PMC:101390 / 1868-2745 JSONTXT

{"project":"2_test","denotations":[{"id":"11914155-4818200-8561947","span":{"begin":268,"end":269},"obj":"4818200"},{"id":"11914155-10822008-8561948","span":{"begin":414,"end":415},"obj":"10822008"},{"id":"11914155-13143010-8561949","span":{"begin":487,"end":488},"obj":"13143010"},{"id":"11914155-10822008-8561950","span":{"begin":567,"end":568},"obj":"10822008"},{"id":"11914155-4757363-8561951","span":{"begin":874,"end":875},"obj":"4757363"}],"text":"Microbial cholesterol oxidases (EC 1.1.3.6) (COX) catalyze the oxidation and isomerization of cholesterol to 4-cholesten-3-one. Interest in these enzymes mostly relies in their utility in the determination of cholesterol in biological samples such as serum and foods [1], and also in the bioconversion of a number of 3β-hydroxysteroids in organic solvents [2] and in reverse micelles [3] (for a recent review see [5]). Since earliest reports on crude preparations from Mycobacterium sp.[4], cholesterol oxidases have been described in a number of bacteria and fungi [5]. Enzymatic properties of cholesterol oxidase from Rhodococcus strains (some of which named formerly as Nocardid) are particularly suitable for use in the analytical determination of cholesterol, in which the hydrogen peroxide formed is used in a chromogenic reaction catalyzed by horseradish peroxidase [6]."}