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C8868

Sigma-Aldrich

Cholesterol Oxidase from microorganisms

lyophilized powder, ≥50 units/mg protein, recombinant, expressed in E. coli

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Synonym(s):
Cholesterol: oxygen oxidoreductase
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

recombinant

expressed in E. coli

Quality Level

form

lyophilized powder

specific activity

≥50 units/mg protein

mol wt

64 kDa

composition

Protein, ≥15% biuret

storage temp.

−20°C

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This Item
C1235C8649C5421
form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

aqueous solution

specific activity

≥50 units/mg protein

specific activity

≥10 units/mg protein

specific activity

≥20 units/mg protein

specific activity

≥30 units/mg protein (biuret)

mol wt

64 kDa

mol wt

55 kDa

mol wt

~34 kDa

mol wt

62 kDa

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−70°C

composition

Protein, ≥15% biuret

composition

-

composition

protein, 55-65% biuret

composition

-

Application

Cholesterol oxidase has been used in a study to demonstrate that microheterogeneity in hydrophobic-hydrophilic block copolymer systems can be exploited for immobilizing enzymes and to carry out enzymatic reactions. Cholesterol oxidase has also been used in a study that concluded that amphipaths that activate cholesterol might be useful in treating NPC disease.
Cholesterol oxidase is used to determine serum cholesterol. The enzyme also finds application in the microanalysis of steroids in food samples and in distinguishing 3-ketosteroids from 3β-hydroxysteroids. Transgenic plants expressing cholesterol oxidase are being investigated in the fight against the cotton boll weevil. CHOD has also been used as a molecular probe to elucidate cellular membrane structures.

Biochem/physiol Actions

Cholesterol oxidase (CHOD) is a monomeric flavoprotein containing FAD that catalyzes the first step in cholesterol catabolism. This bifunctional enzyme oxidizes cholesterol to cholest-5-en-3-one in an FAD-requiring step, which is then isomerized to cholest-4-en-3-one with the release of H2O2.

Physical properties

Type II cholesterol oxidase containing FAD cofactor covalently linked to the enzyme.

Unit Definition

One unit will convert 1.0 μmole of cholesterol to 4-cholesten-3-one per min at pH 7.5 at 25 °C. Note: 4-cholesten-3-one may undergo isomerization.

Physical form

Supplied as a lyophilzed powder containing sucrose

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

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

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Customers Also Viewed

Block copolymer microdomains: a novel medium for enzymatic reactions
Gupte, A., et al.
Biotechnology Progress, 7, 348-354 (2012)
Meihe Zhang et al.
Biosensors & bioelectronics, 32(1), 288-292 (2011-12-31)
A novel cholesterol biosensor was prepared based on gold nanoparticles-catalyzed luminol electrogenerated chemiluminescence (ECL). Firstly, l-cysteine-reduced graphene oxide composites were modified on the surface of a glassy carbon electrode. Then, gold nanoparticles (AuNPs) were self-assembled on it. Subsequently, cholesterol oxidase
Laura Caldinelli et al.
The Journal of biological chemistry, 280(24), 22572-22581 (2005-04-09)
Cholesterol oxidase from Brevibacterium sterolicum is a monomeric flavoenzyme catalyzing the oxidation and isomerization of cholesterol to cholest-4-en-3-one. This protein is a class II cholesterol oxidases, with the FAD cofactor covalently linked to the enzyme through the His(69) residue. In
Porntip H Lolekha et al.
Clinica chimica acta; international journal of clinical chemistry, 339(1-2), 135-145 (2003-12-23)
Cholesterol oxidase is used for the determination of serum cholesterol. It can be derived from Streptomyces, Pseudomonas fluorescens, Cellulomonas, and Brevibacterium. This study compared the performance characteristics of four enzymes in the endpoint cholesterol determination. Using the Mega analyzer, we
Kwang-wook Ahn et al.
Biochemistry, 43(3), 827-836 (2004-01-21)
We investigated the dependence of cholesterol oxidase catalytic activity and membrane affinity on lipid structure in model membrane bilayers. The binding affinities of cholesterol oxidase to 100-nm unilamellar vesicles composed of mixtures of DOPC or DPPC and cholesterol are not

Protocols

This procedure applies to products that have a specification for the enzymatic activity of cholesterol oxidase. This assay is NOT to be used to assay Cholesterol Oxidase from Schizophyllum commune (Discontinued Product Number C7274) and from Brevibacterium sp. (Discontinued Product Number C8153).

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