ArticleAdvanced pharmaceutical bulletin2015
Effects of Environmental Factors on Soluble Expression of a Humanized Anti-TNF-α scFv Antibody in Escherichia coli.
Article in Advanced pharmaceutical bulletin, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
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- Machine learning modeling for solubility prediction of recombinant antibody fragment in four different E. coli strains.Scientific reports · 2022Article
- Review
- Statistical optimization of culture conditions for expression of recombinant humanized anti-EpCAM single-chain antibody using response surface methodology.Research in pharmaceutical sciences · 2021Article
- Challenges Associated With the Formation of Recombinant Protein Inclusion Bodies inFrontiers in bioengineering and biotechnology · 2021Review
- Evolution ofInternational journal of molecular sciences · 2020Review
- Improved production of the recombinant phospholipase A1 from3 Biotech · 2020Article
- The Effects of Lactose Induction on a Plasmid-FreeBioengineering (Basel, Switzerland) · 2020Article
- Design and Construction of a Novel Humanized Single-Chain Variable-Fragment Antibody Against the Tumor Necrosis Factor Alpha.Iranian journal of pharmaceutical research : IJPR · 2019Article
- E. coli HMS174(DE3) is a sustainable alternative to BL21(DE3).Microbial cell factories · 2018Article
- Teaching an old pET new tricks: tuning of inclusion body formation and properties by a mixed feed system in E. coli.Applied microbiology and biotechnology · 2018Article
- Mechanistic platform knowledge of concomitant sugar uptake in Escherichia coli BL21(DE3) strains.Scientific reports · 2017Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeThe bacterial cultivation conditions for obtaining anti-TNF-α single chain variable fragment (scFv) antibody as the soluble product in E. coli was investigated.
methodsTo avoid the production of inclusion bodies, the effects of lactose, IPTG, incubation time, temperature, shaking protocol, medium additives (Mg+2, sucrose), pH, osmotic and heat shocks were examined. Samples from bacterial growth conditions with promising results of soluble expression of GST-hD2 scFv were affinity purified and quantified by SDS-PAGE and image processing for further evaluation.
resultsThe results showed that cultivation in LB medium under induction by low concentrations of lactose and incubation at 10 °C led to partial solubilization of the expressed anti-TNF-α scFv (GST-hD2). Other variables which showed promising increase in soluble expression of GST-hD2 were osmotic shock and addition of magnesium chloride. Furthermore, addition of sucrose to medium suppressed the expression of scFv completely. The other finding was that the addition of sorbitol decreased the growth rate of bacteria.
conclusionIt can be concluded that low cultivation temperature in the presence of low amount of inducer under a long incubation time or addition of magnesium chloride are the most effective environmental factors studied for obtaining the maximum solubilization of GST-hD2 recombinant protein.
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