ArticleBMC biotechnology2014
Cloning, expression and biochemical characterization of the cholesterol oxidase CgChoA from Chryseobacterium gleum.
Article in BMC biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 18 citations in OpenAlex.
- Recombinant Production of a TRAF-Domain Lectin from Cauliflower: A Soluble Expression Strategy for Functional Protein Recovery inInternational journal of molecular sciences · 2025Article
- Cloning, expression, and in silico structural modeling of cholesterol oxidase of Acinetobacter sp. strain RAMD in E. coli.FEBS open bio · 2021Article
- Microbial transformation of cholesterol: reactions and practical aspects-an update.World journal of microbiology & biotechnology · 2019Review
- Characterization and overproduction of cell-associated cholesterol oxidase ChoD from Streptomyces lavendulae YAKB-15.Scientific reports · 2019Article
- Expression optimization, purification, and functional characterization of cholesterol oxidase from Chromobacterium sp. DS1.PloS one · 2019Article
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4 authors at 1 institution in 1 country.
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Abstract
backgroundCholesterol oxidases are important enzymes for applications such as the analysis of cholesterol in clinical samples, the synthesis of steroid derived drugs, and are considered as potential antibacterial drug targets.
resultsThe gene choA encoding a cholesterol oxidase from Chryseobacterium gleum DSM 16776 was cloned into the pQE-30 expression vector and heterologously expressed in Escherichia coli JM109 co-transformed with pRARE2. The N-terminally His-tagged cholesterol oxidase (CgChoA) was assigned to be a monomer in solution by size exclusion chromatography, showed a temperature optimum of 35°C, and a pH optimum at 6.75 using 0.011 M MOPS buffer under the tested conditions. The purified protein showed a maximum activity of 15.5 U/mg. CgChoA showed a Michaelis-Menten like kinetic behavior only when the substrate was dissolved in water and taurocholate (apparent K(m) = 0.5 mM). In addition, the conversion of cholesterol by CgChoA was studied via biocatalytic batches at analytical scale, and cholest-4-en-3-one was confirmed as product by HPLC-MS.
conclusionCgChoA is a true cholesterol oxidase which activity ranges among the high performing described cholesterol oxidases from other organisms. Thus, the enzyme broadens the available toolbox of cholesterol oxidases for e.g. synthetic and biosensing applications.
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