Evidence map›Paper›PMID 29643457›Full record

ArticleScientific reports2018

Catalytically active inclusion bodies of L-lysine decarboxylase from E. coli for 1,5-diaminopentane production.

Ramona Kloss, Michael H Limberg, Ursula Mackfeld, Doris Hahn, Alexander Grünberger, Vera D Jäger, Ulrich Krauss, Marco Oldiges, Martina Pohl

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 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.2field-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

20 citing papers in PubMed, 55 citations in OpenAlex.

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  13. Coiled-Coil Based Inclusion Bodies and Their Potential Applications.Frontiers in bioengineering and biotechnology · 2021
    Review
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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

9 authors at 1 institution in 1 country.

Ramona KlossForschungszentrum Jülich GmbH, IBG-1: Biotechnology, 52425, Jülich, Germany.
Michael H LimbergForschungszentrum Jülich GmbH, IBG-1: Biotechnology, 52425, Jülich, Germany.
Ursula MackfeldForschungszentrum Jülich GmbH, IBG-1: Biotechnology, 52425, Jülich, Germany.
Doris HahnForschungszentrum Jülich GmbH, IBG-1: Biotechnology, 52425, Jülich, Germany.
Alexander GrünbergerForschungszentrum Jülich GmbH, IBG-1: Biotechnology, 52425, Jülich, Germany.
Vera D JägerInstitute of Molecular Enzyme Technology, Heinrich-Heine-Universität Düsseldorf, Forschungszentrum Jülich, 52425, Jülich, Germany.
Ulrich KraussInstitute of Molecular Enzyme Technology, Heinrich-Heine-Universität Düsseldorf, Forschungszentrum Jülich, 52425, Jülich, Germany.ORCID 0000-0003-2219-7388
Marco OldigesForschungszentrum Jülich GmbH, IBG-1: Biotechnology, 52425, Jülich, Germany.
Martina PohlForschungszentrum Jülich GmbH, IBG-1: Biotechnology, 52425, Jülich, Germany. ma.pohl@fz-juelich.de.ORCID 0000-0001-9935-5183
Forschungszentrum Jülich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sustainable and eco-efficient alternatives for the production of platform chemicals, fuels and chemical building blocks require the development of stable, reusable and recyclable biocatalysts. Here we present a novel concept for the biocatalytic production of 1,5-diaminopentane (DAP, trivial name: cadaverine) using catalytically active inclusion bodies (CatIBs) of the constitutive L-lysine decarboxylase from E. coli (EcLDCc-CatIBs) to process L-lysine-containing culture supernatants from Corynebacterium glutamicum. EcLDCc-CatIBs can easily be produced in E. coli followed by a simple purification protocol yielding up to 43% dry CatIBs per dry cell weight. The stability and recyclability of EcLDCc-CatIBs was demonstrated in (repetitive) batch experiments starting from L-lysine concentrations of 0.1 M and 1 M. EcLDC-CatIBs exhibited great stability under reaction conditions with an estimated half-life of about 54 h. High conversions to DAP of 87-100% were obtained in 30-60 ml batch reactions using approx. 180-300 mg EcLDCc-CatIBs, respectively. This resulted in DAP titres of up to 88.4 g l

Indexed as

Batch Cell Culture TechniquesBiocatalysisBioreactorsCadaverineCarboxy-LyasesCorynebacterium glutamicumEscherichia coliEscherichia coli ProteinsInclusion BodiesLysineMetabolic EngineeringRecombinant ProteinsCadaverineCarboxy-LyasesEscherichia coli ProteinsLysinelysine decarboxylaseRecombinant Proteins

Identifiers

PMID29643457
PMCPMC5895699
OpenAlexW2805134036

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.