EC Number   |
Recommended Name  |
Application |
|---|
   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 |
| 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 |
| 1.1.1.176 | 12alpha-hydroxysteroid dehydrogenase |
degradation |
new integrated chemo-enzymatic synthesis of ursodeoxycholic acid starting from sodium cholate by 7alpha- and 12alpha-hydroxysteroid dehydrogenases |
| 1.14.13.20 | 2,4-dichlorophenol 6-monooxygenase |
degradation |
immobilized enzyme exhibits great potential for application in bioremediation |
 1.2.1.26 | 2,5-dioxovalerate dehydrogenase |
degradation |
involved in an alternative pathway of D-glucarate metabolism |
| 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 |
| 3.5.99.5 | 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 |
| 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 |
| 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 |
| 1.14.13.2 | 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 |
| 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 |
| 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 |
| 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 |
| 3.1.2.20 | acyl-CoA hydrolase |
degradation |
TEII can maintain effective polyketide biosynthesis by selectively removing the nonelongatable residues bound to acyl carrier proteins |
| 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 |
| 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 |
| 3.4.19.1 | acylaminoacyl-peptidase |
degradation |
AAP displays both exo- and endopeptidase activities |
| 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 |
| 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 |
| 1.1.3.13 | 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 |
| 1.2.1.5 | aldehyde dehydrogenase [NAD(P)+] |
degradation |
degradation of polyethylene glycols, PEGs |
| 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 |
| 1.14.15.3 | 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 |
| 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 |
| 3.2.1.139 | 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 |
| 3.2.1.40 | 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 |
| 3.2.1.99 | arabinan endo-1,5-alpha-L-arabinanase |
degradation |
synergistic action of arase and pectinase can significantly improve the degradation of sugar beet pulp |
| 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 |
| 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 |
| 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 |
| 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 |
| 3.5.1.9 | arylformamidase |
degradation |
aerobic degradation of L-tryptophan |
| 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.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 |
| 1.2.1.28 | 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 |
| 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 |
| 3.2.1.21 | 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 |
| 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 |
| 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 |
| 2.7.2.2 | carbamate kinase |
degradation |
arginine is metabolized by the arginine deiminase pathway |
| 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 |
| 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 |
| 3.4.17.18 | 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 |
| 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 |
| 1.13.11.1 | 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 |
| 1.1.99.18 | cellobiose dehydrogenase (acceptor) |
degradation |
CDH is able to produce a sufficient amount of H2O2 to decolorize anthocyanins within 2 h |
| 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 9298% |
| 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 |
