F4892
D-Fructose Dehydrogenase from Gluconobacter sp.
≥20 units/mg solid
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
form
amorphous solid
specific activity
≥20 units/mg solid
mol wt
~140 kDa
shipped in
wet ice
storage temp.
−20°C
General description
Isoelectric point : 5.0 ± 0.1
Michaelis constant : 5 x 10‾3M (D-Fructose)
Inhibitors : Ag+, Hg++, SDS
Optimum pH : 4.0
Optimum temperature : 37°C
pH Stability : pH 4.0 – 6.0 (25°C, 16hr)
Thermal stability : Below 40°C (pH 4.5, 15min)
Michaelis constant : 5 x 10‾3M (D-Fructose)
Inhibitors : Ag+, Hg++, SDS
Optimum pH : 4.0
Optimum temperature : 37°C
pH Stability : pH 4.0 – 6.0 (25°C, 16hr)
Thermal stability : Below 40°C (pH 4.5, 15min)
Application
D-Fructose Dehydrogenase from Gluconobacter sp has been used as a standard in the carbohydrate binding specificity assay and SDS-PAGE (sodium dodecyl sulphate-polyacrylamide gel electrophoresis).
This enzyme is also used in a number of basic research projects to examine the electrochemical properties of enzyme-catalyzed electrode reactions called bioelectrocatalysis.This enzyme is useful for enzymatic determination of D-fructose in clinical analysis.
Biochem/physiol Actions
D-fructose dehydrogenase 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.
Physical form
This product is supplied as an amorphous solid containing ~ 80% stabilizers, sugars, amino acids and BSA.
Other Notes
One unit will convert 1.0 μmole D-fructose to 5-ketofructose per min at pH 4.5 at 37 °C.
Storage Class
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
监管及禁止进口产品
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Kevin R Ramkissoon et al.
PloS one, 8(12), e84508-e84508 (2014-01-05)
The power of genome sequencing depends on the ability to understand what those genes and their proteins products actually do. The automated methods used to assign functions to putative proteins in newly sequenced organisms are limited by the size of
Rapid identification of sequences for orphan enzymes to power accurate protein annotation
Ramkissoon KR, et al.
PLoS ONE, 8(12), e84508-e84508 (2013)
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)
Amperometric flow injection determination of fructose with an immobilized fructose 5-dehydrogenase reactor.
K Matsumoto et al.
Analytical chemistry, 58(13), 2732-2734 (1986-11-01)
J Marcinkeviciene et al.
FEBS letters, 318(1), 23-26 (1993-02-22)
Steady-state kinetic analysis was performed on the reaction between D-fructose and ferricyanide with the quinohemoprotein fructose dehydrogenase from Gluconobacter species. The D-fructose oxidation dependence on the ferricyanide concentration resulted in a series of parallel reciprocal plots, and the reaction was
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