ArticleBiotechnology progress2020
Extraction of recombinant periplasmic proteins under industrially relevant process conditions: Selectivity and yield strongly depend on protein titer and methodology.
Article in Biotechnology progress, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed, 26 citations in OpenAlex.
- A scalable recombinant pipeline for disulphide-stapled peptides.bioRxiv : the preprint server for biology · 2026Article
- Towards scalable production of recombinant EIT as a protective antigen against EHEC.Bioprocess and biosystems engineering · 2026Article
- Mechanisms underlying allosteric modulation of antiseizure medication binding to synaptic vesicle protein 2A (SV2A).Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Recombinant Production of Novel Bovine Lactoferricin Engineered Peptide Using Molecular Dynamics Simulation.Archives of Razi Institute · 2025Article
- Extracellular peptide production in Escherichia coli by inducible downregulation of lipoprotein Lpp via MicL sRNA.Applied microbiology and biotechnology · 2025Article
- A production platform for disulfide-bonded peptides in the periplasm of Escherichia coli.Microbial cell factories · 2024Article
- Recombinant Peptide Production SoftensInternational journal of molecular sciences · 2023Article
- Extraction of recombinant periplasmic proteins under industrially relevant process conditions: Selectivity and yield strongly depend on protein titer and methodology.Biotechnology progress · 2020Article
- Selective Release of Recombinant Periplasmic Protein FromFrontiers in bioengineering and biotechnology · 2020Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
In this work, we attempted to identify a method for the selective extraction of periplasmic endogenously expressed proteins, which is applicable at an industrial scale. For this purpose, we used an expression model that allows coexpression of two fluorescent proteins, each of which is specifically targeted to either the cytoplasm or periplasm. We assessed a number of scalable lysis methods (high-pressure homogenization, osmotic shock procedures, extraction with ethylenediaminetetraacetic acid, and extraction with deoxycholate) for the ability to selectively extract periplasmic proteins rather than cytoplasmic proteins. Our main conclusion was that although we identified industrially scalable lysis conditions that significantly increased the starting purity for further purification, none of the tested conditions were selective for periplasmic protein over cytoplasmic protein. Furthermore, we demonstrated that efficient extraction of the expressed recombinant proteins was largely dependent on the overall protein concentration in the cell.
Indexed as
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What OpenQuestion holds
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.