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Search term: analysis

Results 1 - 100 of 1210 > >>
EC Number
Application
Commentary
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
glycerol dehydrogenase
analysis
glycerol dehydrogenase can be immobilised in a polycarbamoyl sulfonate-hydrogel and used as a sensor for glycerol
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
D-arabinitol 4-dehydrogenase
analysis
potential of using arabitol dehydrogenase from the non-virulent enteric bacterium, Escherichia colistrain C, as a plant selectable marker
L-arabinitol 4-dehydrogenase
analysis
enzymatic cycling assay for nicotinic acid adenine dinucleotide phosphate
inositol 2-dehydrogenase
analysis
determination of urinary myo-inositol by an improved enzymatic cycling method
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
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
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
glucose 1-dehydrogenase [NAD(P)+]
analysis
usage for quantitative determination of glucose in clinical tests and in the food industry
glucose 1-dehydrogenase [NAD(P)+]
analysis
use of glucose dehydrogenase in enzyme cycling method for measurement of allantoin in human serum
glucose 1-dehydrogenase [NAD(P)+]
analysis
enzyme can be used for glucose determination
D-galactose 1-dehydrogenase
analysis
determination of lactose using a biosensor made of immobilized beta-galctosidase-galactose dehydrogenase fusion enzyme
D-galactose 1-dehydrogenase
analysis
determination of galactose in various hepatic diseases and galactosaemia in clinical biochemistry
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
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 0.5–10 microM concentration range. The detection limit achieved is 0.15 microM
1-tetralone reductase [NADPH]
analysis
miniaturized assay for quantitative high-throughput screening, by monitoring NADPH oxidation as a decrease in A340 using a spectrophotometer
tagaturonate reductase
analysis
aldonate estimation
4-hydroxybutyrate dehydrogenase
analysis
dipstick assay for the detection of gamma-hydroxybutyrate in alcoholic beverages
mannitol 2-dehydrogenase
analysis
sensitive and specific photometric determination of mannitol in human serum
gluconate 5-dehydrogenase
analysis
enzymatic quantification of 5-keto-D-gluconate
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
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
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
3-isopropylmalate dehydrogenase
analysis
the cloned 3-isopropylmalate dehydrogenase gene can be used as a genetic marker in constructing vectors in Citrobacter freundii
tartrate dehydrogenase
analysis
determination of L-(+)-tartrate in wines and juices
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
pyridoxal 4-dehydrogenase
analysis
the enzyme is useful in determination of vitamin B6 contents, method development, overview
carnitine 3-dehydrogenase
analysis
fluorometric determination of carnitine in serum with immobilized carnitine dehydrogenase and diaphorase
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
D-threo-aldose 1-dehydrogenase
analysis
determination of bound-fucose in biological materials by a coupled enzymatic method in a single buffer system
mannitol 2-dehydrogenase (NADP+)
analysis
determination of D-fructose in the presence of other sugars
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
11beta-hydroxysteroid dehydrogenase
analysis
high-throughput screening for potent and selective inhibitors of 11beta-hydroxysteroid dehydrogenase type I
20alpha-hydroxysteroid dehydrogenase
analysis
the enzyme is a marker for the murine X-zone
3alpha-hydroxy-5beta-androstane-17-one 3alpha-dehydrogenase
analysis
selective microquantitation of steroid substrates
7alpha-hydroxysteroid dehydrogenase
analysis
assay for stereospecific labeling of coenzymes NADP+ and NADPH
erythrulose reductase
analysis
assay development for microdetection of D-erythrulose in catabolic pathway analysis
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
N-acylmannosamine 1-dehydrogenase
analysis
quantitative determination of N-acetylneuraminic acid
12beta-hydroxysteroid dehydrogenase
analysis
potential application in quantification of 12beta-hydroxyl groups in di- and trisubstituted bile acids
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
sn-glycerol-1-phosphate dehydrogenase
analysis
structural and metabolic studies of bacterial and eucaryal phopholipids
3beta-hydroxysteroid 3-dehydrogenase
analysis
enzyme can be used for reconstitution of 4-methyl sterol demethylations of cholesterol biosynthesis from lanosterol
S-(hydroxymethyl)glutathione dehydrogenase
analysis
direct enzymatic assay of formaldehyde dehydrogenase permits screening of yeast colonies
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
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
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
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
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
UDP-N-acetylglucosamine 3-dehydrogenase
analysis
high-throughput chromatographic analysis of UDP–GlcNAc in a complex matrix of deproteinized cell extract
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
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
glucose oxidase
analysis
enzyme immobilized in Bombyx mori silk fibroin membrane applied to glucose sensor
glucose oxidase
analysis
biosensor system prepared for continuous flow analysis of enzyme activity
glucose oxidase
analysis
immobilized enzyme on polyacrylamide employed for the determination of glucose concentration in blood sera
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
glucose oxidase
analysis
phosphate sensor consisting of glucose oxidase coimmobilized with glutaraldehyde with maltose phosphorylase and bovine serum albumin
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
glucose oxidase
analysis
the enzym eis used in a model system to study physiological effects of hepatic H2O2 release on rat liver
glucose oxidase
analysis
co-confined glucose oxidase and horseradish peroxidase bienzyme system as a biosensor for the detection of glucose gives a wider linear range of glucose than for free enzymes in solution
glucose oxidase
analysis
the enzyme is useful as biosensor for glucose detection
glucose oxidase
analysis
the enzyme is useful in designing of biosensors for use in clinical, biochemical, and diagnostic assays
glucose oxidase
analysis
the enzyme might by useful in designing of biosensors for use in clinical, biochemical, and diagnostic assays
glucose oxidase
analysis
the enzyme finds wide application in food industry and clinical analysis
cholesterol oxidase
analysis
platinum electrodes modified with thiolipid/lipid bilayer membranes. Cholesterol oxidase spontaneously inserts into the electrode-supported lipid bilayer membrane from solution and is consequently immobilized to the electrode surface. This electrode architecture may be useful in clinical sensing applications
cholesterol oxidase
analysis
the cholesterol oxidase-immobilized polyacrylonitrile hollow fiber may have an industrial or medical application for cholesterol determination or oxidation
cholesterol oxidase
analysis
the enzyme can be used as cholesterol biosensor co-immobilized with cholesterol esterase on oxygen electrodes, determination of total cholesterol in food samples
cholesterol oxidase
analysis
cholesterol esterase (ChEt) and cholesterol oxidase (ChOx) can be immobilized onto tetraethylorthosilicate derived sol-gel films. These tetraethylorthosilicate sol-gel/ChEt/ChOx enzyme films can be used for the estimation of cholesterol oleate up to 780 mg/dl (mM). These TEOS sol-gel enzyme films provide selectivity towards glucose, lactate, uric acid and ascorbic acid
cholesterol oxidase
analysis
the steady state amperometric measurements of free cholesterol are performed by an enzyme electrode which is developed through electrostatic immobilization of the cholesterol oxidase in poly(vinylferrocenium) perchlorate, PVF+ClO4-, film that is coated on a Pt electrode
cholesterol oxidase
analysis
Cellulomonas enzyme is analytically reliable when used for serum cholesterol determination by the endpoint method. Its analytical performance is equivalent to Streptomyces enzymes and meets the analytical goals. It has an advantage over the other enzymes in that it does not ship in the frozen state
cholesterol oxidase
analysis
simple, reliable, fast and reproducible method to prepare cholesterol oxidase electrodes is described
cholesterol oxidase
analysis
the development of an enzyme-based sensor employing the enzyme ChOx has great potential as a simple and economical sensor system, engineering of the enzyme for electrochemical monitoring of cholesterol, overview
galactose oxidase
analysis
galactose oxidase adsorbed on, and covalently bound to, silica carriers is used for analytical determinations of D-galactose and galactose-containing sugars. Using a flowing oxygen electrode of the Clark-type, sensor system for enzymatic analysis of water solutions of galactose-containing carbohydrates is made. Measurements are taken both in the pulse and continuous modes of a substrate flowing through a column with an immobilized biocatalyst
alcohol oxidase
analysis
enzyme may be useful for the colorimetric determination of methanol, ethanol, or other alcohols
alcohol oxidase
analysis
the enzyme is useful for construction of ethanol biosensors
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
alcohol oxidase
analysis
a dual biosensor analysis system based on alcohol oxidase and alcohol dehydrogenase for the simultaneous analysis of methanol–ethanol 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 15–110 mmol/l for ethanol. The concentration of ethanol and methanol from the sample is determined by processing analytical signals obtained from both biosensors
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
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
alcohol oxidase
analysis
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts; AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts; AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts
alcohol oxidase
analysis
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts
alcohol oxidase
analysis
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts; AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts
alcohol oxidase
analysis
the enzyme is useful in alcohol biosensor applications
(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
choline oxidase
analysis
two-enzyme sensor for determination of choline esters prepared by covalent co-immobilization of choline oxidase and butyrylcholinesterase
choline oxidase
analysis
investigation of an acetylcholinesterase/choline oxidase-based amperometric biosensor as a liqid chromatography detector for acetylcholine determination in brain tissue
choline oxidase
analysis
the immobilized enzyme is used in amperometric biosensors for choline detection, method evaluation
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
N-acylhexosamine oxidase
analysis
enzyme may by useful for measurement of N-acetyl-beta-D-glucosaminidase
paromamine 6'-oxidase
analysis
development of a coupled enzyme assays including 3-(4,5-dimethylthiazolyl-2)-2,5-diphenyltetrazoliumbromide and phenazine methosulfate, resulting in the production of 3-(4,5-dimethylthiazolyl-2)-2,5-diphenyltetrazoliumbromide formazan which can be monitored at 570 nm
6'''-hydroxyneomycin C oxidase
analysis
development of a coupled enzyme assays including 3-(4,5-dimethylthiazolyl-2)-2,5-diphenyltetrazoliumbromide and phenazine methosulfate, resulting in the production of 3-(4,5-dimethylthiazolyl-2)-2,5-diphenyltetrazoliumbromide formazan which can be monitored at 570 nm
glucose 1-dehydrogenase (PQQ, quinone)
analysis
apoenzyme is used as a biological test system for the detection of very low amounts of pyrroloquinoline quinone
glucose 1-dehydrogenase (PQQ, quinone)
analysis
enzyme is used as coupling enzyme for monitoring carbohydrate-transport reactions, the method is particularly suited for determining transport reactions that are not coupled to any form of metabolic energy such as uniport reactions, or for characterizing mutant proteins with a defective energy-coupling mechanism or system with high-affinity constants for sugars
glucose 1-dehydrogenase (PQQ, quinone)
analysis
application of mutant enzyme S231K as a glucose sensor constituent. The mutant has more than 8fold increase in its half-life during the thermal inactivation at 55 C compared with the wild-type enzyme and retains catalytic activity similar to the wild-type enzyme
glucose 1-dehydrogenase (PQQ, quinone)
analysis
because of its high turnover number, PQQ-GDH is proposed as an enzyme label for the development of sensitive electrochemical enzyme-amplified bioaffinity assays. It has, for example, been applied to the amperometric detection of DNA hybrids or sandwich DNA aptamers at the surface of a carbon electrode
alcohol dehydrogenase (quinone)
analysis
construction and evaluation of an ethanol sensor based on the enzyme using direct electron-transfer processes between the polypyrrole entrapped quinohemoprotein alcohol dehydrogenase and a platinum electrode, overview
alcohol dehydrogenase (quinone)
analysis
the enzyme can be used in biosensors, method development, overview
alcohol dehydrogenase (quinone)
analysis
adhA expression is related to the ability to oxidize and grow on ethanol. Differential expression of pyrroloquinoline quinone–alcohol dehydrogenase could be a marker to analyse both growth and oxidation ability in some acetic acid bacteria, especially those of the genus Acetobacter
glucose 1-dehydrogenase (FAD, quinone)
analysis
possible use of the enzyme as amperometric glucose biosensor
Results 1 - 100 of 1210 > >>