ArticleScientific reports2019
Optimization of culture conditions for the expression of three different insoluble proteins in Escherichia coli.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
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- The p40 fusion domain as a scaffold for producing functional inclusion bodies.Applied microbiology and biotechnology · 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
- A fully human IgG1 antibody targeting MICA α1 domain inhibits interaction with NKG2D and activates immune effector functions against MICA-expressing cells.Frontiers in immunology · 2026Article
- The Missing Link: Connecting Cultivation Conditions and Refolding Performance via Inclusion Body Biophysical Properties.Biotechnology and bioengineering · 2025Article
- Identification of a novel D-amino acid oxidase and its application in deracemization of D, L-phosphinothricin.Bioprocess and biosystems engineering · 2025Article
- Expression and functional characterization of an anti-CD22 scFv targeting B-cell malignancies.Research in pharmaceutical sciences · 2025Article
- A review on computational models for predicting protein solubility.Journal of microbiology (Seoul, Korea) · 2025Review
- Optimizing recombinant production of L-asparaginase 1 from Saccharomyces cerevisiae using response surface methodology.Folia microbiologica · 2024Article
- Identification and analysis of the key genes for Escherichia coli heterologous protein expression by transcriptomic profiling.Molecular biology reports · 2024Article
- Non-Invasive Delivery of Negatively Charged Nanobodies by Anodal Iontophoresis: When Electroosmosis Dominates Electromigration.Pharmaceutics · 2024Article
- Characterization of a novel amidohydrolase with promiscuous esterase activity from a soil metagenomic library and its application in degradation of amide herbicides.Environmental science and pollution research international · 2024Article
- SERS-based microdroplet platform for high-throughput screening ofFrontiers in bioengineering and biotechnology · 2024Article
- TIR domains of TLR family-from the cell culture to the protein sample for structural studies.PloS one · 2024Article
- Cloning, Expression and Functional Characterization of a Novel α-Humulene Synthase, Responsible for the Formation of Sesquiterpene in Agarwood Originating fromCurrent issues in molecular biology · 2023Article
- Prokaryotic Expression, Purification, and Antibacterial Activity of the Hepcidin Peptide of Crescent Sweetlips (Current issues in molecular biology · 2023Article
- Efficient recombinant production of mouse-derived cryptdin family peptides by a novel facilitation strategy for inclusion body formation.Microbial cell factories · 2023Article
- Heterologous expression, molecular studies and biochemical characterization of a novel alkaline esterase gene fromRSC advances · 2022Article
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9 authors.
Funding
Abstract
Recombinant protein expression for structural and therapeutic applications requires the use of systems with high expression yields. Escherichia coli is considered the workhorse for this purpose, given its fast growth rate and feasible manipulation. However, bacterial inclusion body formation remains a challenge for further protein purification. We analyzed and optimized the expression conditions for three different proteins: an anti-MICA scFv, MICA, and p19 subunit of IL-23. We used a response surface methodology based on a three-level Box-Behnken design, which included three factors: post-induction temperature, post-induction time and IPTG concentration. Comparing this information with soluble protein data in a principal component analysis revealed that insoluble and soluble proteins have different optimal conditions for post-induction temperature, post-induction time, IPTG concentration and in amino acid sequence features. Finally, we optimized the refolding conditions of the least expressed protein, anti-MICA scFv, using a fast dilution protocol with different additives, obtaining soluble and active scFv for binding assays. These results allowed us to obtain higher yields of proteins expressed in inclusion bodies. Further studies using the system proposed in this study may lead to the identification of optimal environmental factors for a given protein sequence, favoring the acceleration of bioprocess development and structural studies.
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