ArticleMicrobial cell factories2015
Identification of a heterologous cellulase and its N-terminus that can guide recombinant proteins out of Escherichia coli.
Article 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 18 papers.
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Who cites it
18 citing papers in PubMed, 48 citations in OpenAlex.
- Advances, challenges, and future directions towards a cellulolytic Escherichia coli.Biotechnology for biofuels and bioproducts · 2026Review
- A high throughput assay for measuring secreted protein based on a de novo fluorescent reporter reveals regulatory and structural insights in Salmonella type three secretion system.Protein science : a publication of the Protein Society · 2025Article
- The N-terminus of Lactobacillus amylovorus feruloyl esterase plays an important role in its secretion by Lactobacillus plantarum and Escherichia coli.Microbial cell factories · 2021Article
- Perturbation of the peptidoglycan network and utilization of the signal recognition particle-dependent pathway enhances the extracellular production of a truncational mutant of CelA in Escherichia coli.Journal of industrial microbiology & biotechnology · 2021Article
- Hybrid Living Capsules Autonomously Produced by Engineered Bacteria.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021Article
- Consolidated Bioprocessing: Synthetic Biology Routes to Fuels and Fine Chemicals.Microorganisms · 2021Review
- Heterologous Expression of Lignocellulose-Modifying Enzymes in Microorganisms: Current Status.Molecular biotechnology · 2021Review
- Comparison of Enzyme Secretion and Ferulic Acid Production byFrontiers in microbiology · 2020Article
- Flavin-Based Fluorescent Protein EcFbFP Auto-Guided Surface Display of Methyl Parathion Hydrolase in Escherichia coli.Molecular biotechnology · 2019Article
- Identification and characterization of an Endo-glucanase secreted from cellulolytic Escherichia coli ZH-4.BMC biotechnology · 2019Article
- Developing Gram-negative bacteria for the secretion of heterologous proteins.Microbial cell factories · 2018Review
- Review
- A novel Ffu fusion system for secretory expression of heterologous proteins in Escherichia coli.Microbial cell factories · 2017Article
- Non-peptide guided auto-secretion of recombinant proteins by super-folder green fluorescent protein in Escherichia coli.Scientific reports · 2017Article
- Multimer recognition and secretion by the non-classical secretion pathway in Bacillus subtilis.Scientific reports · 2017Article
- Current strategies for protein production and purification enabling membrane protein structural biology.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2016Review
- OmpA signal peptide leads to heterogenous secretion of B. subtilis chitosanase enzyme from E. coli expression system.SpringerPlus · 2016Article
- Construction of cellulose-utilizing Escherichia coli based on a secretable cellulase.Microbial cell factories · 2015Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe Gram-negative bacterium Escherichia coli has been widely used as a cell factory for the production of proteins and specialty chemicals because it is the best characterized host with many available expression and regulation systems. However, recombinant proteins produced in Escherichia coli are generally intracellular and often found in the form of inclusion bodies. Extracellular production of proteins is advantageous compared with intracellular production because extracellular proteins can be purified more easily and can avoid protease attack, which results in higher product quality. In this study, we found a catalytic domain of a cellulase (Cel-CD) and its N-terminus can be employed as carriers for extracellular production of recombinant proteins.
resultsIn this report, we identified the catalytic domain of a cellulase (Cel-CD) from Bacillus sp. that can be secreted into the medium from recombinant E. coli BL21 (DE3) in large quantities without its native signal peptide. By subcellular location analysis, we proved that the secretion was a two-step process and the N-terminal sequence of the full length Cel-CD played a crucial function in secretion. Both the Cel-CD and its N-terminal sequence can serve as carriers for efficient extracellular production of select target proteins.
conclusionsFusion of heterologous proteins with N20 from Cel-CD can carry the target proteins out of the cells with a concentration from 101 to 691 mg/L in flask cultivation. The extracellular recombinant proteins with a relative high purity. The results suggested that this system has a potential application in plant biomass conversion and industrial production of enzymes and therapeutic proteins.
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