Evidence map›Paper›PMID 31502285›Full record

ArticleYeast (Chichester, England)2020

Recombinant production of a hard-to-express membrane-bound cytochrome P450 in different yeasts-Comparison of physiology and productivity.

Johanna Hausjell, Dominik Schendl, Julia Weissensteiner, Christian Molitor, Heidi Halbwirth, Oliver Spadiut

Abstract read
In one paragraph

Article in Yeast (Chichester, England), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

  1. 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

6 authors.

Johanna HausjellTU Wien, Institute of Chemical, Environmental and Bioscience Engineering, Gumpendorfer Straße 1a, Vienna, 1060, Austria.
Dominik SchendlTU Wien, Institute of Chemical, Environmental and Bioscience Engineering, Gumpendorfer Straße 1a, Vienna, 1060, Austria.
Julia WeissensteinerTU Wien, Institute of Chemical, Environmental and Bioscience Engineering, Gumpendorfer Straße 1a, Vienna, 1060, Austria.
Christian MolitorTU Wien, Institute of Chemical, Environmental and Bioscience Engineering, Gumpendorfer Straße 1a, Vienna, 1060, Austria.
Heidi HalbwirthTU Wien, Institute of Chemical, Environmental and Bioscience Engineering, Gumpendorfer Straße 1a, Vienna, 1060, Austria.
Oliver SpadiutTU Wien, Institute of Chemical, Environmental and Bioscience Engineering, Gumpendorfer Straße 1a, Vienna, 1060, Austria.ORCID 0000-0003-0916-0644

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytochrome P450s comprise one of the largest protein superfamilies. They occur in every kingdom of life and catalyse a variety of essential reactions. Their production is of utmost interest regarding biotransformation and structure-function elucidation. However, they have proven hard to express due to their membrane anchor, their complex co-factor requirements and their need for a redox-partner. In our study, we investigated and compared different yeast strains for the production of the plant cytochrome P450 chalcone 3-hydroxylase. To our knowledge, this is the first study evaluating different yeasts for the expression of this abundant and highly significant protein superfamily. Saccharomyces cerevisiae and three different strains of Pichia pastoris expressing chalcone 3-hydroxylase were cultivated in controlled bioreactor runs and evaluated regarding physiological parameters and expression levels of the cytochrome P450. Production differed significantly between the different strains and was found highest in the investigated P. pastoris MutS strain KM71H where 8 mg P450 per gram dry cell weight were detected. We believe that this host could be suitable for the expression of many eukaryotic, especially plant-derived, cytochrome P450s as it combines high specific product yields together with straightforward cultivation techniques for achieving high biomass concentrations. Both factors greatly facilitate subsequent establishment of purification procedures for the cytochrome P450 and make the yeast strain an ideal platform for biotransformation as well.

Indexed as

BioreactorsBiotransformationCell Culture TechniquesCytochrome P-450 Enzyme SystemFungal ProteinsGene Expression Regulation, FungalPichiaRecombinant ProteinsSaccharomyces cerevisiaeCytochrome P-450 Enzyme SystemFungal ProteinsRecombinant Proteinschalcone 3-hydroxylasephysiologyPichia pastorisrecombinant protein productionSaccharomyces cerevisiaeyeast

Identifiers

PMID31502285
PMCPMC7027447

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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.