ArticleMicrobial cell factories2021
A novel protein fusion partner, carbohydrate-binding module family 66, to enhance heterologous protein expression in Escherichia coli.
Article in Microbial cell factories, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 40 citations in OpenAlex.
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- Cis-Acting Chaperoning by Macromolecular Tethering: A Built-In Layer of Cellular Chaperoning.International journal of molecular sciences · 2026Review
- Improving Yield and Thermostability of PETase as a Maltose Binding Protein Fusion in the Periplasm ofInternational journal of molecular sciences · 2026Article
- Beyond Purification: Evolving Roles of Fusion Tags in Biotechnology.Current issues in molecular biology · 2025Review
- EngineeringInternational journal of molecular sciences · 2025Review
- Improving the Catalytic Activity and Thermostability of FAST-PETase with a Multifunctional Short Peptide.Biomolecules · 2025Article
- Therapeutic Peptides: Recent Advances in Discovery, Synthesis, and Clinical Translation.International journal of molecular sciences · 2025Review
- Cloning, heterologous expression and characterization of β-glucosidase deriving from3 Biotech · 2024Article
- Display of PETase on the Cell Surface of Escherichia coli Using the Anchor Protein PgsA.Applied biochemistry and biotechnology · 2024Article
- Production of Mature Recombinant Human Activin A in Transgenic Rice Cell Suspension Culture.Current issues in molecular biology · 2024Article
- Efficient virus detection utilizing chitin-immobilized nanobodies synthesized in Ustilago maydis.Journal of biotechnology · 2023Article
- Improving the activity and thermostability of PETase from Ideonella sakaiensis through modulating its post-translational glycan modification.Communications biology · 2023Article
- Strategies for efficient production of recombinant proteins in Escherichia coli: alleviating the host burden and enhancing protein activity.Microbial cell factories · 2022Review
- Engineering a carbohydrate-binding module to increase the expression level of glucoamylase in Pichia pastoris.Microbial cell factories · 2022Article
- An Intrinsically Disordered Peptide Tag that Confers an Unusual Solubility to Aggregation-Prone Proteins.Applied and environmental microbiology · 2022Article
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Authors and funding
8 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundProteins with novel functions or advanced activities developed by various protein engineering techniques must have sufficient solubility to retain their bioactivity. However, inactive protein aggregates are frequently produced during heterologous protein expression in Escherichia coli. To prevent the formation of inclusion bodies, fusion tag technology has been commonly employed, owing to its good performance in soluble expression of target proteins, ease of application, and purification feasibility. Thus, researchers have continuously developed novel fusion tags to expand the expression capacity of high-value proteins in E. coli.
resultsA novel fusion tag comprising carbohydrate-binding module 66 (CBM66) was developed for the soluble expression of heterologous proteins in E. coli. The target protein solubilization capacity of the CBM66 tag was verified using seven proteins that are poorly expressed or form inclusion bodies in E. coli: four human-derived signaling polypeptides and three microbial enzymes. Compared to native proteins, CBM66-fused proteins exhibited improved solubility and high production titer. The protein-solubilizing effect of the CBM66 tag was compared with that of two commercial tags, maltose-binding protein and glutathione-S-transferase, using poly(ethylene terephthalate) hydrolase (PETase) as a model protein; CBM66 fusion resulted in a 3.7-fold higher expression amount of soluble PETase (approximately 370 mg/L) compared to fusion with the other commercial tags. The intact PETase was purified from the fusion protein upon serial treatment with enterokinase and affinity chromatography using levan-agarose resin. The bioactivity of the three proteins assessed was maintained even when the CBM66 tag was fused.
conclusionsThe use of the CBM66 tag to improve soluble protein expression facilitates the easy and economic production of high-value proteins in E. coli.
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