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19359

Sigma-Aldrich

Glucose dehydrogenase from Pseudomonas sp.

greener alternative

powder, white, ≥200 U/mg

Synonyme(s) :

GDH

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About This Item

Numéro CAS:
9028-53-9
Numéro de classification (Commission des enzymes):
1.1.1.47 (BRENDA, IUBMB)
Numéro CE :
232-836-9
Numéro MDL:
MFCD00131181
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

bacterial (Pseudomonas spp.)

Niveau de qualité

100

Forme

powder

Activité spécifique

≥200 U/mg

Caractéristiques du produit alternatif plus écologique

Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

sustainability

Greener Alternative Product

Couleur

white

Autre catégorie plus écologique

, Enabling

Température de stockage

−20°C

Description générale

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.

Actions biochimiques/physiologiques

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.

Définition de l'unité

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

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

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Muhammad Nadeem Zafar et al.
Analytical chemistry, 84(1), 334-341 (2011-11-19)
A new extracellular flavin adenine dinucleotide (FAD)-dependent glucose dehydrogenase from Glomerella cingulata (GcGDH) was electrochemically studied as a recognition element in glucose biosensors. The redox enzyme was recombinantly produced in Pichia pastoris and homogeneously purified, and its glucose-oxidizing properties on
Selective Access to All Four Diastereomers of a 1, 3-Amino Alcohol by Combination of a Keto Reductase-and an Amine Transaminase-Catalysed Reaction
Kohls H, et al.
Advanced Synthesis & Catalysis, 357(8), 1808-1814 (2015)
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
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
Basic Biotechnology, 370-370 (2006)
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