Evidence map›Paper›PMID 24024096›Full record

ArticleSpringerPlus2013

Characterization of a new oxidant-stable serine protease isolated by functional metagenomics.

Sophie Biver, Daniel Portetelle, Micheline Vandenbol

Open access · diamondAbstract read
In one paragraph

Article in SpringerPlus, 2013. 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
6.6field-weighted citation impact, top 3% 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, 63 citations in OpenAlex.

  1. Article
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  10. Article
  11. Emerging priorities for microbial metagenome research.Bioresource technology reports · 2020
    Review
  12. Review
  13. Article
  14. Recent Advances in Function-based Metagenomic Screening.Genomics, proteomics & bioinformatics · 2018
    Review
  15. Article
  16. Review
  17. Review
  18. Article
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  20. Review
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

3 authors at 2 institutions in 1 country.

Sophie BiverUnité de Microbiologie et Génomique, Gembloux Agro-Bio Tech, Université de Liège, Avenue Maréchal Juin 6, B-5030 Gembloux, Belgium.
Daniel Portetelle
Micheline Vandenbol
University of Liège · BEGembloux Agro-Bio Tech · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A novel serine protease gene, SBcas3.3, was identified by functional screening of a forest-soil metagenomic library on agar plates supplemented with AZCL-casein. Overproduction in Escherichia coli revealed that the enzyme is produced as a 770-amino-acid precursor which is processed to a mature protease of ~55 kDa. The latter was purified by affinity chromatography for characterization with the azocasein substrate. The enzyme proved to be an alkaline protease showing maximal activity between pH 9 and 10 and at 50°C. Treatment with the chelating agent ethylenediaminetetraacetic acid irreversibly denatured the protease, whose stability was found to depend strictly on calcium ions. The enzyme appeared relatively resistant to denaturing and reducing agents, and its activity was enhanced in the presence of 10 ml/l nonionic detergent (Tween 20, Tween 80, or Triton X-100). Moreover, SBcas3.3 displayed oxidant stability, a feature particularly sought in the detergent and bleaching industries. SBcas3.3 was activated by hydrogen peroxide at concentrations up to 10 g/l and it still retained 30% of activity in 50 g/l H2O2.

Indexed as

CalciumFunctional metagenomicsOxidantSerine protease

Identifiers

PMID24024096
PMCPMC3765597
OpenAlexW2162109087

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.