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Recombinant protein expression in Escherichia coli: advances and challenges.

TLDR
The different approaches for the synthesis of recombinant proteins in E. coli are reviewed and recent progress in this ever-growing field is discussed.
Abstract
Escherichia coli is the organism of choice for the production of recombinant proteins. Its use as a cell factory is well-established and it has become the most popular expression platform. For this reason, there are many molecular tools and protocols at hand for the high-level production of recombinant proteins, such as a vast catalog of expression plasmids, a great number of engineered strains and many cultivation strategies. We review the different approaches for the synthesis of recombinant proteins in E. coli and discuss recent progress in this ever-growing field.

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NanoLuc: A Small Luciferase Is Brightening Up the Field of Bioluminescence.

TL;DR: This review will present the NLuc technology to the scientific community in a nonbiased manner, allowing the audience to adopt their own views of this novel system.
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Design of virus-based nanomaterials for medicine, biotechnology, and energy

TL;DR: This review provides an overview of recent developments in "chemical virology", and surveys the broad distribution of viruses and various methods for producing virus-based nanoparticles, as well as engineering principles used to impart new functionalities.
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A Review of the Microbial Production of Bioactive Natural Products and Biologics.

TL;DR: The structures and diverse biological activities of natural products and recombinant proteins that have been exploited as valuable molecules in medicine, agriculture and insect control are introduced and suggested to inspire the development of new therapeutic agents in academia and industry.
Journal ArticleDOI

Recent Developments in Bioprocessing of Recombinant Proteins: Expression Hosts and Process Development.

TL;DR: Recently, advances have been made in the various areas of bioprocessing and are being utilized to develop effective processes for producing recombinant proteins that can be used as therapeutics, vaccines, and diagnostic reagents.
References
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Journal ArticleDOI

Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes

TL;DR: A gene expression system based on bacteriophage T7 RNA polymerase has been developed and high levels of accumulation suggest that the RNAs are relatively stable, perhaps in part because their great length and/or stem-and-loop structures at their 3' ends help to protect them against exonucleolytic degradation.
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Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase.

TL;DR: Plasmid expression vectors have been constructed that direct the synthesis of foreign polypeptides in Escherichia coli as fusions with the C terminus of Sj26, a 26-kDa glutathione S-transferase (GST; EC 2.5.1.18) encoded by the parasitic helminth Schistosoma japonicum.
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Protein production by auto-induction in high-density shaking cultures

TL;DR: Investigation of factors that affect stability, growth, and induction of T7 expression strains in shaking vessels led to the recognition that sporadic, unintended induction of expression in complex media, previously reported by others, is almost certainly caused by small amounts of lactose.
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Construction and characterization of new cloning vehicles. II. A multipurpose cloning system.

TL;DR: In vitro recombination techniques were used to construct a new cloning vehicle, pBR322, which is a relaxed replicating plasmid, does not produce and is sensitive to colicin E1, and carries resistance genes to the antibiotics ampicillin (Ap) and tetracycline (Tc).
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Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter.

TL;DR: The tight regulation of the PBAD promoter is exploited to study the phenotypes of null mutations of essential genes and the use of pBAD vectors as an expression system is explored.
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What are the challenges in recombinant protein production in osmotolerant E. coli?

The provided paper does not mention the challenges in recombinant protein production in osmotolerant E. coli.