19359
Glucose dehydrogenase from Pseudomonas sp.
powder, white, ≥200 U/mg
Sinónimos:
GDH
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About This Item
Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-836-9
MDL number:
Nombre del producto
Glucose dehydrogenase from Pseudomonas sp., powder, white, ≥200 U/mg
biological source
bacterial (Pseudomonas spp.)
form
powder
specific activity
≥200 U/mg
greener alternative product characteristics
Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.
sustainability
Greener Alternative Product
color
white
greener alternative category
, Enabling
storage temp.
−20°C
Quality Level
Categorías relacionadas
Application
Glucose dehydrogenase from Pseudomonas sp. has been used for the oxidation of glucose as a part of flow-injection analysis detection. It has also been used to regenerate the consumed nicotinamide adenine dinucleotide (NADH) during the removal of pyruvate by lactate dehydrogenase.
Biochem/physiol Actions
In bacteria, the membrane integrated glucose dehydrogenase catalyses the conversion of glucose to gluconic acid. It uses pyrroloquinoline quinone as a coenzyme. The intracellular glucose dehydrogenase lack this cofactor. It is a nicotinamide adenine dinucleotide (NADH) dependent enzyme.
General description
We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in biofuel cell research. For more information see the article in biofiles.
Other Notes
One unit corresponds to the amount of enzyme which will oxidizes 1 μmole β-D-glucose to D-glucono-δ-lactone per minute at pH 8.0 and 37 °C
Clase de almacenamiento
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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Basic Biotechnology, 370-370 (2006)
Rastislav Monošík et al.
Enzyme and microbial technology, 50(4-5), 227-232 (2012-03-16)
Amperometric glucose biosensors utilizing commercially available FAD-dependent glucose dehydrogenases from two strains of Aspergillus species are described. Enzymes were immobilized on nanocomposite electrode consisting of multi-walled carbon nanotubes by entrapment between chitosan layers. Unlike the common glucose oxidase based biosensor
Busisiwe V Twala et al.
Enzyme and microbial technology, 50(6-7), 331-336 (2012-04-17)
The use of enzymes in industrial applications is limited by their instability, cost and difficulty in their recovery and re-use. Immobilisation is a technique which has been shown to alleviate these limitations in biocatalysis. Here we describe the immobilisation of
Akasit Siriphongphaew et al.
Applied microbiology and biotechnology, 95(2), 357-367 (2012-05-05)
Oxygenases-based Escherichia coli whole-cell biocatalyst can be applied for catalysis of various commercially interesting reactions that are difficult to achieve with traditional chemical catalysts. However, substrates and products of interest are often toxic to E. coli, causing a disruption of
Interference in a glucose dehydrogenase-based glucose meter revisited.
Brian N Kelly et al.
Clinica chimica acta; international journal of clinical chemistry, 413(7-8), 829-830 (2012-02-04)
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