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Search term: biotechnology

Results 1 - 100 of 724 > >>
EC Number
Application
Commentary
alcohol dehydrogenase
biotechnology
possible usage of the enzyme in bioindustrial processes and as biosensor
glycerol dehydrogenase
biotechnology
production of 1,2-propanediol in yeast
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
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
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
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
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
aldehyde 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
aldehyde reductase
biotechnology
ALDRXV4 gene from Xerophyta viscosa is a potential candidate for developing stress-tolerant crop plants
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
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)
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
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
acetoacetyl-CoA reductase
biotechnology
construction an evaluation of a polyhydroxybutyrate production system using Zea mays chloroplasts expressing the enzyme from Alcaligenes eutrophus
malate dehydrogenase
biotechnology
MDH is widely used in coenzyme regeneration, antigen immunoassays and bioreactors
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
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
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
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
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
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
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
aryl-alcohol dehydrogenase
biotechnology
biotechnological production of vanillin
phosphoglycerate dehydrogenase
biotechnology
metabolic engineering of Corynebacterium glutamicum for L-serine production by enzyme overexpression
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
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
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 -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
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
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
cinnamyl-alcohol dehydrogenase
biotechnology
the spruce CAD promoter represents a valuable tool for research and biotechnology applications related to xylem and wood
(-)-borneol dehydrogenase
biotechnology
the gene encoding the borneol dhdrogenase is a target for metabolic engineering for improvement of essential oil production
mannitol dehydrogenase
biotechnology
constitutive expression of enzyme in Nicotiana tabacum confers significantly enhanced resistance to Alternaria alternata, but not to Cercospora nicotianae
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
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
(+)-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
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
2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase
biotechnology
production of 2-pyrone-4,6-dicarboxylic acid from protocatechuate as a precursor for biopolymers
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
glucose oxidase
biotechnology
GOX is the most widely used enzyme for the development of electrochemical glucose biosensors and biofuel cell in physiological conditions
glucose oxidase
biotechnology
transgenic expression of glucose oxidase may be deployed to improve cold tolerance potential of higher plants
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
cholesterol oxidase
biotechnology
biocatalysis, industrial steroid drug production, steroid production as diagnostic tool
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
pyranose oxidase
biotechnology
studies on biosensors and biofuel cell anodes
pyranose oxidase
biotechnology
studies on stabilization of enzymatic activity by immobilization
pyranose oxidase
biotechnology
biocatalyst for carbohydrate transformations toward higher-value products
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
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
choline oxidase
biotechnology
the immobilized enzyme is used in amperometric biosensors
choline oxidase
biotechnology
development of inhibition biosensors for pesticide determination, butyrylcholinesterase/choline oxidase enzyme electrode and tyrosine electrode compared
choline oxidase
biotechnology
development and applications of biosensors
choline oxidase
biotechnology
development and application of enzyme-based gas sensor
glucose 1-dehydrogenase (PQQ, quinone)
biotechnology
bioengineering of water-soluble isozyme PQQGDH-B production at industrial level
glucose 1-dehydrogenase (PQQ, quinone)
biotechnology
engineering PQQ glucose dehydrogenase with improved substrate specificity
glucose 1-dehydrogenase (PQQ, quinone)
biotechnology
surface charge engineering of the enzyme for optimization of downstream processing in large scale enzyme production
glucose 1-dehydrogenase (PQQ, quinone)
biotechnology
enzyme has a great potential for application as glucose sensor constituent
glucose 1-dehydrogenase (PQQ, quinone)
biotechnology
optimization of an expression system using Pichia pastoris for use in industrial level production
glucose 1-dehydrogenase (PQQ, quinone)
biotechnology
the enzyme is used for glucose biosensor diagnosis
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
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
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
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
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
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
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
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
cellobiose dehydrogenase (acceptor)
biotechnology
the Pichia expression system is well suited for high-level production of recombinant enzyme
cellobiose dehydrogenase (acceptor)
biotechnology
cellobiose dehydrogenase is a promising enzyme for the development of biosensors and biofuel cells
cellobiose dehydrogenase (acceptor)
biotechnology
class II cellobiose dehydrogenases are potential candidates for glucose biosensors and biofuel cell anodes
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
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
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
pyranose dehydrogenase (acceptor)
biotechnology
PDH can be very efficiently wired with osmium polymers having E' values close to that of PDH
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
formate dehydrogenase
biotechnology
overexpression of the NAD+-dependent formate dehydrogenase in Escherichia coli doubles maximum yield of NADH from 2 to 4 mol NADH/mol glucose consumed
formate dehydrogenase
biotechnology
use of enzyme for regeneration of NADH. Coexpression of alpha-haloketone resistant enzyme mutants and a carbonyl reductase from Kluyveromyces aestuarii for production of ethyl-(S)-4-chloro-3-hydroxybutanoate with optical purity of product of 99% enantiomeric excess, from ethyl-4-chloroacetoacetate
formate dehydrogenase
biotechnology
study on stability of recombinant enzyme in homogeneous aequeous solution, at gas-liquid interfaces in a bubble column, and under shear stress. Level of enzyme stability in solution also depends on the enzyme variant employed. Mutants C23S and C23S/C262A perform much better than wild-type in quiescent solution and reactors with little mechanical stress. Mutant C23S/C262A is less stable than wild-type at high stress levels in the Couette viscometer or the bubble column
formate dehydrogenase
biotechnology
FDH from Candida boidinii is an important biocatalyst for the regeneration of the cofactor NADH in industrial enzyme-catalyzed reductions
formate dehydrogenase
biotechnology
immobilization of enzyme on highly activated glyoxyl agarose, optimization protocol. Optimized enzyme retains 50% of the offered activity and becomes 50times more stable at high temperature and neutral pH. Optimal temperature increases by 10C at pH 4.5. Immobilized enzyme accepts dextran-NAD+ as a substrate, use on ultra-filtration reactors to catalyze the recycling of NAD+
aspartate-semialdehyde dehydrogenase
biotechnology
development of lysine-overproducing strains
formaldehyde dehydrogenase
biotechnology
development of novel formaldehyde-selective amperometric biosensors based on immobilized NAD+- and glutathione dependent formaldehyde dehydrogenase with high selectivity to formaldehyde and a low cross-sensitivity to other substances, the laboratory prototype of the sensor is applied for FA testing in some real samples of pharmaceutical (formidron), disinfectant (descoton forte) and industrial product (formalin)
long-chain acyl-protein thioester reductase
biotechnology
production of jojoba plant wax esters
vanillin dehydrogenase
biotechnology
Amycolatopsis sp. ATCC 39116 vdh mutant represents an optimized and industrially applicable platform for biotechnological production of natural vanillin
coniferyl-aldehyde dehydrogenase
biotechnology
highly efficient two-step biotransformation of eugenol to ferulic acid and further conversion to vanillin in recombinant strains of Escherichia coli. Maximum production rate for ferulic acid at large scale is 14.4 mM per h per liter of culture, yield of 93.3% with respect to the added amount of eugenol
coniferyl-aldehyde dehydrogenase
biotechnology
biotransformation of eugenol to ferulic acid by a recombinant strain of Ralstonia eutropha H16. The gene calB, encoding coniferyl aldehyde dehydrogenase, and ehyAB and calA encoding eugenol hydroxylase and coniferyl alcohol dehydrogenase, respectively, are amplified and combined to construct a catabolic gene cassette. This gene cassette is cloned in the broad-host-range vector pBBR1-JO2 and transferred to Ralstonia eutropha H16. A recombinant strain of Ralstonia eutropha H16 harboring this plasmid expresses functionally active eugenol hydroxylase, coniferyl alcohol dehydrogenase, and coniferyl aldehyde dehydrogenase. Cells of Ralstonia eutropha H16 from the late-exponential growth phase are used asa biocatalysts for the biotransformation of eugenol to ferulic acid. A maximum conversion rate of 2.9 mM of eugenol per h per liter of culture is achieved with a yield of 93.8 mol% of ferulic acid from eugenol within 20 h, without further optimization
glutamyl-tRNA reductase
biotechnology
recombinant Escherichia coli allows efficient production of 5-aminolevulinic acid directly from glucose
malonyl-CoA reductase (malonate semialdehyde-forming)
biotechnology
the crystallographic data indicate how to construct a bispecific cofactor binding site and to engineer a malonyl-CoA into methylmalonyl-CoA reductase for polyester building block production
pyruvate dehydrogenase (acetyl-transferring)
biotechnology
active expression of enzyme from non-halophilic Zymomonas mobilis in the haloarchaeon Haloferax volcanii with no difference in the secondary structure. Post-transcriptional mechanisms in the stationary phase appear to limit the amount of recombinant protein expressed
pyruvate dehydrogenase (acetyl-transferring)
biotechnology
overexpression of enzyme in Lactococcus lactis results in up to eightfold increase in acetaldehyde concentration. However, the observed ethanol concentrations are similar to that of wild-type strain
pyruvate synthase
biotechnology
pyruvate:ferredoxin oxidoreductase PFR1 and [Fe-Fe]-hydrogenase HYDA1 of Chlamydomonas can be coupled for pyruvate-dependent H2 production
acyl-CoA dehydrogenase (NADP+)
biotechnology
optimization of oil-based extended fermentation of recombinant Streptomyces cinnamonensis, expressing the enzyme from Streptomyces collinus, is used to provide methylmalonyl-CoA precursors for monensin biosynthesis, overview
maleylacetate reductase
biotechnology
Sphingobium chlorophenolicum has assembled new catabolic pathways to degrade pentachlorophenol and use the ring-cleavage products as their carbon sources
bilirubin oxidase
biotechnology
the wired' enzyme is superior to pure platinum as a electrocatalyst of the four-electron electroreduction of O2 to water. The 'wired' bilirubin oxidase-coated carbon cathode operates for more than 1 week at 37C in a glucose-containing physiological buffer solution. Key application would be in a glucose-O2 biofuel cell. The cathode is short-lived in serum, losing its electrocatalytic activity in a few hours. The damaging serum component is a product of the reaction of urate and dissolved oxygen. Exclusion of urate, by application of Nafion(TM) film in the cathode, improves the stability in serum
bilirubin oxidase
biotechnology
the enzyme functions effectively as the biocathode of a H2/O2 biofuel cell. It is immmobilized as a multiple layer in a cationic polymer (poly-L-lysine) matrix on an electrode surface. The BOD-modified electrode catalyzes four-electron reduction of O2 to water without any mediator, to produce a diffusion-controlled voltammogram for the O2 reduction in a quiescent solution. Construction of such a multiple enzyme layer is useful for increasing the current density even in direct electron transfer-type bioelectrocatalysis
acyl-CoA oxidase
biotechnology
potential depolluting agent by degradation of oils; several biotechnological applications: production of metabolites, such as citrate, secretion of proteins, degradation of fatty acids
succinate dehydrogenase
biotechnology
a new host-vector system for Mortierella alpina 1S-4, zygomycetes, on the basis of self-cloning for the industrial application of Mortierella transformants is developed. Transformants expressing the Escherichia coli uidA gene encoding beta-glucuronidase by using the mutant H243L as the selectable marker (leading to to carboxin resistance)
alanine dehydrogenase
biotechnology
heterologous expression of the Bacillus subtilis AlaDH in Lactococcus lactis using the promoter of lactate dehydrogenase from Streptococcus thermophilus leads to a better alanine production in the recombinant strain
glutamate dehydrogenase
biotechnology
a strategy to control flocculation is investigated using dimorphic yeast, Benjaminiella poitrasii as a model. Parent form of this yeast (Y) exhibit faster flocculation (11.1 min) than the monomorphic yeast form mutant Y-5 (12.6 min). Flocculation of both Y and Y-5 can be altered by supplementing either substrates or inhibitor of NAD-glutamate dehydrogenase (NAD-GDH) in the growth media. The rate of flocculation is promoted by alpha-ketoglutarate or isophthalic acid and decelerated by glutamate with a statistically significant inverse correlation to corresponding NAD-GDH levels. This opens up new possibilities of using NAD-GDH modulating agents to control flocculation in fermentations for easier downstream processing; the rate of flocculation is promoted by a-ketoglutarate or isophthalic acid and decelerated by glutamate with a statistically significant inverse correlation to corresponding NAD-GDH levels. These interesting findings open up new possibilities of using NAD-GDH modulating agents to control flocculation in fermentations for easier downstream processing
glutamate dehydrogenase
biotechnology
method describes immobilization of enzymes by the maximum amount of subunits and rigidification of the enzyme subunits involved in the immobilization
leucine dehydrogenase
biotechnology
an efficient stereospecific enzymatic synthesis of L-valine, L-leucine, L-norvaline, L-norleucine and L-isoleucine from the corresponding alpha-keto acids by coupling the reactions catalysed by leucine dehydrogenase and glucose dehydrogenase/galactose mutarotase. Giving high yields of L-amino acids, the procedure is economical and easy to perform and to monitor at a synthetically useful scale (1-10 g)
Results 1 - 100 of 724 > >>