ArticleMicrobial cell factories2021
Production of soluble regulatory hydrogenase from Ralstonia eutropha in Escherichia coli using a fed-batch-based autoinduction system.
Article in Microbial cell factories, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Genomically integrated orthogonal translation system in Escherichia coli enables production of functional modified [NiFe]-hydrogenases.Microbial cell factories · 2026Article
- Development of a Universal Platform for the Heterologous Expression of Bidirectional [Ni-Fe]-Hydrogenases inACS synthetic biology · 2025Article
- Application of lactose based autoinduction for heterologous production of an active [NiFe] hydrogenase in E. coli.Biotechnology letters · 2025Article
- Physiology-informed use of Cupriavidus necator in biomanufacturing: a review of advances and challenges.Microbial cell factories · 2025Review
- Expression of soluble moloney murine leukemia virus-reverse transcriptase in Escherichia coli BL21 star (DE3) using autoinduction system.Molecular biology reports · 2024Article
- Implementation of a high cell density fed-batch for heterologous production of active [NiFe]-hydrogenase in Escherichia coli bioreactor cultivations.Microbial cell factories · 2022Article
- High-Yield Production of Catalytically Active Regulatory [NiFe]-Hydrogenase FromFrontiers in microbiology · 2022Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
backgroundAutoinduction systems can regulate protein production in Escherichia coli without the need to monitor cell growth or add inducer at the proper time following culture growth. Compared to classical IPTG induction, autoinduction provides a simple and fast way to obtain high protein yields. In the present study, we report on the optimization process for the enhanced heterologous production of the Ralstonia eutropha regulatory hydrogenase (RH) in E. coli using autoinduction. These autoinduction methods were combined with the EnPresso B fed-batch like growth system, which applies slow in situ enzymatic glucose release from a polymer to control cell growth and protein synthesis rate.
resultsWe were able to produce 125 mg L
conclusionsThe findings of this study confirm the general feasibility of the developed fed-batch based autoinduction system and provide an alternative to conventional induction systems for efficient recombinant protein production. We believe that the fed-batch based autoinduction system developed herein will favor the heterologous production of larger quantities of difficult-to-express complex enzymes to enable economical production of these kinds of proteins.
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