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Merck

19359

Glucose dehydrogenase from Pseudomonas sp.

greener alternative

powder, white, ≥200 U/mg

Synonyme(s) :

GDH

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A propos de cet article

Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-836-9
MDL number:
Numéro CE :
Specific activity:
≥200 U/mg
Biological source:
bacterial (Pseudomonas spp.)
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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

storage temp.

−20°C

Quality Level

Catégories apparentées

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.

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.

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

Classe de stockage

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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Consulter la Bibliothèque de documents

Basic Biotechnology, 370-370 (2006)
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)
Stefano Ferri et al.
Journal of diabetes science and technology, 5(5), 1068-1076 (2011-10-27)
The evolution from first-generation through third-generation glucose sensors has witnessed the appearance of a number of very diverse oxidoreductases, which vary tremendously in terms of origin, structure, substrate specificity, cofactor used as primary electron acceptor, and acceptable final electron acceptor.
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

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