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C8868
Cholesterol Oxidase from Brevibacterium
lyophilized powder, ≥50 units/mg protein, recombinant, expressed in E. coli
Synonym(e):
Cholesterol: oxygen oxidoreductase
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About This Item
Empfohlene Produkte
Rekombinant
expressed in E. coli
Qualitätsniveau
Form
lyophilized powder
Spezifische Aktivität
≥50 units/mg protein
Mol-Gew.
64 kDa
Zusammensetzung
Protein, ≥15% biuret
Lagertemp.
−20°C
Anwendung
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. Wirkung
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.
Physikalische Eigenschaften
Type II cholesterol oxidase containing FAD cofactor covalently linked to the enzyme.
Einheitendefinition
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.
Physikalische Form
Supplied as a lyophilzed powder containing sucrose
Signalwort
Danger
H-Sätze
P-Sätze
Gefahreneinstufungen
Resp. Sens. 1
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, type N95 (US)
Analysenzertifikate (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
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
Mitsutoshi Toyama et al.
Protein engineering, 15(6), 477-484 (2002-06-26)
Despite the structural similarities between cholesterol oxidase from Streptomyces and that from Brevibacterium, both enzymes exhibit different characteristics, such as catalytic activity, optimum pH and temperature. In attempts to define the molecular basis of differences in catalytic activity or stability
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