Evidence map›Paper›PMID 36076195›Full record

ArticleBMC biotechnology2022

Production of surfactant-stable keratinase from Bacillus cereus YQ15 and its application as detergent additive.

Rong-Xian Zhang, Zhong-Wei Wu, Hai-Yang Cui, Ying-Nan Chai, Cheng-Wei Hua, Peng Wang, 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 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

12 citing papers in PubMed, 39 citations in OpenAlex.

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  8. Response surface methodology based optimization of keratinase fromSaudi journal of biological sciences · 2023
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  12. Keratinolytic Properties ofInternational journal of environmental research and public health · 2022
    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

8 authors at 2 institutions 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.
Hai-Yang CuiSchool of Life Science and Technology, Henan Institute of Science and Technology, Xinxiang, 453003, People's Republic of China.
Ying-Nan ChaiSchool 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.
Peng WangBlood Transfusion Department, The Third Affiliated Hospital of Xinxiang Medical University, 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 · CNXinxiang Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundWith the growing concern for the environment, there are trends that bio-utilization of keratinous waste by keratinases could ease the heavy burden of keratinous waste from the poultry processing and leather industry. Especially surfactant-stable keratinases are beneficial for the detergent industry. Therefore, the production of keratinase by Bacillus cereus YQ15 was improved; the characterization and use of keratinase in detergent were also studied.

resultsA novel alkaline keratinase-producing bacterium YQ15 was isolated from feather keratin-rich soil and was identified as Bacillus cereus. Based on the improvement of medium components and culture conditions, the maximum keratinase activity (925 U/mL) was obtained after 36 h of cultivation under conditions of 35 °C and 160 rpm. Moreover, it was observed that the optimal reacting temperature and pH of the keratinase are 60 °C and 10.0, respectively; the activity was severely inhibited by PMSF and EDTA. On the contrary, the keratinase showed remarkable stability in the existence of the various surfactants, including SDS, Tween 20, Tween 60, Tween 80, and Triton X-100. Especially, 5% of Tween 20 and Tween 60 increased the activity by 100% and 60%, respectively. Furtherly, the keratinase revealed high efficiency in removing blood stains.

conclusionThe excellent compatibility with commercial detergents and the high washing efficiency of removing blood stains suggested its suitability for potential application as a bio-detergent additive.

Indexed as

Bacillus cereusDetergentsAnimalsEnzyme StabilityFeathersHydrogen-Ion ConcentrationKeratinsPeptide HydrolasesPolysorbatesSurface-Active AgentsTemperatureDetergentskeratinaseKeratinsPeptide HydrolasesPolysorbatesSurface-Active AgentsBacillus cereusDetergent compatibilityKeratinaseProduction

Identifiers

PMID36076195
PMCPMC9454225
OpenAlexW4295079394

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.