ArticleMicrobial cell factories2014
Influence of pH control in the formation of inclusion bodies during production of recombinant sphingomyelinase-D in Escherichia coli.
Article in Microbial cell factories, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 53 citations in OpenAlex.
- The effect of monomers number in peptides on Escherichia coli strain productivity and inclusion bodies-associated target protein accumulation.Folia microbiologica · 2026Article
- Sequence-Encoded Aggregation of AA10 LPMO Domains as a Basis for Inclusion Body Design.International journal of molecular sciences · 2026Article
- The Missing Link: Connecting Cultivation Conditions and Refolding Performance via Inclusion Body Biophysical Properties.Biotechnology and bioengineering · 2025Article
- Recovery of mouse growth hormone from E. coli inclusion bodies using a mild solubilisation and repeated freeze-thaw approach.Molecular biology reports · 2025Article
- The Development of Epitope-Based Recombinant Protein Vaccines against SARS-CoV-2.The AAPS journal · 2024Review
- Immunomodulation Evidence of Nanostructured Recombinant Proteins in Salmonid Cells.Animals : an open access journal from MDPI · 2024Article
- Fundamental insights in early-stage inclusion body formation.Microbial biotechnology · 2023Article
- Process intensification at the expression system level for the production of 1-phosphate aldolase in antibiotic-free E. coli fed-batch cultures.Journal of industrial microbiology & biotechnology · 2022Article
- The pre-induction temperature affects recombinant HuGM-CSF aggregation in thermoinducible Escherichia coli.Applied microbiology and biotechnology · 2022Article
- Transcutaneous Flexible Sensor forACS sensors · 2022Article
- Toxicity Profiling of Bacterial Inclusion Bodies in Human Caco-2 Cells.Frontiers in bioengineering and biotechnology · 2022Article
- Coiled-Coil Based Inclusion Bodies and Their Potential Applications.Frontiers in bioengineering and biotechnology · 2021Review
- Challenges Associated With the Formation of Recombinant Protein Inclusion Bodies inFrontiers in bioengineering and biotechnology · 2021Review
- [Expression, purification and functional assessment of asprosin inclusion body].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2020Article
- Recombinant production of ESAT-6 antigen in thermoinducible Escherichia coli: the role of culture scale and temperature on metabolic response, expression of chaperones, and architecture of inclusion bodies.Cell stress & chaperones · 2019Article
- Perspectives of inclusion bodies for bio-based products: curse or blessing?Applied microbiology and biotechnology · 2019Review
- Custom made inclusion bodies: impact of classical process parameters and physiological parameters on inclusion body quality attributes.Microbial cell factories · 2018Article
- Expression and Characterization of Recombinant Sucrose Phosphorylase.The protein journal · 2018Article
- Production of a recombinant phospholipase A2 in Escherichia coli using resonant acoustic mixing that improves oxygen transfer in shake flasks.Microbial cell factories · 2017Article
- High-throughput recombinant protein expression in Escherichia coli: current status and future perspectives.Open biology · 2016Review
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundInclusion bodies (IBs) are aggregated proteins that form clusters when protein is overexpressed in heterologous expression systems. IBs have been considered as non-usable proteins, but recently they are being used as functional materials, catalytic particles, drug delivery agents, immunogenic structures, and as a raw material in recombinant therapeutic protein purification. However, few studies have been made to understand how culture conditions affect the protein aggregation and the physicochemical characteristics that lead them to cluster. The objective of our research was to understand how pH affects the physicochemical properties of IBs formed by the recombinant sphingomyelinase-D of tick expressed in E. coli BL21-Gold (DE3) by evaluating two pH culture strategies.
resultsUncontrolled pH culture conditions favored recombinant sphingomyelinase-D aggregation and IB formation. The IBs of sphingomyelinase-D produced under controlled pH at 7.5 and after 24 h were smaller (<500 nm) than those produced under uncontrolled pH conditions (>500 nm). Furthermore, the composition, conformation and β-structure formation of the aggregates were different. Under controlled pH conditions in comparison to uncontrolled conditions, the produced IBs presented higher resistance to denaturants and proteinase-K degradation, presented β-structure, but apparently as time passes the IBs become compacted and less sensitive to amyloid dye binding.
conclusionsThe manipulation of the pH has an impact on IB formation and their physicochemical characteristics. Particularly, uncontrolled pH conditions favored the protein aggregation and sphingomyelinase-D IB formation. The evidence may lead to find methodologies for bioprocesses to obtain biomaterials with particular characteristics, extending the application possibilities of the inclusion bodies.
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