Evidence map›Paper›PMID 25586641›Full record

ArticleMicrobial cell factories2015

Optimizing cofactor availability for the production of recombinant heme peroxidase in Pichia pastoris.

Florian W Krainer, Simona Capone, Martin Jäger, Thomas Vogl, Michaela Gerstmann, Anton Glieder, Christoph Herwig, Oliver Spadiut

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

18 citing papers in PubMed, 41 citations in OpenAlex.

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  8. Functional mononuclear molybdenum enzymes: challenges and triumphs in molecular cloning, expression, and isolation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Review
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  12. Isoform-Specific NO Synthesis byPlants (Basel, Switzerland) · 2019
    Article
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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

8 authors at 4 institutions in 1 country.

Florian W KrainerGraz University of Technology, NAWI Graz, Institute of Molecular Biotechnology, Graz, Austria. florian.krainer@tugraz.at.
Simona CaponeVienna University of Technology, Institute of Chemical Engineering, Research Area Biochemical Engineering, Gumpendorfer Strasse 1a, 1060, Vienna, Austria. simona.capone@tuwien.ac.at.
Martin JägerVienna University of Technology, Institute of Chemical Engineering, Research Area Biochemical Engineering, Gumpendorfer Strasse 1a, 1060, Vienna, Austria. martinjaeger@chello.at.
Thomas VoglGraz University of Technology, NAWI Graz, Institute of Molecular Biotechnology, Graz, Austria. thomas.vogl@tugraz.at.
Michaela GerstmannGraz University of Technology, NAWI Graz, Institute of Molecular Biotechnology, Graz, Austria. michaela.gerstmann@gmx.net.
Anton GliederGraz University of Technology, NAWI Graz, Institute of Molecular Biotechnology, Graz, Austria. a.glieder@tugraz.at.
Christoph HerwigVienna University of Technology, Institute of Chemical Engineering, Research Area Biochemical Engineering, Gumpendorfer Strasse 1a, 1060, Vienna, Austria. christoph.herwig@tuwien.ac.at.
Oliver SpadiutVienna University of Technology, Institute of Chemical Engineering, Research Area Biochemical Engineering, Gumpendorfer Strasse 1a, 1060, Vienna, Austria. oliver.spadiut@tuwien.ac.at.
TU Wien · ATNawi Graz · ATGraz University of Technology · ATInstitute of Molecular Biotechnology · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundInsufficient incorporation of heme is considered a central impeding cause in the recombinant production of active heme proteins. Currently, two approaches are commonly taken to overcome this bottleneck; metabolic engineering of the heme biosynthesis pathway in the host organism to enhance intracellular heme production, and supplementation of the growth medium with the desired cofactor or precursors thereof to allow saturation of recombinantly produced apo-forms of the target protein. In this study, we investigated the effect of both, pathway engineering and medium supplementation, to optimize the recombinant production of the heme protein horseradish peroxidase in the yeast Pichia pastoris.

resultsIn contrast to studies with other hosts, co-overexpression of genes of the endogenous heme biosynthesis pathway did not improve the recombinant production of active heme protein. However, medium supplementation with hemin proved to be an efficient strategy to increase the yield of active enzyme, whereas supplementation with the commonly used precursor 5-aminolevulinic acid did not affect target protein yield.

conclusionsThe yield of active recombinant heme peroxidase from P. pastoris can be easily enhanced by supplementation of the cultivation medium with hemin. Thereby, secreted apo-species of the target protein are effectively saturated with cofactor, maximizing the yield of target enzyme activity.

Indexed as

Aldehyde OxidaseBatch Cell Culture TechniquesFerrous CompoundsFungal ProteinsHemeHorseradish PeroxidasePichiaPlant ProteinsPromoter Regions, GeneticRecombinant ProteinsAldehyde OxidaseFerrous Compoundsferrous sulfateFungal ProteinsHemeHorseradish PeroxidasePlant ProteinsRecombinant Proteins

Identifiers

PMID25586641
PMCPMC4299804
OpenAlexW2165448239

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.