F5152
D-Fructose Dehydrogenase from Gluconobacter industrius
lyophilized powder, 400-1,200 units/mg protein
Synonym(s):
D-Fructose:(acceptor) 5-oxidoreductase
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Product Name
D-Fructose Dehydrogenase from Gluconobacter industrius, lyophilized powder, 400-1,200 units/mg protein
form
lyophilized powder
specific activity
400-1,200 units/mg protein
mol wt
140 kDa
composition
Protein, ≤10% Lowry
shipped in
wet ice
storage temp.
−20°C
Quality Level
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Application
D-fructose dehydrogenase is used as a biosensor to detect the presence of D-fructose.
Fructose dehydrogenase (FDH) is used in a number of basic research projects to examine the electrochemical properties of enzyme-catalyzed electrode reactions called bioelectrocatalysis. D-fructose dehydrogenase has been used in a study that contributed towards a convenient method for measuring rare sugars, monosaccharides, for applications in the bio-industry. A direct electron transfer reaction of d-fructose dehydrogenase adsorbed on a porous carbon electrode surface has been used to describe a batch-type coulometric d-fructose biosensor.
Biochem/physiol Actions
D-fructose dehydrogenase catalyzes the oxidation of D-fructose to 5-keto-D-fructose.
Fructose dehydrogenase (FDH) is a heterotrimeric membrane-bound enzyme commonly seen in various Gluconobacter sp. especially in Gluconobacter japonicus (Gluconobacter industrius). It has a molecular mass of ca. 140 kDa, consisting of subunits I (67kDa), II (51 kDa), and III (20 kDa) and catalyzes the oxidation of D-fructose to produce 5-keto-D-fructose. The enzyme is a flavoprotein-cytochrome c complex with subunits I and II covalently bound to flavin adenine dinucleotide (FAD) and heme C as prosthetic groups, respectively.
Other Notes
One unit will convert 1.0 μmole D-fructose to 5-ketofructose per min at pH 4.5 at 37 °C.
Physical form
Lyophilized powder containing citrate-phosphate buffer salts, TRITON® X-100, and stabilizer
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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Seiya Tsujimura et al.
Analytical chemistry, 81(22), 9383-9387 (2009-11-17)
This paper describes a batch-type coulometric d-fructose biosensor based on direct electron transfer reaction of d-fructose dehydrogenase (FDH) adsorbed on a porous carbon electrode surface. The adsorbed-FDH electrodes catalyzed the electrochemical two-electron oxidation of d-fructose to 5-keto-d-fructose without a mediator.
Susana Campuzano et al.
Bioelectrochemistry (Amsterdam, Netherlands), 63(1-2), 199-206 (2004-04-28)
A bienzyme biosensor for the simultaneous determination of glucose and fructose was developed by coimmobilising glucose oxidase (GOD), fructose dehydrogenase (FDH), and the mediator, tetrathiafulvalene (TTF), by cross-linking with glutaraldehyde atop a 3-mercaptopropionic acid (MPA) self-assembled monolayer (SAM) on a
M Boujtita et al.
Applied biochemistry and biotechnology, 89(1), 55-66 (2000-11-09)
A mediated modified carbon paste and renewable surface electrode for fructose amperometric measurement based on D-fructose dehydrogenase (FDH) was prepared and optimized. Commercially available ferrocene (FcH) and hydroxymethyl ferrocene (FcCH2OH) were used as mediators. The substituted FcH showed better linearity
Hongxiang Hui et al.
Pancreas, 38(6), 706-712 (2009-06-10)
We sought to develop an assay to measure circulating fructose concentrations in pancreatic cancer patients. Using fructose dehydrogenase-catalyzed conversion of d-fructose to 5-ketofructose, followed by quantitation of MTT [3-(4,5-dimethylthiaze-syl)-2,5-diphenyltetrazolium bromide] formazan production by direct spectrophotometry, an assay to measure serum
Takeo Miyake et al.
Journal of the American Chemical Society, 133(13), 5129-5134 (2011-03-12)
Nanostructured carbons have been widely used for fabricating enzyme-modified electrodes due to their large specific surface area. However, because they are random aggregates of particular or tubular nanocarbons, the postmodification of enzymes to their intrananospace is generally hard to control.
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