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 1.1.1.6 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 1.1.1.11 D-arabinitol 4-dehydrogenase analysis potential of using arabitol dehydrogenase from the non-virulent enteric bacterium, Escherichia colistrain C, as a plant selectable marker 1.1.1.12 L-arabinitol 4-dehydrogenase analysis enzymatic cycling assay for nicotinic acid adenine dinucleotide phosphate 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 1.1.1.25 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 1.1.1.27 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 1.1.1.30 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 1.1.1.37 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 1.1.1.40 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 1.1.1.42 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 0.5–10 microM concentration range. The detection limit achieved is 0.15 microM 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 1.1.1.58 tagaturonate reductase analysis aldonate estimation 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 1.1.1.107 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 1.1.1.119 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 1.1.1.122 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 1.1.1.205 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 1.1.1.250 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 1.1.1.270 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 1.1.1.333 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 1.1.1.374 UDP-N-acetylglucosamine 3-dehydrogenase analysis high-throughput chromatographic analysis of UDP–GlcNAc 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 1.1.1.414 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 1.1.2.3 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 1.1.3.2 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 1.1.3.4 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 1.1.3.4 glucose oxidase analysis the enzyme is useful in designing of biosensors for use in clinical, biochemical, and diagnostic assays 1.1.3.4 glucose oxidase analysis the enzyme might by useful in designing of biosensors for use in clinical, biochemical, and diagnostic assays 1.1.3.4 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 1.1.3.4 glucose oxidase analysis the enzyme is useful as biosensor for glucose detection 1.1.3.4 glucose oxidase analysis GOx is the main component in glucose biosensors for determination of glucose in industrial solutions and in body fluids such as blood and urine 1.1.3.4 glucose oxidase analysis te enzyme is used on electrode surfaces of biosensors 1.1.3.4 glucose oxidase analysis the enzyme GOx is applied in biosensor technologies 1.1.3.4 glucose oxidase analysis mutant glucose oxidase (B11-GOx) is obtained from directed protein evolution and wild-type enzyme. Higher glucose oxidation currents are obtained from B11-GOx both in solution and polymer electrodes compared to wild type enzyme. Improved electrocatalytic activity towards electrochemical oxidation of glucose from the mutant enzyme. The enzyme electrode with the mutant enzyme B11-GOx shows a faster electron transfer indicating a better electronic interaction with the polymer mediator. Promising application of enzymes developed by directed evolution tailored for the applications of biosensors and biofuel cells 1.1.3.B5 eugenol 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 1.1.3.6 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 1.1.3.6 cholesterol oxidase analysis the cholesterol oxidase-immobilized polyacrylonitrile hollow fiber may have an industrial or medical application for cholesterol determination or oxidation 1.1.3.6 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 1.1.3.6 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 1.1.3.6 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 1.1.3.6 cholesterol oxidase analysis simple, reliable, fast and reproducible method to prepare cholesterol oxidase electrodes is described 1.1.3.6 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 1.1.3.6 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 1.1.3.9 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 1.1.3.9 galactose oxidase analysis galactose oxidase is an important component in electrochemical biosensors of galactose that are used for various biotechnology applications 1.1.3.9 galactose oxidase analysis the enzyme can be useful in biosensors 1.1.3.9 galactose oxidase analysis a photoelectrochemical biosensor for quantitative detection of galactose is obtained immobilizing galactose oxidase on TiO2 nanorod arrays modified F-doped tin oxide (FTO) electrode. The direct electron transfer to galactose oxidase is achieved. The generated photocurrent of the stable platform is significantly enhanced after the addition of galactose in solution and the photocurrent intensity shows linear relationship with the galactose concentration. CaCl2, uric acid and ascorbic acid have no interference with the detection of galactose. The sensor can be reused and applied to measure the concentration of galactose in lactose-free milk 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