Evidence map›Paper›PMID 30405184›Full record

ArticleScientific reports2018

A novel alkaline protease from alkaliphilic Idiomarina sp. C9-1 with potential application for eco-friendly enzymatic dehairing in the leather industry.

Cheng Zhou, Hongliang Qin, Xiujuan Chen, Yan Zhang, Yanfen Xue, Yanhe Ma

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

23 citing papers in PubMed, 84 citations in OpenAlex.

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  12. Overexpression ofFrontiers in microbiology · 2022
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  14. Heliyon · 2021
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  15. PsychrotolerantMolecules (Basel, Switzerland) · 2021
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  16. Article
  17. Article
  18. Article
  19. Article
  20. Multipotential Alkaline Protease From a NovelFrontiers in microbiology · 2021
    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

6 authors at 3 institutions in 1 country.

Cheng ZhouState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China. zhoucheng@im.ac.cn.
Hongliang QinState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Xiujuan ChenSchool of Pharmaceutical Sciences, Jiangnan University, Wuxi, 214122, China.
Yan ZhangState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Yanfen XueState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Yanhe MaState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China. mayanhe@im.ac.cn.
Institute of Microbiology · CNMicrobiology Institute of Shaanxi · CNJiangnan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alkaline proteases have a myriad of potential applications in many industrial processes such as detergent, food and feed production, waste management and the leather industry. In this study, we isolated several alkaline protease producing bacteria from soda lake soil samples. A novel serine alkaline protease (AprA) gene from alkaliphilic Idiomarina sp. C9-1 was cloned and expressed in Escherichia coli. The purified AprA and its pre-peptidase C-terminal (PPC) domain-truncated enzyme (AprA-PPC) showed maximum activity at pH 10.5 and 60 °C, and were active and stable in a wide range of pH and temperature. Ca

Indexed as

Animal FurAlteromonadaceaeAnimalsBacterial ProteinsBase SequenceCloning, MolecularEndopeptidasesHydrogen-Ion ConcentrationIndustryModels, MolecularPhylogenyProtein ConformationRecombinant ProteinsSequence Analysis, DNASubstrate SpecificityTemperaturealkaline proteaseBacterial ProteinsEndopeptidasesRecombinant Proteins

Identifiers

PMID30405184
PMCPMC6220337
OpenAlexW2899259252

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.