Description

Appearance: light yellow amorphous powder
Specific activity: ≥11U/mg
Stability: stable for one year at -20℃
Molecular weight: approx. 60KD
Isoelectric point: 5.2
Molarity: 1 x 10–4 M (cholesterol)
Inhibitor: not inhibited by sodium azide
pH stability: 6.0–10.0 (Fig. 3-1)
Optimal pH: 6.5–7.5 (Fig. 3-2)
Optimal temperature: 52°C (Fig. 3-3)
Thermal stability: stable up to 60°C (Fig. 3-4)
Stabilizer: potassium ions help stabilize enzyme activity

Cholesterol oxidase (EC1.1.3.6 COD) is increasingly being recognized for its role in food processing, medical testing, biological pest control, and other fields, and it has shown great potential for application.
It is a key enzyme in the cholesterol metabolism process, dependent on coenzyme FAD, and can specifically catalyze the conversion of cholesterol to cholest-4-ene-3-one (4-cholesterol-3-one). Recombinant E. coli producing COD was used as the research object, with the goal of developing and applying COD. Research was conducted on the separation and extraction of COD, its enzymatic properties, and the application of the enzyme. The COD was isolated using a purification process that included ultrasonic treatment of recombinant E. coli, 70% (NH_4)_2SO_4 salting out, CM Sepharose F.F. ion exchange chromatography, and Sephadex G-75 Fine gel filtration. The extracted and purified COD had an enzyme activity of 47.3 U/mg, a purification multiple of 45 times, and an enzyme activity recovery rate of 21%.

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