ReviewThe protein journal2013
Strategies for the production of recombinant protein in Escherichia coli.
Review in The protein journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.
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Who cites it
103 citing papers in PubMed.
- A recombinant xylose reductase enzyme with biotechnological potential for xylitol production.Archives of microbiology · 2026Article
- Designing the Next Generation of Endolysins: A Triple Strategy Integrating Bioinformatics Mining, Engineering Modification and Encapsulation Formulation.Probiotics and antimicrobial proteins · 2026Review
- Expression and identification of a novel high-activity recombinant humanized type I collagen SynthCol1 in Pichia pastoris GS115.Applied microbiology and biotechnology · 2026Article
- A novel stationary phase approach for improved recombinant protein expression in Escherichia coli: beyond the exponential phase.Microbial cell factories · 2026Article
- Protein-inducible ribosomal frameshifting enables programmable translational control for genetic circuit design in Escherichia coli.Journal of biological engineering · 2026Article
- Development and application of an ANN-perception-based autonomous control system forFrontiers in microbiology · 2026Article
- Designing an optimized strategy for extracellular expression of recombinant human TNF-α inFrontiers in bioengineering and biotechnology · 2026Article
- Therapeutic Promise and Biotechnological Prospects ofInternational journal of molecular sciences · 2025Review
- Cloning, expression, purification, and characterization of glutamate decarboxylase (Rv3432c) from Mycobacterium tuberculosis.International microbiology : the official journal of the Spanish Society for Microbiology · 2025Article
- Improving the Accumulation and Solubility of Human Interferon-γ (hIFN-γ) in Escherichia coli: A Fusion Protein-Based Method and Network Pharmacology Analysis.Applied biochemistry and biotechnology · 2025Article
- Purification and Evaluation of the Biological Activity of Recombinant Mouse Prolactin.Journal of microbiology and biotechnology · 2025Article
- Extracellular peptide production in Escherichia coli by inducible downregulation of lipoprotein Lpp via MicL sRNA.Applied microbiology and biotechnology · 2025Article
- Increasing recombinant protein production in E. coli via FACS-based selection of N-terminal coding DNA libraries.The FEBS journal · 2025Article
- A review on computational models for predicting protein solubility.Journal of microbiology (Seoul, Korea) · 2025Review
- A comparative guide to expression systems for phage lysin production.Essays in biochemistry · 2024Review
- Improved recombinant expression of soluble cathepsin B and L in Escherichia coli.Applied microbiology and biotechnology · 2024Article
- Computer-Aided Design to Improve the Thermal Stability ofFoods (Basel, Switzerland) · 2024Article
- A robust high-throughput screening system to assess bacterial tyrosine ammonia lyase activity in the context of tyrosine inherited metabolic disorders.Scientific reports · 2024Article
- Application and research progress of MultiBac: A review.Medicine · 2024Review
- Discovery, characterization, and comparative analysis of new UGT72 and UGT84 family glycosyltransferases.Communications chemistry · 2024Article
43 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the recent past years, a large number of proteins have been expressed in Escherichia coli with high productivity due to rapid development of genetic engineering technologies. There are many hosts used for the production of recombinant protein but the preferred choice is E. coli due to its easier culture, short life cycle, well-known genetics, and easy genetic manipulation. We often face a problem in the expression of foreign genes in E. coli. Soluble recombinant protein is a prerequisite for structural, functional and biochemical studies of a protein. Researchers often face problems producing soluble recombinant proteins for over-expression, mainly the expression and solubility of heterologous proteins. There is no universal strategy to solve these problems but there are a few methods that can improve the level of expression, non-expression, or less expression of the gene of interest in E. coli. This review addresses these issues properly. Five levels of strategies can be used to increase the expression and solubility of over-expressed protein; (1) changing the vector, (2) changing the host, (3) changing the culture parameters of the recombinant host strain, (4) co-expression of other genes and (5) changing the gene sequences, which may help increase expression and the proper folding of desired protein. Here we present the resources available for the expression of a gene in E. coli to get a substantial amount of good quality recombinant protein. The resources include different strains of E. coli, different E. coli expression vectors, different physical and chemical agents and the co expression of chaperone interacting proteins. Perhaps it would be the solutions to such problems that will finally lead to the maturity of the application of recombinant proteins. The proposed solutions to such problems will finally lead to the maturity of the application of recombinant proteins.
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Registered trials
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