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CAS-Nummer:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
400-1,200 units/mg protein
form
lyophilized powder
Quality Level
specific activity
400-1,200 units/mg protein
mol wt
140 kDa
composition
Protein, ≤10% Lowry
shipped in
wet ice
storage temp.
−20°C
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.[1] 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.[1]
Physical form
Lyophilized powder containing citrate-phosphate buffer salts, TRITON® X-100, and stabilizer
Other Notes
One unit will convert 1.0 μmole D-fructose to 5-ketofructose per min at pH 4.5 at 37 °C.
Lagerklasse
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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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.
Determination of seminal fructose using D-fructose dehydrogenase.
K Nakashima et al.
Clinica chimica acta; international journal of clinical chemistry, 151(3), 307-310 (1985-10-15)
Shota Kawai et al.
Applied and environmental microbiology, 79(5), 1654-1660 (2013-01-01)
A heterotrimeric flavoprotein-cytochrome c complex fructose dehydrogenase (FDH) of Gluconobacter japonicus NBRC3260 catalyzes the oxidation of d-fructose to produce 5-keto-d-fructose and is used for diagnosis and basic research purposes as a direct electron transfer-type bioelectrocatalysis. The fdhSCL genes encoding the