ArticleApplied microbiology and biotechnology2018
Teaching an old pET new tricks: tuning of inclusion body formation and properties by a mixed feed system in E. coli.
Article in Applied microbiology and biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.
What it found
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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.
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Who cites it
25 citing papers in PubMed, 1 synthesis or guideline pooled it, 48 citations in OpenAlex.
- A Guideline to Set Up Cascaded Continuous Cultivation with E. coli Bl21 (DE3).Methods in molecular biology (Clifton, N.J.) · 2022Guideline
- Catalytically active inclusion bodies of Bacillus clausii laccase protein recombinantly produced in E. coli for dye decolorization.Microbial cell factories · 2026Article
- Lysis and IB washing procedures significantly impact the recovery of rHumanized ranibizumab from inclusion bodies expressed in Escherichia coli.Bioprocess and biosystems engineering · 2026Article
- The Missing Link: Connecting Cultivation Conditions and Refolding Performance via Inclusion Body Biophysical Properties.Biotechnology and bioengineering · 2025Article
- Fundamental insights in early-stage inclusion body formation.Microbial biotechnology · 2023Article
- Unlocking the strength of inducible promoters in Gram-negative bacteria.Microbial biotechnology · 2023Article
- Scaling production of GFP1-10 detector protein in E. coli for secretion screening by split GFP assay.Microbial cell factories · 2021Article
- Cascaded processing enables continuous upstream processing with E. coli BL21(DE3).Scientific reports · 2021Article
- Construction of an AI-2 quorum sensing induced heterologous protein expression system inPeerJ · 2021Article
- Production of Active Recombinant Hyaluronidase Inclusion Bodies fromInternational journal of molecular sciences · 2020Article
- The Effects of Lactose Induction on a Plasmid-FreeBioengineering (Basel, Switzerland) · 2020Article
- High-yield production of recombinant platelet factor 4 by harnessing and honing the gram-negative bacterial secretory apparatus.PloS one · 2020Article
- The LazarusFrontiers in bioengineering and biotechnology · 2020Article
- Repetitive Fed-Batch: A Promising Process Mode for Biomanufacturing WithFrontiers in bioengineering and biotechnology · 2020Article
- The impact of technical failures during cultivation of an inclusion body process.Bioprocess and biosystems engineering · 2019Article
- New tools for recombinant protein production in Escherichia coli: A 5-year update.Protein science : a publication of the Protein Society · 2019Review
- Perspectives of inclusion bodies for bio-based products: curse or blessing?Applied microbiology and biotechnology · 2019Review
- The Rocky Road From Fed-Batch to Continuous Processing WithFrontiers in bioengineering and biotechnology · 2019Review
- Boosting Recombinant Inclusion Body Production-From Classical Fed-Batch Approach to Continuous Cultivation.Frontiers in bioengineering and biotechnology · 2019Article
- Engineered E. coli W enables efficient 2,3-butanediol production from glucose and sugar beet molasses using defined minimal medium as economic basis.Microbial cell factories · 2018Article
Corrections and comments
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
Abstract
Against the outdated belief that inclusion bodies (IBs) in Escherichia coli are only inactive aggregates of misfolded protein, and thus should be avoided during recombinant protein production, numerous biopharmaceutically important proteins are currently produced as IBs. To obtain correctly folded, soluble product, IBs have to be processed, namely, harvested, solubilized, and refolded. Several years ago, it was discovered that, depending on cultivation conditions and protein properties, IBs contain partially correctly folded protein structures, which makes IB processing more efficient. Here, we present a method of tailored induction of recombinant protein production in E. coli by a mixed feed system using glucose and lactose and its impact on IB formation. Our method allows tuning of IB amount, IB size, size distribution, and purity, which does not only facilitate IB processing, but is also crucial for potential direct applications of IBs as nanomaterials and biomaterials in regenerative medicine.
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Registered trials
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.