C8868
Cholesterol Oxidase from microorganisms
lyophilized powder, ≥50 units/mg protein, recombinant, expressed in E. coli
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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
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
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
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
常规特殊物品
Certificates of Analysis (COA)
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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
Tania Pomili et al.
Biosensors, 11(11) (2021-11-26)
In this study, we describe a monolithic and fully integrated paper-based device for the simultaneous detection of three prognostic biomarkers in saliva. The pattern of the proposed multiplexed device is designed with a central sample deposition zone and three identical
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
Protocols
Enzymatic activity assay for cholesterol oxidase, excluding specific product numbers, providing guidelines for accurate cholesterol oxidase assays.
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