Evidence map›Paper›PMID 23112831›Full record

ArticlePloS one2012

The metagenome-derived enzymes LipS and LipT increase the diversity of known lipases.

Jennifer Chow, Filip Kovacic, Yuliya Dall Antonia, Ulrich Krauss, Francesco Fersini, Christel Schmeisser, Benjamin Lauinger, Patrick Bongen, Joerg Pietruszka, Marlen Schmidt and 8 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

25 citing papers in PubMed, 82 citations in OpenAlex.

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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

18 authors at 6 institutions in 1 country.

Jennifer ChowDepartment of Microbiology and Biotechnology, Biocenter Klein Flottbek, University of Hamburg, Hamburg, Germany.
Filip Kovacic
Yuliya Dall Antonia
Ulrich Krauss
Francesco Fersini
Christel Schmeisser
Benjamin Lauinger
Patrick Bongen
Joerg Pietruszka
Marlen Schmidt
Ina Menyes
Uwe T Bornscheuer
Marrit Eckstein
Oliver Thum
Andreas Liese
Jochen Mueller-Dieckmann
Karl-Erich Jaeger
Wolfgang R Streit
Heinrich Heine University Düsseldorf · DEUniversität Hamburg · DEUniversität Greifswald · DEEuropean Molecular Biology Laboratory · DEEvonik (Germany) · DEDeutsches Elektronen-Synchrotron DESY · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Triacylglycerol lipases (EC 3.1.1.3) catalyze both hydrolysis and synthesis reactions with a broad spectrum of substrates rendering them especially suitable for many biotechnological applications. Most lipases used today originate from mesophilic organisms and are susceptible to thermal denaturation whereas only few possess high thermotolerance. Here, we report on the identification and characterization of two novel thermostable bacterial lipases identified by functional metagenomic screenings. Metagenomic libraries were constructed from enrichment cultures maintained at 65 to 75 °C and screened resulting in the identification of initially 10 clones with lipolytic activities. Subsequently, two ORFs were identified encoding lipases, LipS and LipT. Comparative sequence analyses suggested that both enzymes are members of novel lipase families. LipS is a 30.2 kDa protein and revealed a half-life of 48 h at 70 °C. The lipT gene encoded for a multimeric enzyme with a half-life of 3 h at 70 °C. LipS had an optimum temperature at 70 °C and LipT at 75 °C. Both enzymes catalyzed hydrolysis of long-chain (C(12) and C(14)) fatty acid esters and additionally hydrolyzed a number of industry-relevant substrates. LipS was highly specific for (R)-ibuprofen-phenyl ester with an enantiomeric excess (ee) of 99%. Furthermore, LipS was able to synthesize 1-propyl laurate and 1-tetradecyl myristate at 70 °C with rates similar to those of the lipase CalB from Candida antarctica. LipS represents the first example of a thermostable metagenome-derived lipase with significant synthesis activities. Its X-ray structure was solved with a resolution of 1.99 Å revealing an unusually compact lid structure.

Indexed as

MetagenomeAlcoholsBacteriaCloning, MolecularCrystallography, X-RayDNA, BacterialEnzyme StabilityEsterificationGenome, BacterialGlyceridesLipaseMetagenomicsModels, MolecularMolecular Sequence DataNitrophenolsPhylogenyAlcoholsDNA, BacterialGlyceridesLipaseNitrophenolsRecombinant Proteins

Identifiers

PMID23112831
PMCPMC3480424
OpenAlexW1984751786

What OpenQuestion holds

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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.