BL-Cholesterol oxidase

Cholesterol oxidase is an enzyme that is essential for cholesterol metabolism in living organisms. It catalyzes cholesterol oxidation to coolest-4-en-3-one and hydrogen peroxide. The enzyme is widely used in a wide range of applications, including the food industry, medical diagnosis, and research.

In the 1950s, cholesterol oxidase was isolated from the bacterium Streptomyces. It is a flavoenzyme that requires the cofactor FAD (flavin adenine dinucleotide). The enzyme has a molecular weight of approximately 60 Kuda and is composed of two subunits, each containing a single FAD molecule.

Cholesterol oxidase has a wide substrate specificity and can oxidize a variety of sterols and related compounds. The enzyme’s ability to convert cholesterol to chest-4-en-3-one, a precursor of various steroid hormones and bile acids, has been extensively studied.

Cholesterol oxidase is widely used in the food industry to lower the cholesterol content of foods. The enzyme converts cholesterol into coolest-4-en-3-one, which is easily removed from food products. This method is commonly used in the manufacture of low-cholesterol dairy products like cheese and yogurt.