1.1.1.1 alcohol dehydrogenase biotechnology possible usage of the enzyme in bioindustrial processes and as biosensor 1.1.1.6 glycerol dehydrogenase biotechnology production of 1,2-propanediol in yeast 1.1.1.6 glycerol dehydrogenase biotechnology GlyDH is active with immobilized N6-CM-NAD+, suggesting that N6-CM-NAD+ can be immobilized on an electrode to allow TmGlyDH activity in a system that reoxidizes the cofactor electrocatalytically, development of a bioelectrocatalytic reactor 1.1.1.8 glycerol-3-phosphate dehydrogenase (NAD+) biotechnology deletion of the NAD+-dependent glycerol-3-phosphate dehydrogenase gene in an industrial ethanol-producing strain and expression of either the non-phosphorylating NADP+-dependent glyceraldehyde-3-phosphate dehydrogenase from Bacillus cereus, strain AG2A, or the NADP+-dependent glyceraldehyde-3-phosphate dehydrogenase GAPDH from Kluyveromyces lactis, strain AG2B, in the deletion strain. Recombinant strain AG2A exhibits a 48.70% decrease in glycerol production and a 7.60% increase in ethanol yield relative to the amount of substrate consumed, while recombinant strain AG2B exhibits a 52.90% decrease in glycerol production and a 7.34% increase in ethanol yield relative to the amount of substrate consumed, compared with the wild-type strain. The maximum specific growth rates of the recombinant AG2A and AG2B are higher than that of the gpd2 deletion strain and are indistinguishable compared with the wild-type strain in anaerobic batch fermentations 1.1.1.9 D-xylulose reductase biotechnology pretreatment of sugarcane bagasse hydrolysate to eliminate toxic compounds unsuitable for use as growth medium in xylitol production. Optimization of adsorption time, type of acid used, concentration and charcoal leads to a high ratio of xylose reductase, EC1.1.1.21, to xylitol dehydrogenase, EC1.1.1.9, of 4.5 1.1.1.9 D-xylulose reductase biotechnology strain overexpressing enzyme has improved xylitol productivity, production of up to 57g/l xylitol from 225 g/l D-arabitol, via D-xylulose 1.1.1.9 D-xylulose reductase biotechnology cells previously grown in sugar cane bagasse hemicellulosic hydrolysate are effective in enhancing xylitol production by keeping the xylose reductase (EC 1.1.1.21) activity at high levels, reducing the xylitol dehydrogenase (EC 1.1.1.9) activity and increasing xylitol volumetric productivity (26.5%) with respect to the inoculum cultivated in semidefined medium.Therefore, inoculum adaptation to sugar cane bagasse hemicellulosic hydrolysate is an important strategy to improve xylitol productivity 1.1.1.9 D-xylulose reductase biotechnology the productivity and yield of xylitol fermentation by the XYL2-disrupted mutant are remarkably enhanced by screening suitable cosubstrates and optimizing the process 1.1.1.11 D-arabinitol 4-dehydrogenase biotechnology the gene can be expressed in agronomic plants to withstand abiotic stresses 1.1.1.21 aldose reductase biotechnology use of enzyme in production of xylitol from bagasse hydrolysate, enzyme activity is higher in medium containing acetic acid than in control medium 1.1.1.21 aldose reductase biotechnology ALDRXV4 gene from Xerophyta viscosa is a potential candidate for developing stress-tolerant crop plants 1.1.1.27 L-lactate dehydrogenase biotechnology a chimeric bifunctional enzyme composing of galactose dehydrogenase from Pseudomonas fluorescens and lactate dehydrogenase from Bacillus stearothermophilus is successfully constructed. The chimeric enzyme is able to recycle NAD with a continuous production of lactate without any externally added NADH 1.1.1.27 L-lactate dehydrogenase biotechnology genetic tools for use in Clostridium thermocellum that allow creation of unmarked mutations while using a replicating plasmid. The strategy employs counter-selections developed from the native C. thermocellum hpt gene and the Thermoanaerobacterium saccharolyticum tdk gene and is used to delete the genes for both lactate dehydrogenase (Ldh) and phosphotransacetylase (Pta) 1.1.1.28 D-lactate dehydrogenase biotechnology construction of a metabolically engineered Saccharomyces cerevisiae that produces D-lactic acid efficiently. Two copies of the D-lactate dehydrogenase gene from Leuconostoc mesenteroides subsp. mesenteroides strain NBRC3426 are introduced into the genome. The D-lactate production reaches 61.5 g/l, the amount of glucose being transformed into D-lactic acid is 53.0% under non-neutralizing conditions. The D-lactic acid is of extremely high optical purity of 99.9% or higher 1.1.1.34 hydroxymethylglutaryl-CoA reductase (NADPH) biotechnology overexpression of HMG1 is the most effective among all other genes in both hosts Saccharomyces cerevisiae ATCC 200589 and ATCC 76625 for prenyl alcohol production 1.1.1.36 acetoacetyl-CoA reductase biotechnology construction an evaluation of a polyhydroxybutyrate production system using Zea mays chloroplasts expressing the enzyme from Alcaligenes eutrophus 1.1.1.37 malate dehydrogenase biotechnology MDH is widely used in coenzyme regeneration, antigen immunoassays and bioreactors 1.1.1.40 malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) biotechnology malic enzyme is a pivotal regulator in lipid accumulation in green microalga Chlorella pyrenoidosa, and presents a breakthrough of generating ideal algal strains for algal nutrition and biofuels 1.1.1.42 isocitrate dehydrogenase (NADP+) biotechnology the icdA gene is a potentially valuable tool for modulating citric acid production by metabolic engineering 1.1.1.44 phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating) biotechnology immobilization of 6PDGH on ASMNPs can be an effective way for its biotechnological and biosensor applications 1.1.1.47 glucose 1-dehydrogenase [NAD(P)+] biotechnology larger scale production of NAD(P)H in bioreactors by usage of the enzyme, a thermostable enzyme is advantageous 1.1.1.47 glucose 1-dehydrogenase [NAD(P)+] biotechnology azoreductase and glucose 1-dehydrogenase are coupled for both continuous generation of the cofactor NADH and azo dye removal. The results show that 85% maximum relative activity of azoreductase in an integrated enzyme system is obtained at the conditions: 1 U azoreductase: 10 U glucose 1-dehydrogenase, 250 mM glucose, 1.0 mM NAD+ and 150 microM methyl red 1.1.1.47 glucose 1-dehydrogenase [NAD(P)+] biotechnology Escherichia coli transformants are prepared coexpressing the yeast reductase YOL151W and Bacillus GDH for the production of Ethyl (R, S)-4-chloro-3-hydroxybutanoate 1.1.1.47 glucose 1-dehydrogenase [NAD(P)+] biotechnology (±)-ethyl mandelate are important intermediates in the synthesis of numerous pharmaceuticals. Efficient routes for the production of these derivatives are highly desirable. A co-immobilization strategy is developed to overcome the issue of NADPH demand in the short-chain dehydrogenase/reductase (SDR) catalytic process. The SDR from Thermus thermophilus HB8 and the NAD(P)-dependent glucose dehydrogenase (GDH) from Thermoplasma acidophilum DSM 1728 are co-immobilized on silica gel. This dual-system offers an efficient route for the biosynthesis of (+/-)-ethyl mandelate 1.1.1.47 glucose 1-dehydrogenase [NAD(P)+] biotechnology co-immobilization of ketoreductase (KRED) and glucose dehydrogenase (GDH) on highly cross-linked agarose (sepharose) via affnity interaction between His-tagged enzymes (six histidine residues on the N-terminus of the protein) and agarose matrix charged with nickel (Ni2+ ions). Immobilized enzymes are applied in a set of biotransformation reactions in repeated batch flow-reactor mode. Immobilization reduces the requirement for cofactor (NADP+) and allows the use of higher substrate concentration in comparison with free enzymes 1.1.1.47 glucose 1-dehydrogenase [NAD(P)+] biotechnology enzymatic reduction of the nicotinamide biomimetic cofactors 1-phenethyl-1,4-dihydropyridine-3-carboxamide using glucose dehydrogenase mutant I192T/V306I provides a regeneration system for artificial cofactors. The I192T/V306I mutant enzyme shows 10fold higher activity with 1-phenethyl-1,4-dihydropyridine-3-carboxamide compared with the wild-type enzyme. Using this engineered variant in combination with an enoate reductase from Thermus scotoductus results in an enzyme-coupled regeneration process for biomimetic cofactor without ribonucleotide or ribonucleotide analogue and full conversion of 10 mM 2-methylbut-2-enal with 1-phenethyl-1,4-dihydropyridine-3-carboxamide as cofactor 1.1.1.47 glucose 1-dehydrogenase [NAD(P)+] biotechnology production of tert-butyl (3R,5S)-6-chloro-3,5-dihydroxyhexanoate, an important chiral intermediate for the synthesis of rosuvastatin, using carbonyl reductase coupled with glucose dehydrogenase. A recombinant Escherichia coli strain harboring carbonyl reductase R9M and glucose dehydrogenase is constructed with high carbonyl reduction activity and cofactor regeneration efficiency. The recombinant Escherichia coli cells are applied for the efficient production of tert-butyl (3R,5S)-6-chloro-3,5-dihydroxyhexanoate with a substrate conversion of 98.8%, a yield of 95.6% and an enantiomeric excess of more than 99.0% under 350 g/l of tert-butyl (S)-6-chloro-5-hydroxy-3-oxohexanoate after 12 h reaction. A substrate fed-batch strategy is further employed to increase the substrate concentration to 400 g/l resulting in an enhanced product yield to 98.5% after 12 h reaction in a 1 l bioreactor. Meanwhile, the space-time yield is 1182.3 g/l*day 1.1.1.47 glucose 1-dehydrogenase [NAD(P)+] biotechnology the robust stability of the enzyme makes it an attractive participant for cofactor regeneration on practical applications, especially for the catalysis implemented in acidic pH and high temperature 1.1.1.48 D-galactose 1-dehydrogenase biotechnology design and synthesis by protein molecular modelling and ligand docking of several chimeric mimodye-ligands comprising a NAD-pseudomimetic moiety of anthraquinone diaminobenzosulfonic acid and a galactosyl-mimetic moiety of 2-amino-2-deoxygalactose or shikimic acid for usage as tailored ligands in selective affinity chromatography during enzyme purification/production, immobilization on a gel resin, overview 1.1.1.50 3alpha-hydroxysteroid 3-dehydrogenase (Si-specific) biotechnology transfection of cells with plasmids encoding a 3alpha-hydroxysteroid dehydrogenase-Del1 deposition domain fusion protein. The Del1 deposition domain immobilizes the enzyme in the extracellular matrix without interfering with its enzymatic activity. Extracellular matrix conditioned by cells transfected with 3alpha-hydroxysteroid dehydrogenase-Del1 deposition domain fusion significantly suppresses the growth of otherwise untreated LNCaP cells 1.1.1.67 mannitol 2-dehydrogenase biotechnology recombinant Escherichia coli expressing the enzyme from Leuconostoc pseudomesenteroides expressing strong catalytic activity of an NADH-dependent reduction of D-fructose to D-mannitol in cell extracts of the recombinant Escherichia coli strain can be utilized as an efficient biocatalyst for D-mannitol formation 1.1.1.81 hydroxypyruvate reductase biotechnology conditional and specific down-regulation of farnesyltransferase in canola using the AtHPR1 promoter driving an RNAi construct results in yield protection against drought stress in the field 1.1.1.90 aryl-alcohol dehydrogenase biotechnology biotechnological production of vanillin 1.1.1.95 phosphoglycerate dehydrogenase biotechnology metabolic engineering of Corynebacterium glutamicum for L-serine production by enzyme overexpression 1.1.1.118 glucose 1-dehydrogenase (NAD+) biotechnology immobilization of GDH1 on the surface of a graphite felt electrode, construction and optimization of an electrochemical bioreactor, co-immobilization of 3,4-dihydroxybenzaldehyde as mediator allows the system to operate at 0.2 V and increases both the activity (2.4-times) and the stability of the immobilized enzyme by 2.2-times, the immobilized enzyme is termed IMGDH1 1.1.1.122 D-threo-aldose 1-dehydrogenase biotechnology the purified alpha1,2-fucosidase and L-fucose dehydrogenase have sufficiently high activities in phosphate-buffered saline (pH 7.0) at 37 °C, making it possible to develop a one-pot method for the quantitative determination of 2'-fucosyllactose in fermentation samples. The application of this method is more convenient for quantifying 2'-fucosyllactose in a variety of samples that may be obtained from different phases of the biotechnological production of this oligosaccharide. The method is useful for simple and rapid screening of active variants during the development of any industrially important microbial strain producing 2'-fucosyllactose 1.1.1.138 mannitol 2-dehydrogenase (NADP+) biotechnology optimization of culture conditions for production of mannitol, best conditions give 213 g/l mannitol from 250 g/l fructose 1.1.1.149 20alpha-hydroxysteroid dehydrogenase biotechnology a process is developed that that allows the production of 20alpha- dihydrodydrogesterone at technical scale (several grams of 20a-DHD per week and fermenter). Genetic improvement of the production strain, an increase of substrate solubility by addition of ß-cyclodextrin, and the development of a sophisticated high-cell density fermentation at pilot scale are employed. By usage of the exemplary substrate progesterone, it is hsown that this innovative fission yeast-based whole cell biotransformation process is transferable to the conversion of other AKR1C1 substrates without special adaptation 1.1.1.149 20alpha-hydroxysteroid dehydrogenase biotechnology an aldo-keto reductases-dependent whole-cell biotransformation process is established that can be used for production of human aldo-keto reductases metabolites on a large scale 1.1.1.194 coniferyl-alcohol dehydrogenase biotechnology the recombinant Rhodococcus opacus strain PD630, expressing the coniferyl alcohol dehydrogenase from Rhodococcus sp. strain HR199, together with the coniferyl aldehyde dehydrogenase, and the vanillyl alcohol oxidase, the latter from Penicillium simplicissimus strain CBS, is able to produce vanillin from ferulic acid and eugenol 1.1.1.195 cinnamyl-alcohol dehydrogenase biotechnology the spruce CAD promoter represents a valuable tool for research and biotechnology applications related to xylem and wood 1.1.1.216 farnesol dehydrogenase (NADP+) biotechnology recombinant farnesol dehydrogenase may provide a useful molecular tool in manipulating juvenile hormone biosynthesis to generate transgenic plants for pest control 1.1.1.227 (-)-borneol dehydrogenase biotechnology the gene encoding the borneol dhdrogenase is a target for metabolic engineering for improvement of essential oil production 1.1.1.244 methanol dehydrogenase biotechnology metabolic engineering of Escherichia coli for high yield production of succinic acid driven by methanol. When methanol assimilation module is introduced into succinic acid producing Escherichia coli by employing the NAD-dependent methanol dehydrogenase from Bacillus methanolicus and ribulose monophosphate pathway from different donor organisms, succinic acid yield is increased from 0.91 g/g to 0.98 g/g with methanol as an auxiliary substrate under the anaerobic fermentation 1.1.1.255 mannitol dehydrogenase biotechnology constitutive expression of enzyme in Nicotiana tabacum confers significantly enhanced resistance to Alternaria alternata, but not to Cercospora nicotianae 1.1.1.267 1-deoxy-D-xylulose-5-phosphate reductoisomerase biotechnology DXR plays a role in the methyl-D-erythritol 4-phosphate pathway, which is responsible for the biosynthesis of a substantial number of natural compounds of biological and biotechnological importance and is considered as a target to develop new herbicides and antimicrobial drugs 1.1.1.274 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming) biotechnology enzyme is a target for the construction of a NADH-utilizing mutant strain in the industrial production of vitamin C 1.1.1.275 (+)-trans-carveol dehydrogenase biotechnology applicability of strains with high enzyme content or recombinant overproducing strains for production of (+)-carvone, which is used as a flavor compound 1.1.1.301 D-arabitol-phosphate dehydrogenase biotechnology expression of the D-arabitol phosphate dehydrogenase gene of Enterococcus avium in the D-ribulose- and D-xylulose-producing strain results in a strain of Bacillus subtilis capable of converting D-glucose to D-arabitol with a high yield (28%) and little by-product formation 1.1.1.312 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase biotechnology production of 2-pyrone-4,6-dicarboxylic acid from protocatechuate as a precursor for biopolymers 1.1.1.312 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase biotechnology engineering plants with the proposed de-novo PDC pathway provides an avenue to enrich biomass with a value-added co-product while simultaneously improving biomass quality for the supply of fermentable sugars. Implementing this strategy into bioenergy crops has the potential to support existing microbial fermentation approaches that exploit lignocellulosic biomass feedstocks for PDC production 1.1.3.2 L-lactate oxidase biotechnology coupling of mutant S218C in 94% yield to maleimide-activated methoxypoly(ethylene glycol) 5000. PEGylation causes about 30% small decrease in the specific activity of the S218C mutant, and it does not change the protein stability 1.1.3.4 glucose oxidase biotechnology the enzyme encapsulated in the liposomes composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine is a useful biocatalyst for the prolonged glucose oxidation 1.1.3.4 glucose oxidase biotechnology GOX is the most widely used enzyme for the development of electrochemical glucose biosensors and biofuel cell in physiological conditions 1.1.3.4 glucose oxidase biotechnology transgenic expression of glucose oxidase may be deployed to improve cold tolerance potential of higher plants 1.1.3.4 glucose oxidase biotechnology bacteriostatic agent. The combination of different concentrations of glucose oxidase and glucose could significantly inhibit the growth of Agrobacterium and Escherichia coli in logarithmic phase during the fermentation process 1.1.3.4 glucose oxidase biotechnology the enzyme is used for a number of applications in biotechnology and clinical diagnostics 1.1.3.6 cholesterol oxidase biotechnology biocatalysis, industrial steroid drug production, steroid production as diagnostic tool 1.1.3.6 cholesterol oxidase biotechnology Cholesterol oxidase has two major biotechnological applications, i.e. in the determination of serum (and food) cholesterol levels and as biocatalyst providing valuable intermediates for industrial steroid drug production 1.1.3.9 galactose oxidase biotechnology technology: creating hybrid-system by immobilization of GOase on gold electrode, technology enables creation of biosensors and biofuel cells and studying electrochemically the catalytic mechanism of reactions for which free radicals and electron-transfer reactions are involved 1.1.3.10 pyranose oxidase biotechnology studies on biosensors and biofuel cell anodes 1.1.3.10 pyranose oxidase biotechnology studies on stabilization of enzymatic activity by immobilization 1.1.3.10 pyranose oxidase biotechnology biocatalyst for carbohydrate transformations toward higher-value products 1.1.3.10 pyranose oxidase biotechnology P2Ox is a biocatalyst with high potential for biotransformations of carbohydrates and in synthetic carbohydrate chemistry. P2Ox is useful as bioelement in biofuel cells, replacing glucose oxidase 1.1.3.10 pyranose oxidase biotechnology enzyme P2O is a useful biocatalyst in several biotechnological applications, including biotransformation of carbohydrates such as D-glucose and D-galactose to generate 2-oxo-sugars that can be further reduced at the C1 position to yield D-fructose and D-tagatose, respectively 1.1.3.13 alcohol oxidase biotechnology in the core promoter and 5' untranslated region of the gene, mutations in the TATA box motif, regions downstream of the transcription start site or next to the start codon in the 5' UTR have a significant effect on expression. Mutations in most other regions are tolerated. These neutral core promoter positions, not affecting expression, can be exploited to introduce extrinsic sequence elements such as cloning sites and bacterial promoters 1.1.3.17 choline oxidase biotechnology the immobilized enzyme is used in amperometric biosensors 1.1.3.17 choline oxidase biotechnology development and application of enzyme-based gas sensor 1.1.3.17 choline oxidase biotechnology development and applications of biosensors 1.1.3.17 choline oxidase biotechnology development of inhibition biosensors for pesticide determination, butyrylcholinesterase/choline oxidase enzyme electrode and tyrosine electrode compared 1.1.3.21 glycerol-3-phosphate oxidase biotechnology the enzyme is used as triglyceride biosensor when immobilized on a pencil graphite electrode 1.1.3.47 5-(hydroxymethyl)furfural oxidase biotechnology development of a facile gene shuffling approach to rapidly combine stabilizing mutations in a one-pot reaction. This allows the identification of the optimal combination of several beneficial mutations. The approach quickly discriminates stable and active multi-site variants, making it a very useful addition to FRESCO (framework for rapid enzyme stabilization by computational libraries) method 1.1.5.2 glucose 1-dehydrogenase (PQQ, quinone) biotechnology bioengineering of water-soluble isozyme PQQGDH-B production at industrial level 1.1.5.2 glucose 1-dehydrogenase (PQQ, quinone) biotechnology engineering of the soluble enzyme GDH-B to enable the electron transfer to the electrode in absence of artificial electron mediator by mimicking the domain structure of the quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni, which is composed of a PQQ-containing catalytic domain and a cytochrome c domain 1.1.5.2 glucose 1-dehydrogenase (PQQ, quinone) biotechnology engineering PQQ glucose dehydrogenase with improved substrate specificity 1.1.5.2 glucose 1-dehydrogenase (PQQ, quinone) biotechnology enzyme has a great potential for application as glucose sensor constituent 1.1.5.2 glucose 1-dehydrogenase (PQQ, quinone) biotechnology optimization of an expression system using Pichia pastoris for use in industrial level production 1.1.5.2 glucose 1-dehydrogenase (PQQ, quinone) biotechnology surface charge engineering of the enzyme for optimization of downstream processing in large scale enzyme production 1.1.5.2 glucose 1-dehydrogenase (PQQ, quinone) biotechnology the enzyme is used for glucose biosensor diagnosis 1.1.5.2 glucose 1-dehydrogenase (PQQ, quinone) biotechnology a Glucose sensitive biosensor containing GDH immobilized on Prussian blue (PB)-modified graphite electrode is designed. Properties of the biosensor are investigated in the cathodic and anodic response detection regions. It is shown, that anodic response of the biosensor is sum of two signals: direct electron transport from reduced pyrroloquinoline quinine to the electrode and by formation of the pyrroloquinoline quinone-oxygen-Prussion blue-carbon ternary complex. Cathodic response of the biosensor is based on the oxidation of the reduced pyrroloquinoline quinone by Prussian blue-oxygen-Prussian blue complex. Electrochemical regeneration of the enzyme does not produce free hydrogen peroxide 1.1.5.2 glucose 1-dehydrogenase (PQQ, quinone) biotechnology application as biosensor 1.1.5.B3 quinone dependent L-lactate dehydrogenase biotechnology the PQQ-dependent lactate dehydrogenase from Gluconobacter is capable of direct electron transfer at carbon and gold electrodes, which makes it useful for application in biosensors or biofuel cells, overview 1.1.5.4 malate dehydrogenase (quinone) biotechnology the disruption of the mqo gene results in increased L-lysine production. The mutation supports industrial levels of L-lysine production in Corynebacterium glutamicum 1.1.5.9 glucose 1-dehydrogenase (FAD, quinone) biotechnology construction of a direct electron transfer bioanode composed of FADGDH and a single-walled carbon nanotube. The bioanode exhibits a large anodic current due to the enzymatic reaction (1 mA/cm) at ambient temperature and works at 70°C for 12 h 1.1.5.14 fructose 5-dehydrogenase biotechnology an automated, enzymatic insulin assay is developed. Principle: Fructose is produced by the action of inulinase on inulin present in the sample. The resulting fructose reacts with D-fructose dehydrogenase in the presence of the oxidized form of 1-methoxy-5-methylphenazinium methylsulfate (1-m-PMS) to produce the reduced form of 1-m-PMS. Reduced 1-m-PMS acts on dissolved oxygen to produce hydrogen peroxide, which, through the action of peroxidase, oxidatively condenses N-ethyl-N-(2-hydroxy-3-sulfopropyl)-m-toluidine and 4-aminoantipyrine to transform them into quinoneimine dye. The absorbance of the quinoneimine dye is measured spectrophotometrically to determine the concentration of inulin in the sample. The new enzymatic assay offers a more convenient and more accurate measurement of inulin and may be suitable for routine procedures by automated analyzers in clinical laboratories 1.1.5.14 fructose 5-dehydrogenase biotechnology multi-walled carbon nanotubes synthesized on platinum plate (MWCNTs/Pt) electrode are immediately immersed into solutions of FDH to immobilize the enzyme onto electrode surfaces. Thereafter, a well-defined catalytic oxidation current based on FDH is observed from ca. -0.15V, which is close to the redox potential of heme c as a prosthetic group of FDH. From an analysis of a plot of the catalytic current versus substrate, the calibration range for the fructose concentration is up to ca. 40 mmol/dm3, and the apparent Michaelis-Menten constant is evaluated to be 11 mmol/l. The obtained results are useful in applications to prepare the third-generation biosensors and other future bioelectrochemical devices 1.1.5.14 fructose 5-dehydrogenase biotechnology using fructose dehydrogenase-catalyzed conversion of d-fructose to 5-ketofructose, followed by quantitation of MTT [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide] formazan production by direct spectrophotometry, an assay to measure serum fructose concentration is developed. The fructose dehydrogenase-based enzymatic assay correlates highly with gas chromatography-mass spectroscopic analysis of serum fructose. The assay is highly specific, exhibits no cross-reactivity with other sugars and is easy to perform 1.1.9.1 alcohol dehydrogenase (azurin) biotechnology co-immobilization of enzyme with redox polymer poly(vinylpyridine) complex functionalized with osmium bis(bipyridine) chloride on an electrode. The enzyme electrode readily oxidizes primary alcohols and secondary alcohols with maximum current densities varying between 0.43 and 0.98 A per m2 depending on the substrate and the operation temperature. The enzyme electrode is enantioselective in the oxidation of secondary alcohols. A strong preference is observed for the (S)-2-alcohols, the enantioselectivity increases with increasing chain length. The enantiomeric ratio E increases from 13 for (R,S)-2-butanol to approximately 80 for (R,S)-2-heptanol and (R,S)-2-octanol 1.1.99.18 cellobiose dehydrogenase (acceptor) biotechnology the Pichia expression system is well suited for high-level production of recombinant enzyme 1.1.99.18 cellobiose dehydrogenase (acceptor) biotechnology biosensors with a cellulosic carrier containing self-assembled nanocomposites of CDH and other enzymes allow the determination of 100 nm dopamine 1.1.99.18 cellobiose dehydrogenase (acceptor) biotechnology cellobiose dehydrogenase is a promising enzyme for the development of biosensors and biofuel cells 1.1.99.18 cellobiose dehydrogenase (acceptor) biotechnology class II cellobiose dehydrogenases are potential candidates for glucose biosensors and biofuel cell anodes 1.1.99.29 pyranose dehydrogenase (acceptor) biotechnology PDH could be a very interesting alternative to pyranose oxidase for applications in biotechnology or biofuel cells, electrical wiring of the enzyme bound to graphite rod electrodes is studied 1.1.99.29 pyranose dehydrogenase (acceptor) biotechnology PDH is an alternative to pyranose oxidase for applications in biotechnology or biofuel cells, electrical wiring of the enzyme bound to graphite rod electrodes is studied 1.1.99.29 pyranose dehydrogenase (acceptor) biotechnology PDH can be very efficiently wired with osmium polymers having E°' values close to that of PDH 1.1.99.30 2-oxo-acid reductase biotechnology preparative scale production of pyruvate from (R)-lactate in an enzyme-membrane reactor with coupled electrochemical regeneration of the artificial mediator anthraquinone-2,6-disulfonate, process modeling and calculation 1.1.99.35 soluble quinoprotein glucose dehydrogenase biotechnology application as biosensor. Application for glucose sensing. s-GDH can be applied for the ultrasensitive detection of PQQ down to picomolar concentrations 1.2.1.8 betaine-aldehyde dehydrogenase biotechnology BADH overexpression in maize is beneficial for drought tolerance and the three transgenic maize lines can be used for further breeding experiments. The agronomic traits of transgenic maize are not affected by the overexpression of BADH 1.2.1.8 betaine-aldehyde dehydrogenase biotechnology overexpression of AMADHs with high BADH activities is an important strategy to genetically engineer Solanaceae crop plants, such as tomato and tobacco, to produe glycine betaine 1.2.1.11 aspartate-semialdehyde dehydrogenase biotechnology development of lysine-overproducing strains