Evidence map›Paper›PMID 40323466›Full record

ArticleBiotechnology letters2025

Application of lactose based autoinduction for heterologous production of an active [NiFe] hydrogenase in E. coli.

Francisco de la Fuente-Kratzborn, Qin Fan, Peter Neubauer, Matthias Gimpel

Abstract read
In one paragraph

Article in Biotechnology letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
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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

4 authors.

Francisco de la Fuente-KratzbornChair of Bioprocess Engineering, Institute of Biotechnology, Technische Universität Berlin, Ackerstr. 76, ACK24, D‑13355, Berlin, Germany.
Qin FanChair of Bioprocess Engineering, Institute of Biotechnology, Technische Universität Berlin, Ackerstr. 76, ACK24, D‑13355, Berlin, Germany. qin.fan@tu-berlin.de.ORCID http://orcid.org/0000-0001-5801-8690
Peter NeubauerChair of Bioprocess Engineering, Institute of Biotechnology, Technische Universität Berlin, Ackerstr. 76, ACK24, D‑13355, Berlin, Germany.
Matthias GimpelChair of Bioprocess Engineering, Institute of Biotechnology, Technische Universität Berlin, Ackerstr. 76, ACK24, D‑13355, Berlin, Germany.

Funding

Deutsche Forschungsgemeinschaft 2008/1-390540038
6 · The paper itself

Abstract

objectivesThis study aims to assess whether a fed-batch-based auto-induction method can enhance active hydrogenase production, encompassing cofactor formation and space-time yield.

resultsThe recombinant Escherichia coli strain BQF8RH8, possessing plasmids for assembly and proper maturation of Cupriavidus necator regulatory hydrogenase (RH), was cultivated in the fed-batch like EnPresso B medium with an autoinduction lactose-based system. In contrast to classical IPTG induction previously performed, we obtained active RH demonstrating the feasibility of the process for active hydrogenase production.

conclusionOur results affirm the viability of the previously developed auto-induction strategy also for a functional hydrogenase with the complex maturation process. This significantly accelerates the process and enhances hydrogenase productivity.

Indexed as

Escherichia coliHydrogenaseLactoseBatch Cell Culture TechniquesCulture MediaCupriavidus necatorRecombinant ProteinsCulture MediaHydrogenaseLactosenickel-iron hydrogenaseRecombinant ProteinsAutoinductionCupriavidus necator[NiFe]-hydrogenaseRegulatory hydrogenase

Identifiers

PMID40323466
PMCPMC12053349

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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.