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Key Documents

C8649

Sigma-Aldrich

Cholesterol Oxidase from Streptomyces sp.

lyophilized powder, ≥20 units/mg protein

Synonym(s):

Cholesterol: oxygen oxidoreductase

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About This Item

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

biological source

Streptomyces sp.

Quality Level

form

lyophilized powder

specific activity

≥20 units/mg protein

mol wt

~34 kDa

composition

protein, 55-65% biuret

solubility

50 mM potassium phosphate buffer, pH 7.0: soluble (Cold)

shipped in

dry ice

storage temp.

−20°C

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General description

Cholesterol Oxidase produced from Streptomyces sp corresponds to a molecular weight of 62 kDa. It has a pH and temperature optimum of 7 and 37 °C, respectively. Cholesterol Oxidase comprises a FAD-binding and a steroid-binding domain.

Application

Cholesterol oxidase from Streptomyces has been used in a study to assess the relationship between the micellar structure of model bile and the activity of esterase. Cholesterol oxidase from Streptomyces has also been used in a study to investigate the effects of sphingomyelin degradation on cell cholesterol oxidizability and steady-state distribution between the cell surface and the cell interior.
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 from microorganisms use cholesterol for carbon and energy. It is useful in diagnostic assays involving cholesterol, especially in lipid disorders. Cholesterol oxidase has an insecticidal property and aids protection against boll weevil larvae. The Streptomyces sp cholesterol oxidase has long shelf-life with good performance.
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

Isoelectric point : 5.1 ± 0.1 and 5.4 ± 0.1
Michaelis constant : 4.3 x 10‾5M(Cholesterol)
Inhibitors : Ionic detergents, Hg++, Ag+
Optimum pH : 6.5 − 7.0
Optimum temperature : 45 – 50°C
pH Stability : pH 5.0 – 10.0 (25°C, 20hr)
Thermal stability : Below 45°C (pH 7.0, 15min)

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

lyophilized powder containing bovine serum albumin and amino acids as stabilizers

Preparation Note

CHOD is soluble in cold 50 mM potassium phosphate buffer, pH 7.0. Prepare solutions immediately before use.

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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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J P Slotte et al.
Biochimica et biophysica acta, 985(1), 90-96 (1989-10-02)
This study addresses questions related to (i) the distribution of cholesterol between the cell surface and intracellular membranes in cultured fibroblasts and (ii) the effects of plasma membrane sphingomyelin on this distribution. Cholesterol oxidase (Streptomyces sp.) converts cell cholesterol to
Crystal structure determination of cholesterol oxidase from Streptomyces and structural characterization of key active site mutants
Yue QK, et al.
Biochemistry, 38(14), 4277-4286 (1999)
Extracellular cholesterol oxidase production by Streptomyces aegyptia, in vitro anticancer activities against rhabdomyosarcoma, breast cancer cell-lines and in vivo apoptosis
NEA El-Naggar, et al.
Scientific reports, 8(1), 2706-2706 (2018)
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
Effect of cholesterol concentration on organization of viral and vesicle membranes. Probed by accessibility to cholesterol oxidase.
R Pal et al.
The Journal of biological chemistry, 255(12), 5802-5806 (1980-06-25)

Protocols

Protocol for Assay Procedure for Cholesterol Oxidase

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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