Evidence map›Paper›PMID 42020871›Full record

ArticleApplied microbiology and biotechnology2026

A katE katG double-knockout E. coli strain eliminates the risk of catalase contamination in recombinant proteins.

Axel Tobias Scholz, Lucia Coppo, Edward Nolan, Michaella Hernandez, Xuan Wang, Pradeep Mishra, Robert Schnell, Zsuzsanna Anna Pató, Yifei Chen, Markus Dagnell and 3 more

Abstract read
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In one paragraph

Article in Applied microbiology and biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

13 authors.

Axel Tobias ScholzDepartment of Medical Biochemistry and Biophysics, Division of Biochemistry, Karolinska Institutet, SE-171 77, Stockholm, Sweden.
Lucia CoppoDepartment of Medical Biochemistry and Biophysics, Division of Biochemistry, Karolinska Institutet, SE-171 77, Stockholm, Sweden.
Edward NolanSchool of Life Sciences, Arizona State University, Tempe, AZ, USA.
Michaella HernandezSchool of Life Sciences, Arizona State University, Tempe, AZ, USA.
Xuan WangSchool of Life Sciences, Arizona State University, Tempe, AZ, USA.
Pradeep MishraDepartment of Medical Biochemistry and Biophysics, Umeå University, SE, 901 87, Umeå, Sweden.
Robert SchnellDepartment of Neuroscience, Karolinska Institutet, SE, 171 77, Stockholm, Sweden.
Zsuzsanna Anna PatóDepartment of Medical Biochemistry and Biophysics, Division of Biochemistry, Karolinska Institutet, SE-171 77, Stockholm, Sweden.ORCID http://orcid.org/0000-0003-2135-824X
Yifei ChenDepartment of Medical Biochemistry and Biophysics, Division of Biochemistry, Karolinska Institutet, SE-171 77, Stockholm, Sweden.
Markus DagnellDepartment of Medical Biochemistry and Biophysics, Division of Biochemistry, Karolinska Institutet, SE-171 77, Stockholm, Sweden.
Attila AndorDepartment of Medical Biochemistry and Biophysics, Division of Biochemistry, Karolinska Institutet, SE-171 77, Stockholm, Sweden.ORCID http://orcid.org/0000-0002-1829-8824
Qing ChengDepartment of Medical Biochemistry and Biophysics, Division of Biochemistry, Karolinska Institutet, SE-171 77, Stockholm, Sweden.
Elias S J ArnérDepartment of Medical Biochemistry and Biophysics, Division of Biochemistry, Karolinska Institutet, SE-171 77, Stockholm, Sweden. elias.arner@ki.se.

Funding

Cancerfonden 21 1463 PjNemzeti Kutatási Fejlesztési és Innovációs Hivatal 2022-2.1.1-NL-2022-00010, TKP2021-EGA-44 and K 146277Vetenskapsrådet 2021-02214
6 · The paper itself

Abstract

Recombinant protein expression in E. coli is a key methodology for modern biomedical research. Typically, a polyhistidine-tagged ("His-tagged") protein is purified using immobilized metal affinity chromatography (IMAC), achieving close to apparently homogenous target protein preparations. However, contaminant host proteins may nonetheless be co-purified at trace amounts. This includes bacterial catalase, which can even be found crystallized instead of an intended target protein. Here, we found that less than 0.03% of the original endogenous bacterial catalase remaining in a final recombinant protein product can easily be detected in an enzymatic H

Indexed as

Bacterial ProteinsCatalaseEscherichia coliEscherichia coli ProteinsRecombinant ProteinsChromatography, AffinityGene Knockout TechniquesHydrogen PeroxideBacterial ProteinsCatalaseEscherichia coli ProteinsHydrogen PeroxidekatG protein, E coliRecombinant ProteinsCatalaseEscherichia coli (E. coli)Hydrogen peroxidePeroxiredoxinProtein purificationRecombinant protein expressionThioredoxin

Identifiers

PMID42020871
PMCPMC13102901

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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.