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19359

Sigma-Aldrich

Glucose dehydrogenase from Pseudomonas sp.

greener alternative

powder, white, ≥200 U/mg

Sinónimos:

GDH

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About This Item

Número de CAS:
9028-53-9
Comisión internacional de enzimas:
1.1.1.47 (BRENDA, IUBMB)
EC Number:
232-836-9
MDL number:
MFCD00131181
UNSPSC Code:
12352204
NACRES:
NA.54

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

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.

Unit Definition

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

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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
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
Basic Biotechnology, 370-370 (2006)
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)
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
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