ArticleApplied microbiology and biotechnology2017
A novel method to recover inclusion body protein from recombinant E. coli fed-batch processes based on phage ΦX174-derived lysis protein E.
Article in Applied microbiology and biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 27 citations in OpenAlex.
- The recombinant protein of scorpion venom phospholipase A2 exhibits potential anti-leishmanial activity.Scientific reports · 2025Article
- Enhancing extracellular production of lipoxygenase in Escherichia coli by signal peptides and autolysis system.Microbial cell factories · 2022Article
- Optimizing the Preparation Procedure of Recombinant PSCA, as a Practical Biomarker in Prostate Cancer.Iranian journal of biotechnology · 2021Article
- A novel autolysis system for extracellular production and direct immobilization of a phospholipase D fused with cellulose binding domain.BMC biotechnology · 2019Article
- Recent Developments in Bioprocessing of Recombinant Proteins: Expression Hosts and Process Development.Frontiers in bioengineering and biotechnology · 2019Review
- Secretion of recombinant proteins fromEngineering in life sciences · 2018Review
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Production of recombinant proteins as inclusion bodies is an important strategy in the production of technical enzymes and biopharmaceutical products. So far, protein from inclusion bodies has been recovered from the cell factory through mechanical or chemical disruption methods, requiring additional cost-intensive unit operations. We describe a novel method that is using a bacteriophage-derived lysis protein to directly recover inclusion body protein from Escherichia coli from high cell density fermentation process: The recombinant inclusion body product is expressed by using a mixed feed fed-batch process which allows expression tuning via adjusting the specific uptake rate of the inducing substrate. Then, bacteriophage ΦX174-derived lysis protein E is expressed to induce cell lysis. Inclusion bodies in empty cell envelopes are harvested via centrifugation of the fermentation broth. A subsequent solubilization step reveals the recombinant protein. The process was investigated by analyzing the impact of fermentation conditions on protein E-mediated cell lysis as well as cell lysis kinetics. Optimal cell lysis efficiencies of 99% were obtained with inclusion body titers of >2.0 g/l at specific growth rates higher 0.12 h
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