Evidence map›Paper›PMID 30759160›Full record

ArticlePloS one2019

Expression optimization, purification, and functional characterization of cholesterol oxidase from Chromobacterium sp. DS1.

Aliakbar Fazaeli, Abolfazl Golestani, Mostafa Lakzaei, Samaneh Sadat Rasi Varaei, Mahdi Aminian

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 32 citations in OpenAlex.

  1. High-level fed-batch production of recombinant type II cholesterol oxidase fromBiotechnology reports (Amsterdam, Netherlands) · 2026
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  4. Review
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  9. Current Trends and Perspectives in Microbial Bioconversions of Steroids.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Aliakbar FazaeliDepartment of Clinical Biochemistry, School of Medicine, Ardabil University of Medical Sciences, Ardabil, Iran.
Abolfazl GolestaniDepartment of Biochemistry, School of Medicine, Tehran University of Medical Sciences, Ardabil, Iran.
Mostafa LakzaeiDepartment of Biochemistry, School of Medicine, Tehran University of Medical Sciences, Ardabil, Iran.
Samaneh Sadat Rasi VaraeiDepartment of Biochemistry, School of Medicine, Tehran University of Medical Sciences, Ardabil, Iran.
Mahdi AminianDepartment of Biochemistry, School of Medicine, Tehran University of Medical Sciences, Ardabil, Iran.ORCID 0000-0003-3032-851X
Ardabil University of Medical Sciences · IR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cholesterol oxidase is a bifunctional bacterial flavoenzyme which catalyzes oxidation and isomerization of cholesterol. This valuable enzyme has attracted a great deal of attention because of its wide application in the clinical laboratory, synthesis of steroid derived drugs, food industries, and its potentially insecticidal activity. Therefore, development of an efficient protocol for overproduction of cholesterol oxidase could be valuable and beneficial in this regard. The present study examined the role of various parameters (host strain, culture media, induction time, isopropyl ß-D-1-thiogalactopyranoside concentration, as well as post-induction incubation time and temperature) on over-expression of cholesterol oxidase from Chromobacterium sp. DS1. Applying the optimized protocol, the yield of recombinant cholesterol oxidase significantly increased from 92 U/L to 2115 U/L. Under the optimized conditions, the enzyme was produced on a large-scale, and overexpressed cholesterol oxidase was purified from cell lysate by column nickel affinity chromatography. Km and Vmax values of the purified enzyme for cholesterol were estimated using Lineweaver-Burk plot. Further, the optimum pH and optimum temperature for the enzyme activity were determined. This study reports a straightforward protocol for cholesterol oxidase production which can be performed in any laboratory.

Indexed as

Bacterial ProteinsCholesterol OxidaseChromobacteriumBacterial ProteinsCholesterol Oxidase

Identifiers

PMID30759160
PMCPMC6373949
OpenAlexW2914191779

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.