ReviewMicrobial cell factories2015
Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process.
Review in Microbial cell factories, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 175 papers, 1 of them a synthesis that pooled it.
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Who cites it
175 citing papers in PubMed, 1 synthesis or guideline pooled it, 498 citations in OpenAlex.
- Recombinant expression of insoluble enzymes in Escherichia coli: a systematic review of experimental design and its manufacturing implications.Microbial cell factories · 2021Pooled it
- Gene Cloning, Expression, and Purification of Kunitz Trypsin Inhibitor from Glycine max Using Halo Tag.Molecular biotechnology · 2026Article
- Nucleases and Their Inhibitors: Exploring Biological Roles, Industrial Applications, and Challenges in Heterologous Expression.Biotechnology journal · 2026Review
- Article
- Optimization and production of a GLP-grade recombinant Sm29 vaccine against schistosomiasis: From expression to preclinical assessment.PLoS neglected tropical diseases · 2026Article
- Structure-Guided Discovery of a Cold-Responsive Antifreeze-like Protein from AntarcticMicroorganisms · 2026Article
- Overcoming cellular secretion bottlenecks: advanced secretion engineering and molecular tailoring for next-generation microbial α-amylases with enhanced industrial performance.World journal of microbiology & biotechnology · 2026Review
- A Simple Method to Produce Recombinant Mammalian Serum Albumins inInternational journal of molecular sciences · 2026Article
- Advances, challenges, and future directions towards a cellulolytic Escherichia coli.Biotechnology for biofuels and bioproducts · 2026Review
- High-Yield Expression of Arylmalonate Decarboxylase in Escherichia coli Through High-Cell-Density Cultivation Strategies.Chembiochem : a European journal of chemical biology · 2026Article
- Comparative Analysis of Banana Lectins rBanLec-Like and H84T-BanLec: An In Silico and In Vitro Approach.The protein journal · 2026Article
- The response surface method enables efficient optimization of induction parameters for the production of bioactive peptides in fed-batch bioreactors using Escherichia coli.Folia microbiologica · 2026Article
- Cloning, Expression, Purification and Biological Activity Analysis of Recombinant Helicobacter pylori FabI as a Drug Target.Molecular biotechnology · 2026Article
- Lysis and IB washing procedures significantly impact the recovery of rHumanized ranibizumab from inclusion bodies expressed in Escherichia coli.Bioprocess and biosystems engineering · 2026Article
- The landscape of antibody production systems: recombinant expression for research, diagnostics and therapy.Frontiers in bioengineering and biotechnology · 2026Review
- Optimization of Recombinant Human Interferon-Gamma Expression and Purification inBiologics : targets & therapy · 2026Article
- Heterologous expression and functional characterization of recombinant arenin to assess its anticancer and wound-healing potential.Bioresources and bioprocessing · 2025Article
- The Missing Link: Connecting Cultivation Conditions and Refolding Performance via Inclusion Body Biophysical Properties.Biotechnology and bioengineering · 2025Article
- Catalytically active inclusion bodies of cold-adapted lipase: production and its industrial potential.AMB Express · 2025Article
- Generation and Purification of RANKL-Derived Small-Fragment Variants for Osteoclast Inhibition.Pharmaceutics · 2025Article
115 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Formation of inclusion bodies in bacterial hosts poses a major challenge for large scale recovery of bioactive proteins. The process of obtaining bioactive protein from inclusion bodies is labor intensive and the yields of recombinant protein are often low. Here we review the developments in the field that are targeted at improving the yield, as well as quality of the recombinant protein by optimizing the individual steps of the process, especially solubilization of the inclusion bodies and refolding of the solubilized protein. Mild solubilization methods have been discussed which are based on the understanding of the fact that protein molecules in inclusion body aggregates have native-like structure. These methods solubilize the inclusion body aggregates while preserving the native-like protein structure. Subsequent protein refolding and purification results in high recovery of bioactive protein. Other parameters which influence the overall recovery of bioactive protein from inclusion bodies have also been discussed. A schematic model describing the utility of mild solubilization methods for high throughput recovery of bioactive protein has also been presented.
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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.