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19359

Sigma-Aldrich

Glucose dehydrogenase from Pseudomonas sp.

greener alternative

powder, white, ≥200 U/mg

Synonym(s):

GDH

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10 MG
CN¥3,454.57

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10 MG
CN¥3,454.57

About This Item

CAS Number:
EC Number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

CN¥3,454.57


In StockDetails

New, lower price on this item!

Request a Bulk Order

biological source

bacterial (Pseudomonas spp.)

Quality Level

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

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This Item
G3651P4039P6621
biological source

bacterial (Pseudomonas spp.)

biological source

-

biological source

bacterial (Clostridium perfringens)

biological source

-

specific activity

≥200 U/mg

specific activity

≥50 units/mg protein

specific activity

≥150 units/mg protein

specific activity

≥200 units/mg protein

form

powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

Quality Level

100

Quality Level

200

Quality Level

200

Quality Level

300

color

white

color

-

color

-

color

-

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.[1] It has also been used to regenerate the consumed nicotinamide adenine dinucleotide (NADH) during the removal of pyruvate by lactate dehydrogenase.[2]

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.[3]

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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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Kenneth Lan et al.
Journal of diabetes science and technology, 5(5), 1108-1115 (2011-10-27)
A concept for a tear glucose sensor based on amperometric measurement of enzymatic oxidation of glucose was previously presented, using glucose dehydrogenase flavin adenine dinucleotide (GDH-FAD) as the enzyme. Glucose dehydrogenase flavin adenine dinucleotide is further characterized in this article
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
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)
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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