ArticleAMB Express2018
Expression optimization of recombinant cholesterol oxidase in Escherichia coli and its purification and characterization.
Article in AMB Express, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 15 citations in OpenAlex.
- High-level fed-batch production of recombinant type II cholesterol oxidase fromBiotechnology reports (Amsterdam, Netherlands) · 2026Article
- Purification and Immobilization of Burkholderia gladioli Cholesterol Oxidase on Calcium Alginate, with Robust Catalytic Stability for Cholesterol Oxidation In Vitro.Current microbiology · 2025Article
- Cloning, expression, and in silico structural modeling of cholesterol oxidase of Acinetobacter sp. strain RAMD in E. coli.FEBS open bio · 2021Article
- Identification of cholesterol-assimilating actinomycetes strain and application of statistical modeling approaches for improvement of cholesterol oxidase production by Streptomyces anulatus strain NEAE-94.BMC microbiology · 2020Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
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, as well as post-induction incubation time and temperature were determined in a shaking flask mode. Applying the optimized protocol, the production of recombinant cholesterol oxidase was significantly enhanced from 3.2 to 158 U/L. Under the optimized condition, the enzyme was produced on a large-scale, and highly expressed cholesterol oxidase was purified from cell lysate by column nickel affinity chromatography. K
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