ArticleBiotechnology and bioengineering2020
Scalable, two-stage, autoinduction of recombinant protein expression in E. coli utilizing phosphate depletion.
Article in Biotechnology and bioengineering, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 48 citations in OpenAlex.
- From Design to Practice: A Comprehensive Tutorial for the Rapid Multiplex Engineering ofBio-protocol · 2026Article
- Mechanism-guided control of intracellular alkalinization and process pH for production of recombinant human B-type natriuretic peptide under the cSAT scheme in Escherichia coli.Microbial cell factories · 2026Article
- A foundation model for microbial growth dynamics.bioRxiv : the preprint server for biology · 2025Article
- BioFuse: A programmable timer switch of gene expression.Science advances · 2025Article
- Engineering of bacteria towards programmed autolysis: why, how, and when?Microbial cell factories · 2024Review
- Delaying production with prokaryotic inducible expression systems.Microbial cell factories · 2024Review
- Tobacco Plant: A Novel and Promising Heterologous Bioreactor for the Production of Recombinant Bovine Chymosin.Molecular biotechnology · 2024Article
- Scalable, robust, high-throughput expression & purification of nanobodies enabled by 2-stage dynamic control.Metabolic engineering · 2024Article
- 2-Stage microfermentations.Metabolic engineering communications · 2024Article
- Expression of soluble moloney murine leukemia virus-reverse transcriptase in Escherichia coli BL21 star (DE3) using autoinduction system.Molecular biology reports · 2024Article
- Essential factors, advanced strategies, challenges, and approaches involved for efficient expression of recombinant proteins in Escherichia coli.Archives of microbiology · 2024Review
- Characterizing and utilizing oxygen-dependent promoters for efficient dynamic metabolic engineering.Metabolic engineering · 2023Article
- Strategies for efficient production of recombinant proteins in Escherichia coli: alleviating the host burden and enhancing protein activity.Microbial cell factories · 2022Review
- Decoupling Growth and Production by Removing the Origin of Replication from a Bacterial Chromosome.ACS synthetic biology · 2022Article
- Integrated autolysis, DNA hydrolysis and precipitation enables an improved bioprocess for Q-Griffithsin, a broad-spectrum antiviral and clinical-stage anti-COVID-19 candidate.Biochemical engineering journal · 2022Article
- Simple Scalable Protein Expression and Extraction Using Two-stage Autoinducible Cell Autolysis and DNA/RNA Autohydrolysis inBio-protocol · 2022Article
- Strategies for Glycoengineering Therapeutic Proteins.Frontiers in chemistry · 2022Review
- Dynamic control over feedback regulatory mechanisms improves NADPH flux and xylitol biosynthesis in engineered E. coli.Metabolic engineering · 2021Article
- Low-Cost, Large-Scale Production of the Anti-viral Lectin Griffithsin.Frontiers in bioengineering and biotechnology · 2020Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
We report the scalable production of recombinant proteins in Escherichia coli, reliant on tightly controlled autoinduction, triggered by phosphate depletion in the stationary phase. The method, reliant on engineered strains and plasmids, enables improved protein expression across scales. Expression levels using this approach have reached as high as 55% of the total cellular protein. The initial use of the method in instrumented fed-batch fermentations enables cell densities of ∼30 gCDW/L and protein titers up to 8.1 ± 0.7 g/L (∼270 mg/gCDW). The process has also been adapted to an optimized autoinduction media, enabling routine batch production at culture volumes of 20 μl (384-well plates), 100 μl (96-well plates), 20 ml, and 100 ml. In batch cultures, cell densities routinely reach ∼5-7 gCDW/L, offering protein titers above 2 g/L. The methodology has been validated with a set of diverse heterologous proteins and is of general use for the facile optimization of routine protein expression from high throughput screens to fed-batch fermentation.
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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.