1.1.5.14: fructose 5-dehydrogenase
This is an abbreviated version!
For detailed information about fructose 5-dehydrogenase, go to the full flat file.
Word Map on EC 1.1.5.14
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1.1.5.14
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electrode
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biosensors
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amperometric
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gluconobacter
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5-ketofructose
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oxydans
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biocathode
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bioelectrode
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bioanode
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tetrathiafulvalene
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5-keto-d-fructose
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biotechnology
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food industry
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analysis
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synthesis
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biofuel production
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industry
- 1.1.5.14
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electrode
-
biosensors
-
amperometric
-
gluconobacter
- 5-ketofructose
-
oxydans
-
biocathode
-
bioelectrode
-
bioanode
-
tetrathiafulvalene
- 5-keto-d-fructose
- biotechnology
- food industry
- analysis
- synthesis
- biofuel production
- industry
Reaction
Synonyms
D-fructose dehydrogenase, dehydrogenase, fructose 5- (acceptor), FDH, FdhL, FdhS, fdhSCL, fructose 5-dehydrogenase, fructose dehydrogenase
ECTree
1.1.5.14 fructose 5-dehydrogenaseAdvanced search results
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Application on EC 1.1.5.14 - fructose 5-dehydrogenase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
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the enzyme is a satisfactory reagent for microdetermination of D-fructose
biofuel production
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an enzymatic gold bioanode fabricated with fructose dehydrogenase and a polyaniline film can be used as a single-compartment fructose biofuel cell
biotechnology
food industry
industry
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direct electron-transfer bioelectrocatalysis can be used in biosensors, biofuel cells and bioreactors, FDH immobilised on Ketjen black electroconductive material produces a catalytic oxidation wave of D-fructose without a mediator, the electron in FDH seems to be directly transferred to the electrode via the heme c site
synthesis
biotechnology
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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
biotechnology
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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
biotechnology
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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
food industry
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the enzyme can be used as biosensor to quantify D-fructose in commercial beverages and honey
food industry
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the enzyme can be used as biosensor to quantify D-fructose in commercial beverages and honey
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synthesis
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Gluconobacter frateurii CHM 43 have D-mannitol dehydrogenase (quinoprotein glycerol dehydrogenase) and flavoprotein D-fructose dehydrogenase in the membranes. When the two enzymes are functional, D-mannitol is converted to 5-keto-D-fructose with 65% yield when cultivated on D-mannitol. 5-Keto-D-fructose production with almost 100% yield is realized with the resting cells
synthesis
Gluconobacter frateurii CHM 43
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Gluconobacter frateurii CHM 43 have D-mannitol dehydrogenase (quinoprotein glycerol dehydrogenase) and flavoprotein D-fructose dehydrogenase in the membranes. When the two enzymes are functional, D-mannitol is converted to 5-keto-D-fructose with 65% yield when cultivated on D-mannitol. 5-Keto-D-fructose production with almost 100% yield is realized with the resting cells
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