Evidence map›Paper›PMID 36303174›Full record

ArticleBMC biotechnology2022

Gene cloning and molecular characterization of a thermostable chitosanase from Bacillus cereus TY24.

Rong-Xian Zhang, Zhong-Wei Wu, Shu-Juan Zhang, Hui-Min Wei, Cheng-Wei Hua, Lan Li, Tian-You Yang

Open access · goldAbstract read
In one paragraph

Article in BMC biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

1 citing paper in PubMed, 6 citations in OpenAlex.

  1. Article
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

7 authors at 1 institution in 1 country.

Rong-Xian ZhangSchool of Life Science and Technology, Henan Institute of Science and Technology, Xinxiang, 453003, People's Republic of China. RongxZhang@163.com.
Zhong-Wei WuSchool of Life Science and Technology, Henan Institute of Science and Technology, Xinxiang, 453003, People's Republic of China.
Shu-Juan ZhangSchool of Life Science and Technology, Henan Institute of Science and Technology, Xinxiang, 453003, People's Republic of China.
Hui-Min WeiSchool of Life Science and Technology, Henan Institute of Science and Technology, Xinxiang, 453003, People's Republic of China.
Cheng-Wei HuaSchool of Life Science and Technology, Henan Institute of Science and Technology, Xinxiang, 453003, People's Republic of China.
Lan LiSchool of Life Science and Technology, Henan Institute of Science and Technology, Xinxiang, 453003, People's Republic of China.
Tian-You YangSchool of Life Science and Technology, Henan Institute of Science and Technology, Xinxiang, 453003, People's Republic of China.
Henan Institute of Science and Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAn important conceptual advance in health and the environment has been recognized that enzymes play a key role in the green processing industries. Of particular interest, chitosanase is beneficial for recycling the chitosan resource and producing chitosan oligosaccharides. Also, chitosan gene expression and molecular characterization will promote understanding of the biological function of bacterial chitosanase as well as explore chitosanase for utilizing chitosan resources.

resultsA chitosanase-producing bacterium TY24 was isolated and identified as Bacillus cereus. Moreover, the chitosanase gene was cloned and expressed in Escherichia coli. Sequence analysis reveals that the recombinant chitosanase (CHOE) belongs to the glycoside hydrolases 8 family. The purified CHOE has a molecular weight of about 48 kDa and the specific activity of 1150 U/mg. The optimal pH and temperature of CHOE were 5.5 and 65 °C, respectively. The enzyme was observed stable at the pH range of 4.5-7.5 and the temperature range of 30-65 °C. Especially, the half-life of CHOE at 65 °C was 161 min. Additionally, the activity of CHOE was remarkably enhanced in the presence of Mn

conclusionA bacterial chitosanase was cloned from B. cereus and successfully expressed in E. coli (BL21) DE3. The recombinant enzyme displayed good stability under acid pH and high-temperature conditions.

Indexed as

Bacillus cereusChitosanCloning, MolecularEscherichia coliGlycoside HydrolasesHydrogen-Ion ConcentrationChitosanchitosanaseGlycoside HydrolasesBacillus cereusChitosanasechoeRecombinant expressionThermostability

Identifiers

PMID36303174
PMCPMC9615241
OpenAlexW4307412822

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.