Evidence map›Paper›PMID 23160923›Full record

ArticleJournal of industrial microbiology & biotechnology2013

Characterization of three new carboxylic ester hydrolases isolated by functional screening of a forest soil metagenomic library.

Sophie Biver, Micheline Vandenbol

Open access · bronzeAbstract read
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In one paragraph

Article in Journal of industrial microbiology & biotechnology, 2013. 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
2.3field-weighted citation impact, top 12% 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, 57 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
  6. Article
  7. Emerging priorities for microbial metagenome research.Bioresource technology reports · 2020
    Review
  8. Article
  9. Article
  10. Review
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  14. Article
  15. Isolation and characterization of a thermostable esterase from a metagenomic library.Journal of industrial microbiology & biotechnology · 2013
    Article
  16. 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

2 authors at 1 institution in 1 country.

Sophie BiverUnité de Microbiologie et Génomique, Gembloux Agro-Bio Tech, Université de Liège, Avenue Maréchal Juin 6, 5030 Gembloux, Belgium. Sophie.Biver@ulg.ac.be
Micheline Vandenbol
University of Liège · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Three new lipolytic genes were isolated from a forest soil metagenomic library by functional screening on tributyrin agar plates. The genes SBLip1, SBLip2 and SBLip5.1 respectively encode polypeptides of 445, 346 and 316 amino acids. Phylogenetic analyses revealed that SBLip2 and SBLip5.1 belong to bacterial esterase/lipase family IV, whereas SBLip1 shows similarity to class C β-lactamases and is thus related to esterase family VIII. The corresponding genes were overexpressed and their products purified by affinity chromatography for characterization. Analyses of substrate specificity with different p-nitrophenyl esters showed that all three enzymes have a preference for short-acyl-chain p-nitrophenyl esters, a feature of carboxylesterases as opposed to lipases. The β-lactamase activity of SBLip1, measured with the chromogenic substrate nitrocefin, was very low. The three esterases have the same optimal pH (pH 10) and remain active across a relatively broad pH range, displaying more than 60 % activity between pH 6 and 10. The temperature optima determined were 35 °C for SBLip1, 45 °C for SBLip2 and 50 °C for SBLip5.1. The three esterases displayed different levels of tolerance to salts, solvents and detergents, SBLip2 being overall more tolerant to high concentrations of solvent and SBLip5.1 less affected by detergents.

Indexed as

Gene LibraryMetagenomicsSoil MicrobiologyTreesAmino Acid Sequencebeta-LactamasesBiological EvolutionCarboxylic Ester HydrolasesChromatography, AffinityEsterasesHydrogen-Ion ConcentrationKineticsLipaseLipolysisMolecular Sequence DataSaltsbeta-LactamasesCarboxylic Ester HydrolasesEsterasesLipaseSalts

Identifiers

PMID23160923
OpenAlexW2046889034

What OpenQuestion holds

Textmetadata
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.