ArticleMicrobial cell factories2017
Efficient soluble expression of disulfide bonded proteins in the cytoplasm of Escherichia coli in fed-batch fermentations on chemically defined minimal media.
Article in Microbial cell factories, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 98 citations in OpenAlex.
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- High-cell-density Escherichia coli-based nanobody production: benchmarking of subcellular targeting, strain background and process development strategies.Microbial cell factories · 2026Article
- Overcoming cellular secretion bottlenecks: advanced secretion engineering and molecular tailoring for next-generation microbial α-amylases with enhanced industrial performance.World journal of microbiology & biotechnology · 2026Review
- Designing strategies for high-level production of peptide-N-glycosidase F (PNGase F) from Flavobacterium meningosepticum using high cell density fed-batch culture of E. coli.Bioprocess and biosystems engineering · 2026Article
- Systematic determination of disulfide bond reduction potentials reveals a nonequilibrium redox hierarchy in cyanobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Optimization of an improved chemically defined medium for high-efficiency expression of glucokinase in Escherichia coli.Microbial cell factories · 2026Article
- Conkazal-M1 from the MKAVA family of conotoxins: A dual-function protease inhibitor and neuroactive peptide.Protein science : a publication of the Protein Society · 2026Article
- Designing an optimized strategy for extracellular expression of recombinant human TNF-α inFrontiers in bioengineering and biotechnology · 2026Article
- The landscape of antibody production systems: recombinant expression for research, diagnostics and therapy.Frontiers in bioengineering and biotechnology · 2026Review
- Conkazal-M1 from the MKAVA family of conotoxins - a dual-function protease inhibitor and neuroactive peptide.bioRxiv : the preprint server for biology · 2025Article
- Structural similarities reveal an expansive conotoxin family with a two-finger toxin fold.Protein science : a publication of the Protein Society · 2025Article
- Hydrophobin-Coated Echogenic Microbubbles for Molecular Targeting of Tumor Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Enhancing recombinant growth factor and serum protein production for cultivated meat manufacturing.Microbial cell factories · 2025Review
- Papain expression in theApplied and environmental microbiology · 2025Article
- Scalable, robust, high-throughput expression & purification of nanobodies enabled by 2-stage dynamic control.Metabolic engineering · 2024Article
- Article
- Production and Purification of Cysteine-Rich Leptospiral Virulence-Modifying Proteins with or Without mCherry Fusion.The protein journal · 2023Article
- Growth hormone receptor agonists and antagonists: From protein expression and purification to long-acting formulations.Protein science : a publication of the Protein Society · 2023Review
- Biochemical analysis of Komagataella phaffii oxidative folding proposes novel regulatory mechanisms of disulfide bond formation in yeast.Scientific reports · 2023Article
- A previously unrecognized superfamily of macro-conotoxins includes an inhibitor of the sensory neuron calcium channel Cav2.3.PLoS biology · 2023Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe production of recombinant proteins containing disulfide bonds in Escherichia coli is challenging. In most cases the protein of interest needs to be either targeted to the oxidizing periplasm or expressed in the cytoplasm in the form of inclusion bodies, then solubilized and re-folded in vitro. Both of these approaches have limitations. Previously we showed that soluble expression of disulfide bonded proteins in the cytoplasm of E. coli is possible at shake flask scale with a system, known as CyDisCo, which is based on co-expression of a protein of interest along with a sulfhydryl oxidase and a disulfide bond isomerase. With CyDisCo it is possible to produce disulfide bonded proteins in the presence of intact reducing pathways in the cytoplasm.
resultsHere we scaled up production of four disulfide bonded proteins to stirred tank bioreactors and achieved high cell densities and protein yields in glucose fed-batch fermentations, using an E. coli strain (BW25113) with the cytoplasmic reducing pathways intact. Even without process optimization production of purified human single chain IgA
conclusionsOur results show for the first time that efficient production of high yields of soluble disulfide bonded proteins in the cytoplasm of E. coli with the reducing pathways intact is feasible to scale-up to bioreactor cultivations on chemically defined minimal media.
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