized cellulase on AEAPTMES functionalized magnetic nanospheres has higher temperature stability and broader pH stability than other immobilized cellulases and free cellulase 3.2.1.4 cellulase degradation pretreatment method for lignocellulosic wheat straw to depolymerize lignin and expose the cellulose polymers to produce bioethanol. Wheat straw is pretreated with ligninolytic enzymes extract produced from Ganoderma lucidum under optimum solid state fermentation conditions. The pretreated biomass was further subjected to the enzymatic hydrolysis by crude unprocessed cellulases (beta-1,4-endoglucanase, 53.5 U/ml, beta-1,4-exoglucanase, 41.3 U/ml, beta-1,4-glucosidase, 46.8 U/ml, and xylanase 39 U/ml) produced by Trichoderma harzaianum. Under optimal conditions for enzymatic saccharification, 10% (w/v) of pretreated biomass is hydrolyzed completely and converted to 72.5 and 2.4 g/l of glucose and xylose, respectively 3.2.1.4 cellulase degradation saccharification of pretreated dry potato peels, carrot peels, composite waste mixture, orange peels, onion peels, banana peels, pineapple peels by crude enzyme extract from Aspergillus niger NS-2 results in cellulose conversion efficiencies of 92–98% 3.2.1.4 cellulase degradation the purified enzyme decreases the viscosity of carboxymethyl cellulose when assessed at 70-85°C and is capable of releasing reducing sugars from acid-pretreated straw at 70 and 75°C 3.2.1.4 cellulase degradation Trichoderma reesei NRRL-6156 filter paper exocellulase and endocellulase hydrolysis of sugarcane bagasse, results in 224.0 and 229 gram of total reducing sugar per kilogram of dry bagasse at 43.4°C and a concentration of enzymatic extract of 18.6% in water and ultrasound baths, respectively. The yields obtained are comparable to commercial enzymes 3.2.1.4 cellulase degradation under simulated mashing conditions, addition of 60 U Egl5A reduces more viscosity (10.0 vs.7.6%) than 80 U of Ultraflo XL from Novozymes 3.2.1.4 cellulase degradation under simulated mashing conditions, addition of Cel7A (99 microg) reduces the mash viscosity by 9.1% and filtration time by 24.6% 3.2.1.4 cellulase degradation use of amine-functionalized cobalt ferrite (AF-CoFe2O4) magnetic nanoparticles for immobilization of cellulase. Particles show a mean diameter of about 8 nm and remain distinct with no significant change in size after binding with cellulase. The immobilized cellulase has higher thermal stability than free cellulase and shows good reusability after recovery 3.2.1.4 cellulase degradation use of mutant T57N/E53D/S79P/T80E/V101I/S133R/N155E/G189S/F191V/T233V/G239E/V265T/D271Y/G293A7S309W/S318P and previously engineered highly active, thermostable variants of the fungal cellobiohydrolases Cel6A and Cel7A to hydrolyzes cellulose synergistically at an optimum temperature of 70°C over 60 h.The thermostable mixture produces three times as much total sugar as the best mixture of the wild type enzymes operating at their optimum temperature of 60°C 3.2.1.4 cellulase degradation a fungal consortium of Aspergillus nidulans, Mycothermus thermophilus, and Humicola sp. composts a mixture (1:1) of silica rich paddy straw and lignin rich soybean trash during summer period in North India, results in a product with C:N ratio 9.5:1, available phosphorus 0.042% and fungal biomass 6.512 mg of N-acetyl glucosamine/100 mg of compost. A C:N ratio of 10.2:1 and highest humus content of 3.3% is achieved with 1:1 mixture of paddy straw and soybean trash. The consortium shows showed high cellobiase, carboxymethyl cellulase, xylanase, and FPase activities 3.2.1.4 cellulase degradation addition of recombinant Eg5A to cellobiase (cellobiohydrolase and beta-glucosidase) results in a 53% increase in saccharification of NaOH-pretreated barley straw, whereas the glucose release is 47% higher than with cellobiase treatment alone 3.2.1.4 cellulase degradation cellulase enzyme filtrate from Chaetomium thermophile saccharifies 5% kallar grass straw to 69% reducing sugars (quantitatively) at 50°C. Glucose concentration in the hydrolysates from different fungi is in the decreasing order of Chaetomium thermophile > Trichoderma reesei > Sporotrichum thermophile > Aspergillus fumigatus > Torula thermophila > Humicola grisea > Malbranchea pulchella. At 60°C, thermostable enzymes hydrolyse kallar grass straw at a maximum rate for the initial 20 h 3.2.1.4 cellulase degradation comparison of endoglucanases able to rapidly reduce the viscosity of 15% (w/w, dry matter) hydrothermally pretreated wheat straw. Based on temperature profiling studies, Thermoascus aurantiacus EGII/Cel5A is the most promising enzyme for biomass liquefaction 3.2.1.4 cellulase degradation crude cellulase efficiently hydrolyzes office waste paper, algal pulp (Gracillaria verulosa), and biologically treated wheat straw at 60°C with sugar release of about 830 mg/ml, 285 mg/g, and 260 mg/g of the substrate, respectively 3.2.1.4 cellulase degradation crude thermostable cellulases and xylanase hydrolyze phosphoric acid-swollen wheat straw, avicel and untreated xylan up to 74, 71 and 90 %, respectively 3.2.1.4 cellulase degradation Freeze-dried enzyme of Trichoderma reesei, even at higher enzyme concentration results in 60% reducing sugars yield (quantitatively) at 50°C. Glucose concentration in the hydrolysates from different fungi is in the decreasing order of Chaetomium thermophile > Trichoderma reesei > Sporotrichum thermophile > Aspergillus fumigatus > Torula thermophila > Humicola grisea > Malbranchea pulchella. At 60°C, thermostable enzymes hydrolyse kallar grass straw at a maximum rate for the initial 20 h 3.2.1.4 cellulase degradation hydrolysis of pretreated Alfa fibers (Stipa tenacissima) by beta-D-glucosidase and xylanase, produced by a solid state fermentation process of wheat bran supplemented with lactose. The maximum saccharification yield of 83.23% is achieved under substrate concentration 3.7% (w/v), time 144 h and enzyme loading of 0.8 FPU, 15 U CMCase, 60 U beta-D-glucosidase and 125 U xylanase 3.2.1.4 cellulase degradation oligosaccharides with degree of polymerization 2-10 are formed by hydrolysis of beta-glucan. The recombinant enzyme preparations are fast and effective in decreasing the reduced viscosity of wholegrain barley extract than some commercial enzyme preparations 3.2.1.4 cellulase degradation scale-up systems for cellulase production and enzymatic hydrolysis of pretreated rice straw at highsolid loadings and by Aspergillus terreus. In a horizontal rotary drum reactor at 50°C with 25 % (w/v) solid loading and 9 FPU/g substrate enzyme load up to 20 % highly concentrated fermentable sugars are obtained at 40 h with an increased saccharification efficiency of 76 % compared to laboratory findings (69.2 %). Nearly 79-84% of the cellulases and more than 90% of the sugars are recovered from the saccharification mixture 3.2.1.4 cellulase degradation use of lucerne fibre as a cellulase-recycling vehicle during bioconversion processes. Adsorption of cellulase complexes is minimal at the pH optimum, 5.0, for fibre conversion to soluble sugars. Lowering of incubation temperature to 3°C enhances adsorption of fungal cellulases. The adsorptive capacity can be improved about 30% by raising the pH above the hydrolysis optimum during the recycling phase 3.2.1.4 cellulase degradation use of lucerne fibre as a cellulase-recycling vehicle during bioconversion processes. Adsorption of cellulase complexes is minimal at the pH optimum, 6.2, for fibre conversion to soluble sugars. Lowering of incubation temperature to 3°C enhances adsorption of fungal cellulases. The adsorptive capacity can be improved about 30% by raising the pH above the hydrolysis optimum during the recycling phase 3.2.1.4 cellulase degradation use to release dye in neutral pH conditions from indigo-dyed cotton-containing fabric in biostoning applications 3.2.1.4 cellulase degradation using enzymatic extract from M. thermophila JCP 1-4 to saccharify sugarcane bagasse pretreated with microwaves and glycerol, glucose and xylose yields obtained are 15.6% and 35.13% (2.2 g/l and 1.95 g/l), respectively 3.2.1.4 cellulase degradation addition of Cel9K to a commercial enzyme set (Celluclast 1.5L + Novozym 188) increases the saccharification of the pretreated reed and rice straw powders by 30.4% and 15.9%, respectively 3.2.1.4 cellulase degradation enzyme releases high amounts of reducing sugars from wheat bran and corn cobs, being a useful biocatalyst for producing bioethanol and fine chemicals from agroresidues 3.2.1.4 cellulase degradation replacement of carbohydrate-binding module by modules from enzymes with different specificities leads to enhanced activity that is affected by carbohydrate-binding module binding specificity, e.g. on ball-milled cellulose or avicel. The chimeric enzymes can efficiently degrade milled lignocellulosic materials, such as corn hulls 3.2.1.4 cellulase degradation under acidic conditions at 50°C, the enzyme is effective in digesting the green algae Ulva pertusa 3.2.1.6 endo-1,3(4)-beta-glucanase degradation oligosaccharides with degree of polymerization 2-10 are formed by hydrolysis of beta-glucan and laminarin. The recombinant enzyme preparations are fast and effective in decreasing the reduced viscosity of wholegrain barley extract than some commercial enzyme preparations 3.2.1.8 endo-1,4-beta-xylanase degradation the substrate binding site of Xyn11A probably contains six subsites. Aromatic residues Tyr165, Trp9, Tyr69, Tyr80, Tyr65, Tyr88 and Tyr173 play an important role in the six subsites of Xyn11A 3.2.1.8 endo-1,4-beta-xylanase degradation enzyme is able to degrade pulp and release substantial chromophoric materials and lignin derived compounds indicating its effective utility in pulp bleaching 3.2.1.8 endo-1,4-beta-xylanase degradation Abf51A shows greater synergistic effect in combination with xylanase (2.92fold) on wheat arabinoxylan degradation than other reported enzymes, the amounts of arabinose, xylose, and xylobiose are all increased in comparison to that by the enzymes acting individually 3.2.1.8 endo-1,4-beta-xylanase degradation agroresidues subjected to alkali and microwave irradiation for 6 min in order to expose the polysaccharide component to enzymatic hydrolysis lead to increased relase of sugars. The maximum sugar content is detected in the hydrolysate of microwave-irradiated wheat bran (6.20 mg/g substrate) followed by wheat straw (4.9 mg/g substrate) 3.2.1.8 endo-1,4-beta-xylanase degradation co-immobilization of xylanase, beta-xylosidase and alpha-L-arabinofuranosidase from Penicillium janczewskii on a single support leads to a functional multi-enzymatic biocatalyst acting in the complete hydrolysis of different and complex substrates such as oat spelt and wheat arabinoxylans, with xylose yield higher than 40%. The xylanase and the alpha-L-arabinofuranosidase present high stability retaining 86.6 and 88.0% of activity after 10 reuse cycles 3.2.1.8 endo-1,4-beta-xylanase degradation during degradation of bagasse, hemicellulose content, especially arabinan, and the cellulose crystallinity of bagasse affects the synergism of degrading enzymes cellulase and xylanase. Higher synergism (above 3.4) is observed for glucan conversion, at low levels of arabinan (0.9%), during the hydrolysis of peracetic acid pretreated bagasse. In contrast, 1-ethyl-3-methylimidazolium acetate pretreated bagasse shows lower cellulose crystallinity and achieves higher synergism (over 1.9) for xylan conversion. The combination of Thermobidfida endoglucanase Cel6A and xylanase Xyn11A results in higher synergism for glucan conversion than the combination of Cel6A with Clostridium thermocellum XynZ-C 3.2.1.8 endo-1,4-beta-xylanase degradation hydrolysis of insoluble wheat arabinoxylan using different endoxylanases in combination with arabinofuranosidase Araf51A. The optimized combination is endoxylanases XynZ/Xyn11A/Araf51A with a loading ratio of 2:2:1, and the value of degree of synergy increases with the increase of Araf51A proportion in the enzyme mixture. Both free and enzymes immobilizedon commercial magnetic nanoparticles show a similar conversion to reducing sugars after hydrolysis for 48 h. After 10 cycles, approximately 20% of the initial enzymatic activity of both the individual or mixture of immobilized enzymes is retained, with 5.5fold increase in the production of sugars. A sustainable synergism between immobilized arabinofuranosidase and immobilized endoxylanases in the hydrolysis of arabinoxylan is observed 3.2.1.8 endo-1,4-beta-xylanase degradation immobilization of enzyme within calcium alginate beads using entrapment technique. Temperature (50°C) and pH (7.0) optima of immobilized enzyme remain same, but enzyme-substrate reaction time increases from 5.0 to 30.0 min as compared to free enzyme. The diffusion limit of high molecular weight xylan (corncob) causes a decline in Vmax of immobilized enzyme from 4773 to 203.7 U/min, whereas the Km value increases from 0.5074 to 0.5722 mg/ml. Immobilized endo-beta-1,4-xylanase is stable even at high temperatures and retains 18 and 9% residual activity at 70°C and 80°C, respectively. The immobilized enzyme also exhibits sufficient recycling efficiency up to five reaction cycles 3.2.1.8 endo-1,4-beta-xylanase degradation immobilizazion of enzyme on various supports. Most active immobilized enzyme is achieved when Xyl2 is covalently bound to low functionalized agarose matrices, poorer activity is observed for Xyl2 immobilized on highly functionalized agarose or on nickel-affinity resin 3.2.1.8 endo-1,4-beta-xylanase degradation pretreatments with alkali or acid significantly increase the relative release of pentose sugars, especially in alkali-pretreated canola meal (about 44%) and mustard bran (about 72%). The amounts of pentosan (g/100 g) in acid- and alkali-pretreated canola meal are 7.50 and 8.21 and in corresponding mustard bran are 8.67 and 10.39, respectively. These pretreated substrates produced a pentose content (g/100 g) of 2.10 in 18 h and 2.95 in 24 h, respectively, during hydrolysis. The main oligosaccharides in the hydrolyzates of alkali-pretreated substrates are xylo-glucuronic acid and xylobiose 3.2.1.8 endo-1,4-beta-xylanase degradation the combination of Axy43A and Paenibacillus curdlanolyticus B-6 endo-xylanase Xyn10C greatly improves the efficiency of xylose and arabinose production from the highly substituted rye arabinoxylan 3.2.1.8 endo-1,4-beta-xylanase degradation a fungal consortium of Aspergillus nidulans, Mycothermus thermophilus, and Humicola sp. composts a mixture (1:1) of silica rich paddy straw and lignin rich soybean trash during summer period in North India, results in a product with C:N ratio 9.5:1, available phosphorus 0.042% and fungal biomass 6.512 mg of N-acetyl glucosamine/100 mg of compost. A C:N ratio of 10.2:1 and highest humus content of 3.3% is achieved with 1:1 mixture of paddy straw and soybean trash. The consortium shows high cellobiase, carboxymethyl cellulase, xylanase, and FPase activities 3.2.1.8 endo-1,4-beta-xylanase degradation crude thermostable cellulases and xylanase hydrolyze phosphoric acid-swollen wheat straw, avicel and untreated xylan up to 74, 71 and 90 %, respectively 3.2.1.8 endo-1,4-beta-xylanase degradation degradation of alpha-amylase-treated wheat bran by xylanase solubilises about 20% of the fibre residue, i.e. 10% of the original bran. Amylase, protease and xylanase treatments alter the composition of the original bran, removing starch (100%), a portion of the non-starch glucan (39%), xylan (57%), arabinan (61%), ash (62%) and other components including protein (52%). Pre-extraction of enzymatically-hydrolysable starch and xylan reduces the release of furfural. Steam explosion of the lignocellulosic residue followed by cellulase treatment and conversion to ethanol at a high substrate concentration (19%) gives an ethanol titre ofabout 25 g/l or a yield of 93% of the theoretical maximum 3.2.1.8 endo-1,4-beta-xylanase degradation enzymatic treatment of kraft pulp with xylanase and laccase decreases the amount of chlorine needed for bleaching. Pretreatment of pulp followed by a chemical treatment with 3% NaOCl gives the same results as with chemicals at 7% NaOCl, resulting in 42% reduction in chlorine consumption 3.2.1.8 endo-1,4-beta-xylanase degradation hydrolysis of pretreated Alfa fibers (Stipa tenacissima) by beta-D-glucosidase and xylanase, produced by a solid state fermentation process of wheat bran supplemented with lactose. The maximum saccharification yield of 83.23% is achieved under substrate concentration 3.7% (w/v), time 144 h and enzyme loading of 0.8 FPU, 15 U CMCase, 60 U beta-D-glucosidase and 125 U xylanase 3.2.1.8 endo-1,4-beta-xylanase degradation maximum saccharification is obtained from treatment of cane bagasse by partially purified xylanase from Thermomyces lanuginosus A72 and Thermomyces lanuginosus YMN72 after 24 hrs of incubation. The maximum production of ethanol and xylitol is obtained after 48 and 24 h fermentation giving 22.48 g/l and 13.54 g/l, respectively, in enzyme broth of Thermomyces lanuginosus YMN72 using Candida tropicalis EMCC2 3.2.1.8 endo-1,4-beta-xylanase degradation optimization of xylanase production using agro-industrial substrates. Pretreated rice straw yields 126.9 mg/g maximum fermentable sugars 3.2.1.8 endo-1,4-beta-xylanase degradation treatment of Eucalyptus kraft pulp with culture supernatant at 10 IU per gram pulp to enhance bleaching of kraft pulp results in a 10.5% reduction in Kappa number (indicating the amount of chemicals needed for bleaching pulps) and has a positive effect on the brightness of the resulting handsheets 3.2.1.8 endo-1,4-beta-xylanase degradation using enzymatic extract from Myceliophthora thermophila JCP 1-4 to saccharify sugarcane bagasse pretreated with microwaves and glycerol, glucose and xylose yields obtained are 15.6% and 35.13% (2.2 g/l and 1.95 g/l), respectively 3.2.1.8 endo-1,4-beta-xylanase degradation application in enzymatic hydrolysis for sugars production from lignocellulosic biomass. On empty fruit bunch as a feedstock, the total sugars conversion is 3.8%, and the conversion after alkaline pretreatment is approximately 16fold improved (61.1%) 3.2.1.8 endo-1,4-beta-xylanase degradation application of enzyme for biobleaching of Eucalyptus kraft pulp, the xylanase increases the brightness of the pulp by 14.5% and reduces the kappa number by 24.5% 3.2.1.8 endo-1,4-beta-xylanase degradation enzyme can be used for hydrolysis of pretreated agro-wastes. Sugarcane juice substituted medium yields maximum (52.19%) reducing sugar, followed by bioethanol production (4.19 g/l) at 72 h of incubation 3.2.1.8 endo-1,4-beta-xylanase degradation when a fusion protein with the carbohydrate-binding domain of xylanase XynZ from Clostridium thermocellum supplements the commercial cocktail Accellerase1 1500, reducing sugar release is improved by 17% from pretreated sugarcane bagasse 3.2.1.11 dextranase degradation crosslinking of dextranase on chitosan hydrogel microspheres. A shift in optimum pH and temperature from 7.0 to 7.5 and 50 to 60°C is observed after immobilization, respectively. Recycling efficiency, thermal stability, and activation energy distinctly improve after immobilization, whereas anchoring of substrate at the active site of the soluble dextranase exhibits an increase in Km with no change in Vmax after crosslinking 3.2.1.11 dextranase degradation the hydrolysis of dextran under ultrasound/microwave irradiation shock treatment is significantly higher than those performed under ultrasound, microwave irradiation shock and conventional thermal incubation at all conditions studied. The maximum hydrolysis rate is observed when ultrasound/microwave irradiation shock (ultrasound of 50 W combined with microwave irradiation shock of 60 W at a sock rate of 20 s/min for 25 min) is used in which the dextran hydrolysis increases by 171.13% compared with routine conventional heating. Vmax and KM values of dextranase under ultrasound/microwave irradiation shock treatment are higher than those under ultrasound, microwave irradiation shock and conventional thermal incubation 3.2.1.14 chitinase degradation the enzyme is used for degradation of chitin-rich waste materials 3.2.1.14 chitinase degradation exo-acting enzyme with potential interest regarding the biodegradation of chitin waste or its bioconversion into biologically active products 3.2.1.15 endo-polygalacturonase degradation multiplicity of PGs that degrade the pectin component of the plant tissue in different fashions 3.2.1.21 beta-glucosidase degradation beta-glucan can be completely degraded to glucose at high temperature with a combination of the hyperthermophile Pyrococcus furiosus endocellulase (EGPf) and beta-glucosidase (BGLPf). beta-Glucans are polysaccharides of D-glucose monomers formed by beta(1->3),(1->4) mixed-linkage bonds. They occur most commonly as cellulose in plants, in the bran of cereal grains, the cell wall of baker's yeast, and in certain fungi, mushrooms, and bacteria 3.2.1.21 beta-glucosidase degradation a 3.43fold synergistic effect by combining with Trichoderma reesei cellulases is observed 3.2.1.21 beta-glucosidase degradation enzyme shows increased thermal stability and saccharification yield on pretreated corn stover compared with Hypocrea jecorina Cel3A 3.2.1.21 beta-glucosidase degradation hydrolysis of pretreated Alfa fibers (Stipa tenacissima) by beta-D-glucosidase and xylanase, produced by a solid state fermentation process of wheat bran supplemented with lactose. The maximum saccharification yield of 83.23% is achieved under substrate concentration 3.7% (w/v), time 144 h and enzyme loading of 0.8 FPU, 15 U CMCase, 60 U beta-D-glucosidase and 125 U xylanase 3.2.1.21 beta-glucosidase degradation using enzymatic extract from Myceliophthora thermophila JCP 1-4 to saccharify sugarcane bagasse pretreated with microwaves and glycerol, glucose and xylose yields obtained are 15.6% and 35.13% (2.2 g/l and 1.95 g/l), respectively 3.2.1.21 beta-glucosidase degradation addition of beta-glucosidase to the rice straw hydrolysis reaction containing a commercial cellulase results in increase of reducing sugars being released 3.2.1.21 beta-glucosidase degradation application of enzyme in fed-batch hydrolysis of cellulose and high-temperature simultaneous saccharification and fermentation. beta-Glucosidase is suitable for lignocellulose conversion into ethanol 3.2.1.21 beta-glucosidase degradation enzyme shows synergistic effects when commercial cellulase when is supplemented with the crude beta-glucosidase leading to improved sugar release of up to 548.4 mg/gds from paddy straw at 40°C 3.2.1.21 beta-glucosidase degradation highly efficient synergistic effects exist between TN0602 and cellulases for cellulose hydrolysis 3.2.1.21 beta-glucosidase degradation saccharification of pretreated paddy straw by supplementing beta-glucosidase enzyme results in 1.34fold higher glucose release 3.2.1.21 beta-glucosidase degradation the supplementation of BglP significantly enhances the glucose yield from sugarcane bagasse, especially in the presence of high concentrations of glucose or xylose 3.2.1.21 beta-glucosidase degradation use for bioethanol production from different cellulosic biomass sources. Using simultaneous saccharification and fermentation, 9.47 g/l and 14.32 g/l of bioethanol can be obtained from carboxymethyl cellulose and pretreated rice straw, respectively 3.2.1.21 beta-glucosidase degradation the high-catalytic turn-over rate by mutant enzyme D206N for beta-glucosidase activity makes it a useful enzyme in cellulose degradation at high temperatures 3.2.1.22 alpha-galactosidase degradation enzyme completely hydrolyzes raffinose and stachyose present in soybeans and kidney beans at 50°C within 60 min 3.2.1.23 beta-galactosidase degradation evaluation of different commercial soluble beta-galactosidases for removal of the residual lactose in crude galactooligosaccharides. Best enzyme tested is lactase NL, with a hydrolytic activity of 286 IU/mg and a half-life of 9 h at 35°C in the presence of 1 mM Mn2+. The best reaction conditions are 35°C, 50% initial carbohydrate concentration and 135 IU/g, leading to 70% reduction of lactose in raw galactooligosaccharides, with an increase of 48% in monosaccharides and of 30% in galactooligosaccharides 3.2.1.B28 Pyrococcus furiosus beta-glycosidase degradation encapsulation of CelB into silica microcapsules for degradation of biomass. The encapsulated enzyme is active at 80-100°C, but diffusion of cellobiose into the silica microcapsules is a rate-limiting step 3.2.1.37 xylan 1,4-beta-xylosidase degradation hydrolysis of water-soluble and water-insoluble arabinoxylan and whole vinasse by an enzyme cocktail containing a 20%:20%:20%:40% mixture and a 25%:25%:25%:25% mixture, respectively, of the GH43 alpha-L-arabinofuranosidase from Humicola insolens, the GH51 alpha-L-arabinofuranosidase from M. giganteus, a GH10 endo-1,4-beta-xylanase from H. insolens, and a GH3 beta-xylosidase from Trichoderma reesei. The optimal dosages of the minimal enzyme cocktails are 0.4, 0.3, and 0.2 g enzyme protein per kilogram of substrate dry matter for the water-soluble wheat arabinoxylan, the water-insoluble wheat arabinoxylan, and the vinasse, respectively 3.2.1.37 xylan 1,4-beta-xylosidase degradation hydrolysis of xylan by co-action of enzyme and xylanase from Anoxybacillus flavithermus BC gives 63.6% conversion after 4 h. Beechwood xylan is the best substrate, main product is xylose 3.2.1.37 xylan 1,4-beta-xylosidase degradation in hydrolysis of corn stover hemicellulose, the xylose production increases by 94.9% and 140% when Trichoderma reesei hemicellulase is supplemented with purified beta-xylosidase and crude cell wall proteins of corn stover, respectively 3.2.1.37 xylan 1,4-beta-xylosidase degradation co-immobilization of xylanase, beta-xylosidase and alpha-L-arabinofuranosidase from Penicillium janczewskii on a single support leads to a functional multi-enzymatic biocatalyst acting in the complete hydrolysis of different and complex substrates such as oat spelt and wheat arabinoxylans, with xylose yield higher than 40%. The xylanase and the alpha-L-arabinofuranosidase present high stability retaining 86.6 and 88.0% of activity after 10 reuse cycles 3.2.1.37 xylan 1,4-beta-xylosidase degradation enzyme increases reducing sugar release of birchwood xylan, beechwood xylan, and arabinoxylan by 6.4%, 13%, 15.8%, respectively, in synergistic action with endoxylanase. The late addition of the enzyme into reaction with endoxylanase results in a larger increase of reducing sugar release from pretreated barley straw that addition at the start or by treatment with endoxylanases alone. The increases observed are 6.3% and 13.8%, respectively 3.2.1.37 xylan 1,4-beta-xylosidase degradation treatment of Eucalyptus kraft pulp with culture supernatant at 10 IU per gram pulp to enhance bleaching of kraft pulp results in a 10.5% reduction in Kappa number (indicating the amount of chemicals needed for bleaching pulps) and has a positive effect on the brightness of the resulting handsheets 3.2.1.37 xylan 1,4-beta-xylosidase degradation the enzyme has potential for promoting hemicellulose degradation and other industrial applications 3.2.1.37 xylan 1,4-beta-xylosidase degradation the enzyme is useful for degradation of lignocellulosic biomass in bioethanol production, pulp bleaching process and beverage industry 3.2.1.40 alpha-L-rhamnosidase degradation recombinant rhamnosidase is thermostable and highly active for naringin hydrolysis up to more than 77%, thus producing L-rhamnose and prunin from citrus peel waste 3.2.1.41 pullulanase degradation pullulanase is useful in the fermentation of high-gravity maize, together with other proteolytic and polysaccharide-degrading enzyme. Adding pullulanase resultes in the acceleration of the starch hydrolysis degree, which leads to lower amounts of unhydrolyzed dextrins and higher ethanol yield 3.2.1.55 non-reducing end alpha-L-arabinofuranosidase degradation enzyme of industrial interest because of its ability to improve hydrolytic action of other glycanases on hemicellulolytic polysaccharides 3.2.1.55 non-reducing end alpha-L-arabinofuranosidase degradation application potential for industrial purposes, biomass degradation and refining, extremely low end-product inhibition by arabinose further increases its applicability 3.2.1.55 non-reducing end alpha-L-arabinofuranosidase degradation enzymatic hydrolysis of wheat arabinoxylan. Treatment of water-soluble and water-insoluble wheat arabinoxylan with an enzyme cocktail containing a 20%:20%:20%:40% mixture and a 25%:25%:25%:25% mixture, respectively, of the GH43 alpha-L-arabinofuranosidase from Humicola insolens (Abf II), the GH51 alpha-L-arabinofuranosidase from Meripilus giganteus (Abf III), a GH10 endo-1,4-beta-xylanase from Humicola insolens (Xyl III), and a GH3 beta-xylosidase from Trichoderma reesei releases 322 mg of arabinose and 512 mg of xylose per gram of water-soluble wheat arabinoxylan dry matter and 150 mg of arabinose and 266 mg of xylose per gram of water-insoluble wheat arabinoxylan dry matter after 24 h at pH 5, 50°C. A 10%:40%:50% mixture of Abf II, Abf III, and beta-xyl releases 56 mg of arabinose and 91 mg of xylose per gram of vinasse dry matter after 24 h at pH 5, 50°C. The optimal dosages of the enzyme cocktails are determined to be 0.4, 0.3, and 0.2 g enzyme protein per kilogram of substrate dry matter for the water-soluble wheat arabinoxylan, the water-insoluble wheat arabinoxylan, and the vinasse, respectively 3.2.1.55 non-reducing end alpha-L-arabinofuranosidase degradation Abf51A shows greater synergistic effect in combination with xylanase (2.92fold) on wheat arabinoxylan degradation than other reported enzymes, the amounts of arabinose, xylose, and xylobiose are all increased in comparison to that by the enzymes acting individually 3.2.1.55 non-reducing end alpha-L-arabinofuranosidase degradation co-immobilization of xylanase, beta-xylosidase and alpha-L-arabinofuranosidase from Penicillium janczewskii on a single support leads to a functional multi-enzymatic biocatalyst acting in the complete hydrolysis of different and complex substrates such as oat spelt and wheat arabinoxylans, with xylose yield higher than 40%. The xylanase and the alpha-L-arabinofuranosidase present high stability retaining 86.6 and 88.0% of activity after 10 reuse cycles 3.2.1.55 non-reducing end alpha-L-arabinofuranosidase degradation enzyme shows synergistic effect on arabinose liberation from wheat arabinoxylan when combined with endoxylanase from Penicillium purpurogenum 3.2.1.55 non-reducing end alpha-L-arabinofuranosidase degradation hydrolysis of insoluble wheat arabinoxylan using different endoxylanases in combination with arabinofuranosidase Araf51A. The optimized combination is endoxylanases XynZ/Xyn11A/Araf51A with a loading ratio of 2:2:1, and the value of degree of synergy increases with the increase of Araf51A proportion in the enzyme mixture. Both free and enzymes immobilized on commercial magnetic nanoparticles show a similar conversion to reducing sugars after hydrolysis for 48 h. After 10 cycles, approximately 20% of the initial enzymatic activity of both the individual or mixture of immobilized enzymes is retained, with 5.5fold increase in the production of sugars. A sustainable synergism between immobilized arabinofuranosidase and immobilized endoxylanases in the hydrolysis of arabinoxylan is observed 3.2.1.55 non-reducing end alpha-L-arabinofuranosidase degradation the combination of Axy43A and Paenibacillus curdlanolyticus B-6 endo-xylanase Xyn10C greatly improves the efficiency of xylose and arabinose production from the highly substituted rye arabinoxylan 3.2.1.68 isoamylase degradation thermophilic enzyme shows a potential to be used in industry to degrade the debranching points of starch at a high temperature 3.2.1.73 licheninase degradation hydrolysis of insoluble wheat arabinoxylan using different endoxylanases in combination with arabinofuranosidase Araf51A. The optimized combination is endoxylanases XynZ/Xyn11A/Araf51A with a loading ratio of 2:2:1, and the value of degree of synergy increases with the increase of Araf51A proportion in the enzyme mixture. Both free and enzymes immobilizedon commercial magnetic nanoparticles show a similar conversion to reducing sugars after hydrolysis for 48 h. After 10 cycles, approximately 20% of the initial enzymatic activity of both the individual or mixture of immobilized enzymes is retained, with 5.5fold increase in the production of sugars. A sustainable synergism between immobilized arabinofuranosidase and immobilized endoxylanases in the hydrolysis of arabinoxylan is observed 3.2.1.73 licheninase degradation the saccharification of untreated reed and rice straw powders by commercial enzymes (Celluclast 1.5 L and Novozym 188) is increased by 10.4 and 4.8%, respectively, by the addition of BGlc8H. In the presence of Ca2+ and BGlc8H, the saccharification of the pretreated reed and rice straw powders by the commercial enzymes is increased by 18.5 and 11.7%, respectively 3.2.1.73 licheninase degradation fermentation capacity of recombinant Bacillus subtilis expressing mutant K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P reaches 242.02 U ml/h. The addition of the mutant protein in Congress mashing significantly reduces the filtration time and viscosity of mash by 29.7% and 12.3%, respectively 3.2.1.78 mannan endo-1,4-beta-mannosidase degradation when assembled with the mini-CbpA, which contains a carbohydrate-binding module that provides proximity to insoluble substrates, a mixture of endoglucanase E and ManB at a molar ratio of 1:2 shows the highest synergistic effect of 2.4fold on locust bean gum degradation. The mixture at a ratio of 1:3 shows the highest synergistic effect of 2.8fold on guar gum 3.2.1.78 mannan endo-1,4-beta-mannosidase degradation the addition of Man26A as a supplement to the commercial enzyme mixture Celluclast 1.5 L and Novozyme 188 results in enhanced enzymatic hydrolysis of pretreated beechwood sawdust, the release of total reducing sugars and glucose is improved by 13 and 12%, respectively 3.2.1.91 cellulose 1,4-beta-cellobiosidase (non-reducing end) degradation application of recombinant CBH II in hydrolysis of corn stover and rice straw pretreated with sodium hydroxide by improving the exo-exosynergism between CBH II and CBH I in Hypocrea jecorina. The yields 94.7% and 83.3% are achieved in the enzymatic hydrolysis of corn stover and rice straw pretreated by sodium hydroxide, respectively 3.2.1.91 cellulose 1,4-beta-cellobiosidase (non-reducing end) degradation construction of a consolidated bioprocessing-enabling yeast by constitutive expression of genes Cbh1 from Aspergillus aculeatus, Cbh1 and Cbh2 from Hypocrea jecorina. Additionally, Hypocrea jecorina Eg2, Aspergillus aculeatus Bgl1 are integrated into the Saccharomyces cerevisiae chromosome. The resultant strains expressing uni-, bi-, and trifunctional cellulases, respectively, exhibit corresponding cellulase activities and both the activities and glucose producing activity ascends. Evaluation in acid- and alkali-pretreated corncob containing media with 5 FPU exogenous cellulase/g biomass loading shows that compared with the control strains, the engineered strains efficiently ferment pretreated corncob to ethanol 3.2.1.91 cellulose 1,4-beta-cellobiosidase (non-reducing end) degradation using enzymatic extract from Myceliophthora thermophila JCP 1-4 to saccharify sugarcane bagasse pretreated with microwaves and glycerol, glucose and xylose yields obtained are 15.6% and 35.13% (2.2 g/l and 1.95 g/l), respectively 3.2.1.91 cellulose 1,4-beta-cellobiosidase (non-reducing end) degradation combined use of isoforms CBH A and Cbh C on degradation of cotton. Conversion after 72 h is about 19 % by weight, with an almost fourfold increase in enzymatic hydrolysis yield by intermittent product removal of cellobiose with membrane filtration. A synergistic effect, achieving about 27 % substrate conversion, is obtained by addition of endo-1,4-beta-D-glucanase 3.2.1.99 arabinan endo-1,5-alpha-L-arabinanase degradation synergistic action of arase and pectinase can significantly improve the degradation of sugar beet pulp 3.2.1.129 endo-alpha-sialidase degradation degradation of non-toxic modified polysialic acid hydrogel scaffold in neuro-regenerative tissue engineering (4.26 microgram enzyme + 39 mg hydrogel), in phosphate buffered saline (400 microl, pH 7.4), at 37°C, degradation speed 2-11 days depending on cross-linker amount (0.6, 0.8, 2 equivalents diepoxyoctane, no activity with 3 equivalents diepoxyoctane), hydrogel was coated with collagen I, poly-L-lysine/collagen I, or diluted matrigel for neurite formation in PC12 cells 3.2.1.129 endo-alpha-sialidase degradation degradation of non-toxic modified polysialic acid hydrogel scaffold in neuro-regenerative tissue engineering: no degradation in 12 days with 1 microg/ml active enzyme + 105 cubic mm hydrogel in phosphate buffered saline (pH 7.4), at room temperature, increase to 4 microg/ml at end of week 2 initiates degradation, total degradation after 4 weeks, hydrogel was coated with poly-L-lysine, poly-L-ornithine-laminin or collagen for neurite formation in neonatal and adult rat Schwann cells, neural rat stem cells, and dorsal root ganglionic cells from rats 3.2.1.131 xylan alpha-1,2-glucuronosidase degradation synergistic effects by use of enzyme and endoxylanase for degradation of oat xylan 3.2.1.131 xylan alpha-1,2-glucuronosidase degradation intracellular extract from Paenibacillus curdlanolyticus B-6, with synergistic alpha-glucuronidase and beta-xylosidase activities, degrades hexenuronosyl xylotriose to hexenuronic acid and xylotriose 3.2.1.131 xylan alpha-1,2-glucuronosidase degradation xylan degradation by endoxylanase Xyn10A is enhanced by about 10% in presence of AguA 3.2.1.133 glucan 1,4-alpha-maltohydrolase degradation microcapsules from poly(vinyl alcohol) and hexamethylene diisocyanate, encapsulated with aqueous solution of maltogenic alpha-amylase from Bacillus stearothermophilus have potential application in biotechnology for saccharification of starch 3.2.1.139 alpha-glucuronidase degradation an enzymatic cocktail consisting of Agu115 with xylanase (Xyn10C), an alpha-L-arabinofuranosidase (AbfA), and a beta-xylosidase (XynB) achieves almost complete conversion of glucuronoarabinoxylan to arabinofuranose, xylopyranose, and methyl glucuronate monosaccharides. Addition of isoform Agu115 to the enzymatic cocktail contributes specifically to 25% of the conversion 3.2.1.139 alpha-glucuronidase degradation intracellular extract from Paenibacillus curdlanolyticus B-6, with synergistic alpha-glucuronidase and beta-xylosidase activities, degrades hexenuronosyl xylotriose to hexenuronic acid and xylotriose 3.2.1.151 xyloglucan-specific endo-beta-1,4-glucanase degradation xyloglucan endotransglucosylase can act as a cell wall-loosening enzyme 3.2.1.176 cellulose 1,4-beta-cellobiosidase (reducing end) degradation commercial cellulases contain mannan hydrolysing enzymes. Addition of 10 mg/ml mannan reduces the glucose yield of avicel (at 20 g/l) from 40.1 to 24.3%. The inhibitory effect is at least partly attributed to the inhibition of Cel7A(CBHI), but not on beta-glucosidase 3.2.1.176 cellulose 1,4-beta-cellobiosidase (reducing end) degradation comparison of the activity w ith Humicola jecorina Cel7A reveals a much higher hydrolytic rate for Humicola grisea Cel7A at both 65°C (4.8fold higher initial rate) and 38°C (3.3fold higher) 3.2.1.176 cellulose 1,4-beta-cellobiosidase (reducing end) degradation construction of a consolidated bioprocessing-enabling yeast by constitutive expression of genes Cbh1 from Aspergillus aculeatus, Cbh1 and Cbh2 from Hypocrea jecorina. Additionally, Hypocrea jecorina Eg2, Aspergillus aculeatus Bgl1 are integrated into the Saccharomyces cerevisiae chromosome. The resultant strains expressing uni-, bi-, and trifunctional cellulases, respectively, exhibit corresponding cellulase activities and both the activities and glucose producing activity ascends. Evaluation in acid- and alkali-pretreated corncob containing media with 5 FPU exogenous cellulase/g biomass loading shows that compared with the control strains, the engineered strains efficiently ferment pretreated corncob to ethanol 3.2.1.176 cellulose 1,4-beta-cellobiosidase (reducing end) degradation development of optimal enzyme mixtures of six Trichoderma reesei enzymes and five thermostable enzyme for the hydrolysis of hydrothermally pretreated wheat straw, alkaline oxidised sugar cane bagasse and steam-exploded bagasse by statistically designed experiments. The composition of optimal enzyme mixtures depends clearly on the substrate and on the enzyme system studied. The optimal enzyme mixture of thermostable enzymes is dominated by Cel7A and requires a relatively high amount of xylanase, whereas with Hypocrea jecorina enzymes, the high proportion of Cel7B appears to provide the required xylanase activity 3.2.1.176 cellulose 1,4-beta-cellobiosidase (reducing end) degradation enzyme works synergistically with the commercial enzyme cocktail Cellic R  CTec2 to enhance saccharification by 39% when added to a reaction mixture containing 0.25% alkaline pretreated oil palm empty fruit bunch 3.2.1.176 cellulose 1,4-beta-cellobiosidase (reducing end) degradation a fungal consortium of Aspergillus nidulans, Mycothermus thermophilus, and Humicola sp. composts a mixture (1:1) of silica rich paddy straw and lignin rich soybean trash during summer period in North India, results in a product with C:N ratio 9.5:1, available phosphorus 0.042% and fungal biomass 6.512 mg of N-acetyl glucosamine/100 mg of compost. A C:N ratio of 10.2:1 and highest humus content of 3.3% is achieved with 1:1 mixture of paddy straw and soybean trash. The consortium shows showed high cellobiase, carboxymethyl cellulase, xylanase, and FPase activities 3.4.13.9 Xaa-Pro dipeptidase degradation advantages of using Alteromonas recombinant prolidase in biodecontamination foams due to its high activity against G-type nerve agents, such as soman and sarin 3.4.13.9 Xaa-Pro dipeptidase degradation prolidase is able to degrade toxic organophosphorus compounds, namely, by cleaving the P-F and P-O bonds in the nerve agents, sarin and soman. Applications using prolidase to detoxify organophosphorous nerve agents include its incorporation into fire-fighting foams and as biosensors for organophosphorous compound detection 3.4.17.18 carboxypeptidase T degradation reconstruction of the primary specificity pocket of CpT to make it like CpB neither enhances the CpT5 activity with a substrate possessing C-terminal Arg, nor lowers the activity with a substrate carrying C-terminal Leu. Notwithstanding the considerable structural similarity of CpT and CpB, the mechanisms underlying their substrate specificities are different 3.4.19.1 acylaminoacyl-peptidase degradation AAP displays both exo- and endopeptidase activities 3.4.19.12 ubiquitinyl hydrolase 1 degradation a natural dodecapeptide amide from UCH-L3 with the sequence DPDELRFNAIAL is capable of binding to monoubiquitin and may enable the design of peptides with different affinities towards K48- and K63-linked polyubiquitin 3.4.19.12 ubiquitinyl hydrolase 1 degradation protein L-isoaspartate O-methyltransferase initiates the repair of isoaspartyl residues in aged or stress-damaged proteins in vivo, e.g. UCHL1 is a substrate for the L-isoaspartate methyltransferase in vivo 3.4.21.7 plasmin degradation cleavage at Arg336 is a central mechanism of plasmin-catalyzed factor VIII inactivation. Cleavages at Arg336 and Lys36 are selectively regulated by the A2 and A3-C1-C2 domains, respectively, interacting with plasmin 3.4.21.61 Kexin degradation ASP preferentially cleaves the peptide bond following two basic residues, one of which is Lys, but not the bond following a single basic residue. Tertiary structure around the catalytic domain of ASP resembles, but is not identical to that of furin 3.4.21.61 Kexin degradation Dpy-5 procollagen requires processing by BLI-4 for normal cuticle production 3.4.21.61 Kexin degradation PC1/3 is essential and sufficient for the production of the intestinal incretin hormone GIP 3.4.21.62 Subtilisin degradation subtilisin releases Phr signalling peptides derived from the C-terminus of their precursor proteins, but does not release Phr peptides derived from an internal portion of its precursor proteins 3.4.21.64 peptidase K degradation use of enzyme to degrade poly(L-lactide) film. Adsorption of enzyme to film is irreversible, enzyme moves on the surface of substrate to hydrolyze the film around it 3.4.21.79 granzyme B degradation human and murine GzmB are distinct enzymes with different substrate preferences. Subtle differences in enzyme structure can radically affect substrate selection. Caspases are essential for apoptosis initiated by mouse GzmB 3.4.21.79 granzyme B degradation human and murine GzmB are distinct enzymes with different substrate preferences. Subtle differences in enzyme structure can radically affect substrate selection. Caspases are not essential for apoptosis initiated by human GzmB 3.4.21.112 site-1 protease degradation S1P reduces the size of the luminal domain to prepare ATF6 to be an optimal S2P substrate 3.4.24.B6 matrix metalloproteinase-20 degradation MMP-20 processes dentin sialophosphoprotein into smaller subunits in the dentin matrix during odontogenesis 3.4.24.12 envelysin degradation one of the earliest zygotic genes activated, about 12-20 h after fertilization, the hatching enzyme is secreted, digesting the fertilization envelope and freeing the swimming blastula 3.4.24.B16 protease lasA degradation two-stage enzymatic reaction for the continuous measurement of LasA protease activity using a defined substrate, supplemented with Streptomyces griseus aminopeptidase for further cleavage of the product, rate of release of the chromophore can be measured spectrophotometrically 3.4.24.B19 i-AAA protease degradation essential function of the central pore loop for the ATP-dependent translocation of membrane proteins into a proteolytic cavity formed by AAA protease 3.4.24.37 saccharolysin degradation most likely major intracellular oligopeptidase responsible for the degradation of peptides resulting from nonvacuolar proteolysis 3.4.24.37 saccharolysin degradation Prd1 together with Mop112 is involved in the complete degradation of a large number of mitochondrial proteins to amino acids and therefore broadly influences the peptide efflux from mitochondria 3.4.24.38 gametolysin degradation degrades gametic cell walls, cell walls of vegetative cells and those of mother sporangial cells 3.4.24.66 choriolysin L degradation first choriolysin H swells the inner layer of egg envelope by limited digestion, and then choriolysin L solubilizes the swollen part of it completely 3.4.24.67 choriolysin H degradation HCE dissolves the inner layer of the egg envelope to facilitate hatching of the embryo 3.4.24.77 snapalysin degradation enzymatic and microbiological hydrolysis at the industrial level 3.4.24.78 gpr endopeptidase degradation D127 and D193 are essential for activity and autoprocessing 3.4.24.82 ADAMTS-4 endopeptidase degradation abrasion of cartilage aggrecan in rheumatoid arthritis and osteoarthritis 3.4.24.82 ADAMTS-4 endopeptidase degradation degradation of cartilage in late-stage Lyme arthritis 3.4.24.82 ADAMTS-4 endopeptidase degradation degradation of cartilage proteoglycan (aggrecan) in osteoarthritis and rheumatoid arthritis 3.4.25.1 proteasome endopeptidase complex degradation targeted proteasomal knockdown of GFP is induced by use of a specific anti-GFP nanobody in plants. GFP is depleted by a chimeric nanobody fused to a distinct F-box domain, which enables protein degradation via the ubiquitin proteasome pathway 3.5.1.9 arylformamidase degradation aerobic degradation of L-tryptophan 3.5.4.42 N-isopropylammelide isopropylaminohydrolase degradation biotic interaction between earthworms and the bacterial community involved in degradation of the herbicide atrazine in a maize-cropped soil, earthworms significantly affect the structure of the soil bacterial communities in the biostructures, they reduce the size of the population of Pseudomonas sp. ADP, thereby contributing to the diminution of the atrazine-degrading genetic potential in soil microsites 3.5.4.42 N-isopropylammelide isopropylaminohydrolase degradation broad level bacterial community interactions that are involved in atrazine degradation in nature 3.5.4.42 N-isopropylammelide isopropylaminohydrolase degradation broad level bacterial community interactions that are involved in atrazine degradation in nature, Nocardia sp. plays a crucial role for stable maintenance of the degrader community, dechlorination of atrazine is carried out exclusively by Nocardia sp. which apart from the atzC gene contains the trzN gene 3.5.4.42 N-isopropylammelide isopropylaminohydrolase degradation enzyme degrades the herbicide atrazine, biodegredation in the microcosm appears to occur predominantely by Nocardioides sp. to yield cyanuric acid, which can be mineralised by other relatively ubiquitous microbes 3.5.4.42 N-isopropylammelide isopropylaminohydrolase degradation novel atrazine catabolic pathway combining trzN with atzB and atzC, the gene products dechlorinate and then dealkylate atrazine 3.5.4.43 hydroxydechloroatrazine ethylaminohydrolase degradation strain ADP, use of atrazine as sole nitrogen source, but not as sole carbon source. Comparison of degradation products with those from Pseudoaminobacter sp. and Nocardiodes sp. 3.5.4.43 hydroxydechloroatrazine ethylaminohydrolase degradation use of atrazine as sole nitrogen source and as sole carbon source. Comparison of degradation products with those from Pseudomonas sp. and Nocardiodes sp. 3.5.4.43 hydroxydechloroatrazine ethylaminohydrolase degradation use of atrazine as sole nitrogen source and as sole carbon source. End product of atrazine metabolism is N-ethylammelide. Comparison of degradation products with those from Pseudomonas sp. and Nocardiodes sp. 3.5.4.43 hydroxydechloroatrazine ethylaminohydrolase degradation mineralization of low concentrations of atrazine in the groundwater zone at low temperatures is possible by bioremediation treatments. In combined biostimulation treatment using citrate or molasses and augmentation with Pseudomonas citronellolis ADP or Arthrobacter aurescens strain TC1, up to 76% of atrazine is mineralized at 30°C, and the atrazine degradation gene numbers increase up to 10 million copies/g soil 3.5.4.43 hydroxydechloroatrazine ethylaminohydrolase degradation mineralization of low concentrations of atrazine in the groundwater zone at low temperatures is possible by bioremediation treatments. In combined biostimulation treatment using citrate or molasses and augmentation with Pseudomonas citronellolis ADP or Arthrobacter aurescens strain TC1, up to 76%of atrazine is mineralized at 30°C, and the atrazine degradation gene numbers increase up to 10 million copies/g soil 3.5.4.43 hydroxydechloroatrazine ethylaminohydrolase degradation strain HB-6 is capable of utilizing atrazine and cyanuric acid as a sole nitrogen source for growth and even cleaves the s-triazine ring and mineralizes atrazine. The strain demonstrate a very high efficiency of atrazine biodegradation with a broad optimum pH and temperature ranges and can be enhanced by cooperating with other bacteria 3.5.5.4 cyanoalanine nitrilase degradation this enzyme is of interest for the use in the biodegradation of cyanide and the degradation of nitrile wastes 3.5.99.5 2-aminomuconate deaminase degradation new tryptophan catabolic pathway in Burholderia cepacia J2315, formation of the intermediate 4-oxalocrotonate differentiates this pathway from the proposed mammalian pathway which converts 2-aminomuconate to 2-ketoadipate and, ultimately, glutaryl-coenzyme A 3.7.1.2 fumarylacetoacetase degradation the enzyme is part of the key catabolic trait for biodegradation of a small number of aromatic compounds 3.7.1.8 2,6-dioxo-6-phenylhexa-3-enoate hydrolase degradation key determinant in the aerobic transformation of polychlorinated biphenyls by divergent biphenyl degraders 3.7.1.11 cyclohexane-1,2-dione hydrolase degradation the enzyme is involved in biodegradation of alicyclic compounds involving a C-C bond ring cleavage to generate an aliphatic intermediate. Alicyclic alcohols compounds, which can serve as insecticides, herbicides, or as intermediates and solvents in chemical industries, are widespread in nature as the secondary metabolites of plant and occurring in fossil fuels 3.8.1.3 haloacetate dehalogenase degradation 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 degradation simple route of detoxification 3.8.1.5 haloalkane dehalogenase degradation potential biocatalyst for bioremediation/biosensing of mixed pollutants 4.1.1.2 oxalate decarboxylase degradation oxalic acid removal in industrial bleaching plant filtrates containing oxalic acid 4.1.1.102 phenacrylate decarboxylase degradation expression of aldehyde dehydrogenase Ald5, phenylacrylic acid decarboxylase Pad1, and alcohol acetyltransferases Atf1 and Atf2 increases conversion of coniferyl aldehyde, ferulic acid and p-coumaric acid. Combined overexpression of ALD5, PAD1, ATF1 and ATF2 helps Saccharomyces cerevisiae in phenolics conversion and tolerance 4.1.99.2 tyrosine phenol-lyase degradation removal and bioconversion of phenol in wastewater by a thermostable beta-tyrosinase 4.2.1.28 propanediol dehydratase degradation possible use in anaerobic polyethylene glycol degradation 4.2.1.84 nitrile hydratase degradation treatment of acetonitrile-containing wastes on-site, Brevundimonas diminuta containing enzyme degrades acetonitrile at concentrations up to 6 M 4.2.1.84 nitrile hydratase degradation treatment of acetonitrile-containing wastes on-site, Rhodococcus pyridinivorans S85-2 containing enzyme degrades acetonitrile at concentrations up to 6 M 4.2.2.1 hyaluronate lyase degradation use of biocompatible magnetic macroporous bead cellulose functionalised with hyaluronan lyase for controlled fragmetation of hyaluronan. Immobilisation of enzyme on macroporous bead cellulose via reductive amination or macroporous bead cellulose with fixed iminodiacetic acid via a His8-tag has minimal impact on its catalytic activity. The carrier with with fixed iminodiacetic acid shows excellent operational and storage stability, and both carriers enable reproducible time-controlled fragmentation of highly viscous high moleculare weight hyaluronan solutions, yielding hyaluronan fragments of appropriate molecular weight 4.2.2.2 pectate lyase degradation useful for degradation of pectin networks at high temperatures 4.2.2.2 pectate lyase degradation enzyme is able to remove most of pectin in hemp fiber with less damage compared to alkaline degumming. Predigestion with the enzyme improves glucose and xylose yield by 14.2% and 311.6%, respectively, for corn stalk, 6.5% and 55% for rice stalk compared with sole action of Novozymes Cellic CTec2 4.2.2.2 pectate lyase degradation significant ramie (Boehmeria nivea) fiber weight loss (21.5%) is obtained following enzyme treatment and combined enzyme-chemical treatment (29.3%). The productivity may reach 48.3 U ml/h under high-cell-density cultivation for 30 h in 1l fed-batch fermenter, using Escherichia coli as host 4.2.2.3 mannuronate-specific alginate lyase degradation alginate lyase is probably not suitable for hydrolysis of microcapsules in the presence of cells, in order to achieve high cell density and high productivity. However, the high activity may be useful for releasing cells from alginate beads or AG/PLL microcapsules 4.2.2.3 mannuronate-specific alginate lyase degradation enzymatic treatment for 24 hours is sufficient to release all potential glucose from the glucan rich brown seaweed Laminaria digitata 4.2.2.3 mannuronate-specific alginate lyase degradation enzymatical saccharification of acid pretreated and untreated brown macroalgae, first at pH 7.5, 25°C for 12 h with a blend of recombinant alginate and oligoalginate lyases, then at pH 5.2 using a commercial cellulase cocktail. The use of recombinant alginate lyases and oligoalginate lyases in combination with cellulases increases the release of glucose from untreated seaweed. For saccharification of pretreated algae, only cellulases are needed to achieve high glucose yields 4.2.2.11 guluronate-specific alginate lyase degradation enzymatic treatment for 24 hours is sufficient to release all potential glucose from the glucan rich brown seaweed Laminaria digitata 4.2.2.11 guluronate-specific alginate lyase degradation enzymatical saccharification of acid pretreated and untreated brown macroalgae, first at pH 7.5, 25°C for 12 h with a blend of recombinant alginate and oligoalginate lyases, then at pH 5.2 using a commercial cellulase cocktail. The use of recombinant alginate lyases and oligoalginate lyases in combination with cellulases increases the release of glucose from untreated seaweed. For saccharification of pretreated algae, only cellulases are needed to achieve high glucose yields 4.2.2.26 oligo-alginate lyase degradation combining exotype alginate lyases OalC6 and OalC17 and the endotype alginate lyase AlySY08 enables the production of alginate monomers due to synergistic processes 4.2.2.26 oligo-alginate lyase degradation enzymatical saccharification of acid pretreated and untreated brown macroalgae, first at pH 7.5, 25°C for 12 h with a blend of recombinant alginate and oligoalginate lyases, then at pH 5.2 using a commercial cellulase cocktail. The use of recombinant alginate lyases and oligoalginate lyases in combination with cellulases increases the release of glucose from untreated seaweed. For saccharification of pretreated algae, only cellulases are needed to achieve high glucose yields 4.3.1.18 D-Serine ammonia-lyase degradation the enzyme is applied to remove endogenous D-serine from organotypic hippocampal slices. Complete removal of D-serine virtually abolishes NMDA-elicited neurotoxicity 4.4.1.16 selenocysteine lyase degradation transgenic plants could be used for decontamination of high Se soil or water 4.4.1.23 2-hydroxypropyl-CoM lyase degradation the phylotype Nocardioides (Actinobacteria) is responsible for carbon assimilation from vinyl chloride. This phylotype is observed in the heavy fractions from the 13C-vinyl chloride-amended cultures at both day 32 and day 45. Identifcation of degrading strains uses gene etnE, encoding for epoxyalkane coenzymeM-transferase, a critical enzyme in the pathway for vinyl chloride degradation 4.4.1.34 isoprene-epoxide-glutathione S-transferase degradation enzyme is involved in degradation of primary oxidation products of isoprene, cis-1,2-dichloroethanol, and trans-1,2-dichloroethanol 4.5.1.3 dichloromethane dehalogenase degradation enzyme activity in recombinant cells is 3 times higher than that in the wild-type Methylorubrum rhodesianum. Degradation efficiency of dichloromethane reaches 86.11% within 20 h and is highly associated with glutathione concentration 5.2.1.4 maleylpyruvate isomerase degradation the potential use of pure culture microbial cells for the cleanup of organophosphorus-pesticide-contaminated enviroments is highlighted, and the mechanisms for isocarbophos degradation are presented 5.3.1.5 xylose isomerase degradation enzyme additionally displays xylose fermenting activity. A Saccharomyces cerevisae strain coexpressing xylose isomerase and endo-1,4-beta-xylanase Xyn11B from Saccharophagus degradans, and beta-xylosidase XlnD from Aspergillus niger is able to produce 6.0 g/l ethanol from xylan 7.1.1.2 NADH:ubiquinone reductase (H+-translocating) degradation quantification of superoxide production from Escherichia coli complex I is very prone to artifacts 7.1.1.2 NADH:ubiquinone reductase (H+-translocating) degradation strain Bacillus sp. SR-2-1/1 efficiently decolorizes azo dyes such as reactive black-5, reactive red-120, direct blue-1 and congo red through NADH-ubiquinone:oxidoreductase enzyme activity