EC Number   |
Recommended Name  |
Application |
|---|
   1.1.1.107 | pyridoxal 4-dehydrogenase |
analysis |
the enzyme is useful in determination of vitamin B6 contents, method development, overview |
 1.1.1.108 | carnitine 3-dehydrogenase |
analysis |
fluorometric determination of carnitine in serum with immobilized carnitine dehydrogenase and diaphorase |
| 1.1.1.11 | D-arabinitol 4-dehydrogenase |
analysis |
potential of using arabitol dehydrogenase from the non-virulent enteric bacterium, Escherichia colistrain C, as a plant selectable marker |
| 1.1.1.119 | glucose 1-dehydrogenase (NADP+) |
analysis |
method for determination of D-glucose- and D-galactose levels in glycoconjugates. The NAD(P)H produced from the enzymatic oxidation of the monosaccharides reacts with a CuSO4-bathocuproinedisulfonic acid reagent to produce a color complex absorbing maximally at 486 nm. With galactose dehydrogenase and glucose dehydrogenase serving as the model enzymes, reaction analysis gives a linear plot from 2.5 to 250 nmol of sugar. Method has been applicated to sugar released by acid hydrolysis from lactose, porcine submaxillary mucin and raffinose was quantified |
| 1.1.1.12 | L-arabinitol 4-dehydrogenase |
analysis |
enzymatic cycling assay for nicotinic acid adenine dinucleotide phosphate |
| 1.1.1.122 | D-threo-aldose 1-dehydrogenase |
analysis |
determination of bound-fucose in biological materials by a coupled enzymatic method in a single buffer system |
| 1.1.1.138 | mannitol 2-dehydrogenase (NADP+) |
analysis |
determination of D-fructose in the presence of other sugars |
| 1.1.1.146 | 11beta-hydroxysteroid dehydrogenase |
analysis |
high-throughput screening for potent and selective inhibitors of 11beta-hydroxysteroid dehydrogenase type I |
| 1.1.1.146 | 11beta-hydroxysteroid dehydrogenase |
analysis |
use of microdialysis sampling coupled with liquid chromatography/electrospray ionization mass spectrometry to study 11beta-hydroxysteroid dehydrogenase type 1 catalyzed conversion of stable-isotope-labeled cortisone to cortisol in liver microsome. Results show species-specific reaction profiles, with a five times higher coversion rate in dog than in human and monkey liver microsome |
| 1.1.1.149 | 20alpha-hydroxysteroid dehydrogenase |
analysis |
the enzyme is a marker for the murine X-zone |
| 1.1.1.152 | 3alpha-hydroxy-5beta-androstane-17-one 3alpha-dehydrogenase |
analysis |
selective microquantitation of steroid substrates |
| 1.1.1.159 | 7alpha-hydroxysteroid dehydrogenase |
analysis |
assay for stereospecific labeling of coenzymes NADP+ and NADPH |
| 1.1.1.162 | erythrulose reductase |
analysis |
assay development for microdetection of D-erythrulose in catabolic pathway analysis |
| 1.1.1.17 | mannitol-1-phosphate 5-dehydrogenase |
analysis |
application of CRISPRi-dCas9 technique for gene repression |
| 1.1.1.18 | inositol 2-dehydrogenase |
analysis |
determination of urinary myo-inositol by an improved enzymatic cycling method |
| 1.1.1.2 | alcohol dehydrogenase (NADP+) |
analysis |
the enzyme is utilized in a dehydrogenase-acetone NADP-regeneration system for the enzymatic preparative-scale production of 12-ketochenodeoxycholic acid, overview |
| 1.1.1.205 | IMP dehydrogenase |
analysis |
real-time reverse-transcription PCR assay for mRNA quantification of isoforms IMPDH1 and IMPDH2 in blood samples and cultured cells. Limits of detection and quantification are 10 and 1000 copies of cDNA per reaction, respectively |
| 1.1.1.233 | N-acylmannosamine 1-dehydrogenase |
analysis |
quantitative determination of N-acetylneuraminic acid |
| 1.1.1.238 | 12beta-hydroxysteroid dehydrogenase |
analysis |
potential application in quantification of 12beta-hydroxyl groups in di- and trisubstituted bile acids |
| 1.1.1.25 | shikimate dehydrogenase (NADP+) |
analysis |
usage of Escherichia coli shikimate dehydrogenase as sensor reaction for determination of the cytosolic NADPH/NADP ratio in Saccharomyces cerevisiae, quantitative measurements of physiological variables in the cytosolic compartment by GC-MS/MS, cytosolic NADPH/NADP ratio in batch experiments, overview. The steady state sensor reaction based cytosolic free NADPH/NADP ratio is 15.6 |
| 1.1.1.250 | D-arabinitol 2-dehydrogenase |
analysis |
the specificity of the enzyme makes it useful for the development of a simple and specific method for the measurement of D-arabinitol, a metabolite of the pathogenic Candida spp. which has been described as a marker for disseminated candidiasis |
| 1.1.1.261 | sn-glycerol-1-phosphate dehydrogenase |
analysis |
structural and metabolic studies of bacterial and eucaryal phopholipids |
| 1.1.1.27 | L-lactate dehydrogenase |
analysis |
CpLDH with APAD+ may be useful as a diagnostic tool for detection of protozoan parasite Cryptosporidium |
| 1.1.1.27 | L-lactate dehydrogenase |
analysis |
construction of multiplexed direct electron transfer-type lactate and glucose sensors using a fusion enzyme between L-lactate oxidase from Aerococcus viridans, A96L/N212K mutant, which is minimized in its oxidase activity and b-type cytochrome protein. The sensors achieve simultaneous detection of lactate and glucose without cross-talking error, with the detected linear ranges of 0.5-20 mM for lactate and 0.1-5 mM for glucose, sensitivities of 4.1 nA/mM x mm2 for lactate and 56 nA/mM x mm2 for glucose, and limit of detections of 0.41 mM for lactate and 0.057 mM for glucose |
| 1.1.1.27 | L-lactate dehydrogenase |
analysis |
reproducible and validated LDH assay optimized for several cell types for application in clinical medicine and biomedical sciences. Assay is cost effective and allows for experiment-specific optimization |
| 1.1.1.270 | 3beta-hydroxysteroid 3-dehydrogenase |
analysis |
enzyme can be used for reconstitution of 4-methyl sterol demethylations of cholesterol biosynthesis from lanosterol |
| 1.1.1.284 | S-(hydroxymethyl)glutathione dehydrogenase |
analysis |
direct enzymatic assay of formaldehyde dehydrogenase permits screening of yeast colonies |
| 1.1.1.284 | S-(hydroxymethyl)glutathione dehydrogenase |
analysis |
the enzyme is useful for direct detection of formaldehyde in air by a novel NAD+- and glutathione-independent formaldehyde dehydrogenase-based biosensor, the sensor depends on the enzymatic conversion of the analyte to formic acid, method development, overview |
| 1.1.1.284 | S-(hydroxymethyl)glutathione dehydrogenase |
analysis |
the enzyme is useful in a formaldehyde-selective biosensor using NAD+- and glutathione-dependent recombinant formaldehyde dehydrogenase as a bio-recognition element immobilized on the surface of Si/SiO2/Si3N4 structure |
| 1.1.1.284 | S-(hydroxymethyl)glutathione dehydrogenase |
analysis |
usage of the enzyme in a bi-enzyme biosensor based on NAD+- and glutathione-dependent recombinant formaldehyde dehydrogenase activity and diaphorase activity for a formaldehyde assay, overview |
| 1.1.1.30 | 3-hydroxybutyrate dehydrogenase |
analysis |
construction of a biosensor for amperometric sensing of beta-hydroxybutyrate using MXene nanosheets of type Ti3C2Tx modified with beta-hydroxybutyrate dehydrogenase. The MXene-based biosensor operates best at a potential of -0.35 V (vs. Ag/AgCl), displays a wide linear range (0.36 to 17.9 mM), a sensitivity of 0.480 microA per mM and cm, and a low detection limit (45 microM). The biosensor can be applied to the determination of beta-hydroxybutyrate in (spiked) serum samples |
| 1.1.1.333 | decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase |
analysis |
developed of an assay method based on the visualization of mycobacterium replication within host cells and application for the search of compounds that are able to chase the pathogen from its hideout |
| 1.1.1.341 | CDP-abequose synthase |
analysis |
selection and use of primers to target defined regions of the abequose and paratose synthase genes responsible for biosynthesis of the oligosaccharide repeating units of the 0-antigenic lipopolysaccharide, in order to differentiate Salmonella serogroups. In a polymerase chain reaction assay utilizing these rjb-specific primers, all of the 40 salmonellae belonging to serogroups B, C2, and D plus A could accurately be identified among a total of 123 clinical isolates tested. No false-positive reactions were detected |
| 1.1.1.37 | malate dehydrogenase |
analysis |
use of the thermostable enzyme from Vulcanithermus medioatlanticu DSM 14978 opens broad possibilities for the application of malate dehydrogenase as an analytical reagent and creation on biosensors for biochemical and cliniucal tests |
| 1.1.1.374 | UDP-N-acetylglucosamine 3-dehydrogenase |
analysis |
high-throughput chromatographic analysis of UDPGlcNAc in a complex matrix of deproteinized cell extract |
| 1.1.1.380 | L-gulonate 5-dehydrogenase |
analysis |
YjjN can be applied for a quantitative L-galactonate and L-gulonate detection in a coupled reaction with diaphorase |
| 1.1.1.40 | malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) |
analysis |
squential fluorometric quantification of malic acid enantiomers in a single line flow-injection system using immobilized-enzyme reactors. An immobilized D -malate dehydrogenase (EC 1.1.1.83) reactor and an immobilized L-malate dehydrogenase (EC 1.1.1.40) reactor are introduced into the flowline in series. Sample and coenzyme (NAD+ or NADP+) are injected into the flow line by an open sandwich method. D -Malate is selectively oxidized by EC 1.1.1.83 when NAD+ is injected with a sample. When NADP+ is injected with a sample, L -malate is oxidized only by 1.1.1.40. NADH or NADPH produced by the immobilized-enzyme reactors is monitored fluorometrically at 455 nm |
| 1.1.1.414 | L-galactonate 5-dehydrogenase (NAD+) |
analysis |
YjjN can be applied for a quantitative L-galactonate and L-gulonate detection in a coupled reaction with diaphorase |
| 1.1.1.42 | isocitrate dehydrogenase (NADP+) |
analysis |
simultaneous detection, quantitation and purification of glucose 6-phosphate dehydrogenase, malic enzyme, and NADP-dependent isocitrate dehydrogenase by blue native gel electrophoresis |
| 1.1.1.47 | glucose 1-dehydrogenase [NAD(P)+] |
analysis |
enzyme can be used for glucose determination |
| 1.1.1.47 | glucose 1-dehydrogenase [NAD(P)+] |
analysis |
usage for quantitative determination of glucose in clinical tests and in the food industry |
| 1.1.1.47 | glucose 1-dehydrogenase [NAD(P)+] |
analysis |
use of glucose dehydrogenase in enzyme cycling method for measurement of allantoin in human serum |
| 1.1.1.48 | D-galactose 1-dehydrogenase |
analysis |
determination of lactose using a biosensor made of immobilized beta-galctosidase-galactose dehydrogenase fusion enzyme |
| 1.1.1.48 | D-galactose 1-dehydrogenase |
analysis |
determination of galactose in various hepatic diseases and galactosaemia in clinical biochemistry |
| 1.1.1.50 | 3alpha-hydroxysteroid 3-dehydrogenase (Si-specific) |
analysis |
replacement of hsdA gene by the green fluorescent protein gene inserted downstream from the hsdA regulatory region and use of the resulting strain as fluorescence based biosensor system for steroid determination. With this cell-based system, testosterone can be determined in a range between 57 and 450 ng/ml, estradiol between 1.6 and 12.8 ng/ml, and cholesterol between 19.3 and 154.4 ng/nl. The sensitivity of this bioassay can be further increased by using only the cytosol of the mutant. With the resulting cell-free system testosterone is determined in a range between 28 and 219 pg/ml, estradiol between 0.029 and 0.430 fg/ml, and cholesterol between 9.7 and 77.2 fg/ml. The recovery ratio of the extraction is around 95% and the maximum fluorescence signals are obtained as early as after 30 min. Limitations of the established steroid biosensor system are quenching at higher steroid concentrations and the relatively high background of fluorescence |
| 1.1.1.50 | 3alpha-hydroxysteroid 3-dehydrogenase (Si-specific) |
analysis |
engineering of 3alpha-hydrosteroid biosensor for androsterone determination by immobilizing the enzyme 3alpha-hydroxysteroid dehydrogenase in a composite electrode platform constituted of a mixture of multi-walled carbon nanotubes, octylpyridiniumhexafluorophosphate ionic liquid and NAD+ cofactor.This configuration allows the fast, sensitive and stable electrochemical detection of the NADH generated in the enzyme reaction. Reaction is linear for androsterone in the 0.510 microM concentration range. The detection limit achieved is 0.15 microM |
| 1.1.1.58 | tagaturonate reductase |
analysis |
aldonate estimation |
| 1.1.1.6 | glycerol dehydrogenase |
analysis |
glycerol dehydrogenase can be immobilised in a polycarbamoyl sulfonate-hydrogel and used as a sensor for glycerol |
| 1.1.1.6 | glycerol dehydrogenase |
analysis |
development of an integrated multienzyme electrochemical biosensor for the determination of glycerol in wines. The biosensor is based on the glycerol dehydrogenase/diaphorase bienzyme system. The enzyme system is immobilized together with the mediator tetrathiafulvalene on a 3-mercaptopropionic acid self-assembled monolayer-modified gold electrode by using a dialysis membrane |
| 1.1.1.6 | glycerol dehydrogenase |
analysis |
the recombinant chimeric fusion enzyme GDH-NOX has a potential application for quick glycerol analysis and dioxyacetone biosynthesis |
| 1.1.1.6 | glycerol dehydrogenase |
analysis |
assay for triglycerides. Triglycerides are hydrolysed to glycerol and fatty acids by lipoprotein lipase followed by the oxidation of glycerol to dihydroxyacetone with simultaneous production of NADH by glycerol dehydrogenase. Addition of 2-(2-methoxy-4-nitrophenyl)-3-(4-nitrophenyl)-5-(2,4-disulfophenyl)-2H-tetrazolium monosodium salt (WST-8) to the reaction mixture removes NADH, allowing the reaction to complete while showing stoichiometric production of reduced WST-8. The reaction is linear up to 6.4mM, no interference by 2.5 g/l haemoglobin, 65 microM free bilirubin and 359 microM conjugated bilirubin is observed |
| 1.1.1.6 | glycerol dehydrogenase |
analysis |
GldA shows a strong intrinsic fluorescence at 320 nm, when excited at 280 nm. The fluorescence intensity decreases in the presence of NAD+, NADH, and dihydroxyacetone, the substrate and products for GldA, which allows to determine the dissociation constants for those molecules as 110.6 microM, 9,1 microM, 33.3 mM, respectively |
| 1.1.1.6 | glycerol dehydrogenase |
analysis |
accurate, simple and sensitive method for the quantitative analysis of triglycerides. Assay for triglycerides using glycerol dehydrogenase and a water-soluble formazan dye, WST-8 |
| 1.1.1.61 | 4-hydroxybutyrate dehydrogenase |
analysis |
dipstick assay for the detection of gamma-hydroxybutyrate in alcoholic beverages |
| 1.1.1.67 | mannitol 2-dehydrogenase |
analysis |
sensitive and specific photometric determination of mannitol in human serum |
| 1.1.1.69 | gluconate 5-dehydrogenase |
analysis |
enzymatic quantification of 5-keto-D-gluconate |
| 1.1.1.83 | D-malate dehydrogenase (decarboxylating) |
analysis |
sequential fluorometric quantification of malic acid enantiomers in a single line flow-injection system using immobilized-enzyme reactors. An immobilized D-malate dehydrogenase (EC 1.1.1.83) reactor and an immobilized L-malate dehydrogenase (EC 1.1.1.40) reactor are introduced into the flowline in series. Sample and coenzyme (NAD+ or NADP+) are injected into the flow line by an open sandwich method. D-Malate is selectively oxidized by EC 1.1.1.83 when NAD+ is injected with a sample. When NADP+ is injected with a sample, L -malate is oxidized only by 1.1.1.40. NADH or NADPH produced by the immobilized-enzyme reactors is monitored fluorometrically at 455 nm |
| 1.1.1.85 | 3-isopropylmalate dehydrogenase |
analysis |
the cloned 3-isopropylmalate dehydrogenase gene can be used as a genetic marker in constructing vectors in Citrobacter freundii |
| 1.1.1.85 | 3-isopropylmalate dehydrogenase |
analysis |
cloning of a fragment of DNA carrying the gene for 3-IMDH will be useful in the development of transformation methods in Candida albicans |
| 1.1.1.85 | 3-isopropylmalate dehydrogenase |
analysis |
use of the cloned 3-isopropylmalate dehydrogenase gene for the development of a new host-vector system for cloning in Acetobacter aceti |
| 1.1.1.93 | tartrate dehydrogenase |
analysis |
determination of L-(+)-tartrate in wines and juices |
| 1.1.1.93 | tartrate dehydrogenase |
analysis |
quantification of L-tartrate in wine by a stopped-flow injection system with an immobilized enzyme reactor and fluorescence detection, the enzyme is immobilized on aminopropyl-controlled pore glass beads with glutaraldehyde |
| 1.1.1.B57 | 1-tetralone reductase [NADPH] |
analysis |
miniaturized assay for quantitative high-throughput screening, by monitoring NADPH oxidation as a decrease in A340 using a spectrophotometer |
| 1.1.2.3 | L-lactate dehydrogenase (cytochrome) |
analysis |
development of a amperometric biosensor selective to L-lactate, bioanalytical properties are very fast response and high sensitivity and selectivity |
| 1.1.2.3 | L-lactate dehydrogenase (cytochrome) |
analysis |
sensitive and stable visualization of enzyme activity in cell-free extracts or during purification by by formation of precipitates of Berlin blue |
| 1.1.2.3 | L-lactate dehydrogenase (cytochrome) |
analysis |
enzymatic oxidation of L-lactate catalyzed by flavocytochrome b2 and coupled with formazan production from nitrotetrazolium blue can be used for L-lactate assay in food samples. A high correlation between results of the proposed method and reference ones proves the possibility to use flavocytochrome b2-catalysed reaction for enzymatic measurement of L-lactate in biotechnology and food chemistry |
| 1.1.2.3 | L-lactate dehydrogenase (cytochrome) |
analysis |
lactate-selective microbial sensor based on flavocytochrome b2-enriched yeast cells |
| 1.1.3.10 | pyranose oxidase |
analysis |
immobilization of enzyme on carbon nanotubes for application as enzymatic electrodes for enzyme-based biosensors and biofuel cells. The sensitivities of the covalent attachment, enzyme coating, and enzyme precipitate coating electrodes without 4-benzoquinone are 0.27, 0.76 and 3.7 mA/M/cm2, while covalent attachment, enzyme coating and enzyme precipitate coating electrodes in presence of 4-benzoquinone show 25, 25, and 60mA/M/cm2 of sensitivities, respectively. The maximum power densities of biofuel cells using covalent attachment, enzyme coating and enzyme precipitate coating electrodes without 4-benzoquinone are 41, 47 and 53 microW/cm2, while covalent attachment, enzyme coating and enzyme precipitate coating electrodes with 4-benzoquinone show 260, 330 and 500 microW/cm2, respectively |
| 1.1.3.13 | alcohol oxidase |
analysis |
enzyme may be useful for the colorimetric determination of methanol, ethanol, or other alcohols |
| 1.1.3.13 | alcohol oxidase |
analysis |
the enzyme is useful for construction of ethanol biosensors |
| 1.1.3.13 | alcohol oxidase |
analysis |
a dual biosensor analysis system based on alcohol oxidase and alcohol dehydrogenase for the simultaneous analysis of methanolethanol mixtures is developed. The alcohol dehydrogenase biosensor quantifies only the ethanol in the range 0.3-8 mmol/l without interference from methanol in concentrations as high as 100 mmol/l. The alcohol oxidase biosensor is able to respond to both analytes in the range 3-70 mmol/l for methanol and 15110 mmol/l for ethanol. The concentration of ethanol and methanol from the sample is determined by processing analytical signals obtained from both biosensors |
| 1.1.3.13 | alcohol oxidase |
analysis |
amperometric sensor for ethanol based on one-step electropolymerization of thionine-carbon nanofiber nanocomposite containing alcohol oxidase. The ethanol biosensor can monitor ethanol ranging from 0.002 to 0.252 mM with a detection limit of 0.0017 mM. It displays a rapid response, an expanded linear response range as well as excellent reproducibility and stability |
| 1.1.3.13 | alcohol oxidase |
analysis |
an amperometric biosensor for ethanol monitoring is developed and optimised. The biosensor uses poly(neutral red), as redox mediator, which is electropolymerised on carbon film electrodes and alcohol oxidase from Hansenula polymorpha as recognition element, immobilised by cross-linking with glutaraldehyde in the presence of bovine serum albumin as carrier protein. The biosensor is used for the determination of ethanol in Portuguese red and white wines. No significant interferences were found from compounds usually present in wine |
| 1.1.3.13 | alcohol oxidase |
analysis |
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts |
| 1.1.3.13 | alcohol oxidase |
analysis |
selection procedure for isolation of the mutant forms of AOX, and their use as a suitable bioelement for biosensor technologies. The created biosensor based on mAOX (from the strain CA2) was characterised by a decreased affinity towards analyzed substrates and slightly increased Vmax. The operational stability of the mAOX-immobilised electrode is not affected and remains similar to an electrode based on the natural enzyme. The described methodology opens up the possibility for construction of biosensors appropriate for precise, rapid, and cheap analysis of target analytes, e.g. ethanol in real samples of wines, beers or fermentation cultures |
| 1.1.3.13 | alcohol oxidase |
analysis |
the enzyme is useful in alcohol biosensor applications |
| 1.1.3.13 | alcohol oxidase |
analysis |
fabrication of a self-powered ethanol biosensor comprising a beta-NAD+-dependent alcohol dehydrogenase bioanode and a bienzymatic alcohol oxidase and horseradish peroxidase biocathode. beta-NAD+ is regenerated by means of a toluidine blue modified redox polymer. The biofuel cell exhibits an open-circuit voltage of approximately 660 mV and can be used as self-powered device for the determination of the ethanol content in liquor |
| 1.1.3.13 | alcohol oxidase |
analysis |
the behaviour of commercially available AOx and ADH enzymes is studied in 12 different biosensor designs towards butanol-1 detection in liquid media. Four out of twelve proposed designs demonstrate a good signal reproducibility and linear response (up to 14.6 mM of butanol) under very low applied potentials (from -0.02 to -0.32 V) |
| 1.1.3.15 | (S)-2-hydroxy-acid oxidase |
analysis |
development of a lactate biosensor through immobilization of lactate oxidase in an albumin and mucin composed hydrogel by gluitaraldehyde cross-linking and trapping between two polycarbonate membranes. Hydrogen peroxide produced is detected on a platinum electrode. The response time of the sensor to 0.010 mM lactate requires 90 s to give a 100% steady-state response of 0.079 microA. Linear behavior is obtained between0.7 microM and 1.5 mM. The detection limit calculated from the signal to noise ratio was 0.7 microM |
| 1.1.3.15 | (S)-2-hydroxy-acid oxidase |
analysis |
construction of a D-Lactate electrochemical biosensor. The electrode for detection of D-lactate is prepared by immobilizing dye-linked D-LDH and multi-walled carbon nanotube within Nafion membrane. The electrode response to D-lactate is linear within the concentration range of 0.03-2.5 mM, and it shows little reduction in responsiveness after 50 days |
| 1.1.3.17 | choline oxidase |
analysis |
investigation of an acetylcholinesterase/choline oxidase-based amperometric biosensor as a liqid chromatography detector for acetylcholine determination in brain tissue |
| 1.1.3.17 | choline oxidase |
analysis |
two-enzyme sensor for determination of choline esters prepared by covalent co-immobilization of choline oxidase and butyrylcholinesterase |
| 1.1.3.17 | choline oxidase |
analysis |
the immobilized enzyme is used in amperometric biosensors for choline detection, method evaluation |
| 1.1.3.17 | choline oxidase |
analysis |
determination of lead ions by inhibition of choline oxidase enzyme using an amperometric choline biosensor. Choline oxidase is immobilized on a glassy carbon electrode modified with multiwalled carbon nanotubes through cross-linking with glutaraldehyde. In the presence of choline oxidase, choline is enzymatically oxidized into betaine at -0.3 V versus Ag/AgCl reference electrode, lead ion inhibition of enzyme activity causing a decrease in the choline oxidation current. Under the best conditions for measurement of the lowest concentrations of lead ions, the choline oxidase/multiwalled carbon nanotubes/glassy carbon electrode gives a linear response from 0.1 to 1.0 nM Pb2+ and a detection limit of 0.04 nM |
| 1.1.3.17 | choline oxidase |
analysis |
development of a metal composite material based on zirconium dioxide decorated gold nanoparticles (ZrO2 at AuNPs), copper (I) oxide at manganese (IV) oxide (Cu2O at MnO2) and immobilized choline oxidase (ChOx) onto a glassy carbon electrode (GCE) (ChOx/Cu2O at MnO2-ZrO2 at AuNPs/GCE) for enhancing the electro-catalytic property, sensitivity and stability of the amperometric choline biosensor. The ChOx/Cu2O at MnO2-ZrO2 at AuNPs/GCE displays a good electrocatalytic response to the oxidation of the byproduct H2O2 from the choline catalyzed reaction. The modified electrode also provides a wide linear range of choline concentration from 0.5 to 1000.0 microM with good sensitivity and low detection limit (0.3 microM). The apparent Michaelis-Menten constant is 0.08 mM with Imax of 0.67 microA. The choline biosensor presents high repeatability, good reproducibility, long time of use and good selectivity without interfering effects from possible electroactive species such as ascorbic acid, aspirin, amoxicillin, caffeine, dopamine, glucose, sucrose and uric acid |
| 1.1.3.17 | choline oxidase |
analysis |
facile and sensitive colorimetric biosensor based on DNAzyme-choline oxidase coupling used for the determination of choline. In this method, choline oxidase produces H2O2 and betaine in the presence of choline and oxygen, then, the DNAzyme converts colorless ABTS into green ABTS+ radicals. The linear range and the limit of detection of this biosensor are 0.1-25 microM and 22 nM. Choline measurement using this biosensor shows satisfactory selectivity and repeatability. Its recovery is 96.95-107.73% in biological samples |
| 1.1.3.2 | L-lactate oxidase |
analysis |
development of a bienzyme fiberoptic sensor for flow injection analysis of L-lactate using lactate oxidase and peroxidase immobilized on a polyamide membrane. Hydrogen peroxide generated by lactate oxidase is substrate of peroxidase in presence of luminol. For the sensor strip, the detection limit is 250 pmol lactate, with 1.7% variation for 10 replicates using 6.25 nmol lactate |
| 1.1.3.2 | L-lactate oxidase |
analysis |
engineering the enzyme in order to minimize the effects of oxygen interference on sensor strips. Mutant A96L shows a drastic reduction in oxidase activity using molecular oxygen as the electron acceptor and a small increase in dehydrogenase activity employing an artificial electron acceptor. After immobilization on a screen-printed carbon electrode and under argon or atmospheric conditions, the response current increases linearly from 0.05 to 0.5 mM L-lactate for both wild-type and mutant A96L. Under atmospheric conditions, the response of wild-type electrode is suppressed by 9-12% due to oxygen interference. The mutant maintains 56-69% of the response current at the same L-lactate level and minimizes the relative bias error to -19% from -49% of wild-type |
| 1.1.3.21 | glycerol-3-phosphate oxidase |
analysis |
co-immobilization of lipase, glycerol kinase, glycerol-3-phosphate oxidase and peroxidase on to aryl amine glass beads affixed on plastic strip for determination of triglycerides in serum |
| 1.1.3.21 | glycerol-3-phosphate oxidase |
analysis |
building of an improved amperometric triglyceride biosensor using lipase nanoparticles/glycerol kinase nanoparticles/glycerol 3-phosphate oxidase nanoparticles/pencil graphite electrode as the working electrode, Ag/AgCl as the standard electrode and Pt wirebas auxiliary electrode. The biosensor shows optimum response within 2.5 s at a pH 7.0 and temperature of 35°C. It measures current due to electrons generated at 0.1 V against Ag/AgCl, from H2O2, which is produced from triolein by coimmobilized enzyme nanoparticles. Analytical recovery of added triolein in serum is 98.01. The biosensor can be employed for determination of triglycerides in the serum of apparently healthy subject and persons suffering from hypertriglyceridemia |
| 1.1.3.29 | N-acylhexosamine oxidase |
analysis |
enzyme may by useful for measurement of N-acetyl-beta-D-glucosaminidase |
| 1.1.3.38 | vanillyl-alcohol oxidase |
analysis |
development of a screening assay for the substrate specificity of para-phenol oxidases based on the detection of hydrogen peroxide using the ferric-xylenol orange complex method |
| 1.1.3.4 | glucose oxidase |
analysis |
coupling of the enzyme with Fenton's reagent used for the determination of glucose produced as a result of the hydrolysis of cellobiose catalyzed by beta-glucosidase |
| 1.1.3.4 | glucose oxidase |
analysis |
phosphate sensor consisting of glucose oxidase coimmobilized with glutaraldehyde with maltose phosphorylase and bovine serum albumin |
| 1.1.3.4 | glucose oxidase |
analysis |
enzyme immobilized in Bombyx mori silk fibroin membrane applied to glucose sensor |
| 1.1.3.4 | glucose oxidase |
analysis |
immobilized enzyme on polyacrylamide employed for the determination of glucose concentration in blood sera |
| 1.1.3.4 | glucose oxidase |
analysis |
biosensor system prepared for continuous flow analysis of enzyme activity |
| 1.1.3.4 | glucose oxidase |
analysis |
application in glucose biosensors. An unmediated, reagentless glucose biosensor is prepared with two polyethylenimine/glucose oxidase bilayers-modified pyrolytic graphite electrodes. A calibration linear range of glucose is 0.5-8.9 mM with a detection limit of 0.05 mM and sensitivity of 0.76 microA per mM |
| 1.1.3.4 | glucose oxidase |
analysis |
the enzym eis used in a model system to study physiological effects of hepatic H2O2 release on rat liver |
| 1.1.3.4 | glucose oxidase |
analysis |
the enzyme finds wide application in food industry and clinical analysis |
