ArticlePloS one2011
An approach to the production of soluble protein from a fungal gene encoding an aggregation-prone xylanase in Escherichia coli.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 25 citations in OpenAlex.
- In Silico Analysis and Development of the Secretory Expression of D-Psicose-3-Epimerase inMicroorganisms · 2024Article
- Production, purification, characterization, and safety evaluation of constructed recombinant D-psicose 3-epimerase.Microbial cell factories · 2024Article
- Preparation of Sweet Potato Porous Starch by Marine Dextranase and Its Adsorption Characteristics.Foods (Basel, Switzerland) · 2024Article
- Article
- Production of Neoagaro-Oligosaccharides With Various Degrees of Polymerization by Using a Truncated Marine Agarase.Frontiers in microbiology · 2020Article
- Expression and Functional Properties of an Anti-Triazophos High-Affinity Single-Chain Variable Fragment Antibody with Specific Lambda Light Chain.International journal of molecular sciences · 2016Article
- Enhancing the secretion efficiency and thermostability of a Bacillus deramificans pullulanase mutant (D437H/D503Y) by N-terminal domain truncation.Applied and environmental microbiology · 2015Article
- Heterologous expression, purification, crystallization and preliminary X-ray analysis of Trichoderma reesei xylanase II and four variants.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Tat peptide-mediated soluble expression of the membrane protein LSECtin-CRD in Escherichia coli.PloS one · 2013Article
- Enhanced soluble expression of a thermostable cellulase from Clostridium thermocellum in Escherichia coli.Current microbiology · 2011Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The development of new procedures and protocols that allow researchers to obtain recombinant proteins is of fundamental importance in the biotechnology field. A strategy was explored to overcome inclusion-body formation observed when expressing an aggregation-prone fungal xylanase in Escherichia coli. pHsh is an expression plasmid that uses a synthetic heat-shock (Hsh) promoter, in which gene expression is regulated by an alternative sigma factor (σ(32)). A derivative of pHsh was constructed by fusing a signal peptide to xynA2 gene to facilitate export of the recombinant protein to the periplasm. The xylanase was produced in a soluble form. Three factors were essential to achieving such soluble expression of the xylanase: 1) the target gene was under the control of the Hsh promoter, 2) the gene product was exported into the periplasm, and 3) gene expression was induced by a temperature upshift. For the first time we report the expression of periplasmic proteins under the control of an Hsh promoter regulated by σ(32). One unique feature of this approach was that over 200 copies of the Hsh promoter in an E. coli cell significantly increased the concentration of σ(32). The growth inhibition of the recombinant cells corresponded to an increase in the levels of soluble periplasmic protein. Therefore, an alternative protocol was designed to induce gene expression from pHsh-ex to obtain high levels of active soluble enzymes.
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