Expression optimization of recombinant cholesterol oxidase in Escherichia coli and its purification and characterization.

ABSTRACT: Cholesterol oxidase is a bacterial flavoenzyme which catalyzes oxidation and isomerization of cholesterol. This enzyme has a great commercial value because of its wide applications in cholesterol analysis of clinical samples, synthesis of steroid-derived drugs, food industries, and potentially insecticidal activity. Accordingly, development of an efficient protocol for overexpression of cholesterol oxidase can be very valuable and beneficial. In this study, expression optimization of cholesterol oxidase from Streptomyces sp. SA-COO was investigated in Escherichia coli host strains. Various parameters that may influence the yield of a recombinant enzyme were evaluated individually. The optimal host strain, culture media, induction time, Isopropyl ß-D-1-thiogalactopyranoside concentration, a

SUBMITTER: Fazaeli A 

PROVIDER: S-EPMC6232189 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature