ArticleApplied and environmental microbiology2010
In vivo enzyme immobilization by inclusion body display.
Article in Applied and environmental microbiology, 2010. 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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Who cites it
15 citing papers in PubMed.
- Advances in zearalenone-degrading enzymes research: characteristics, mining, improvement, and application.Journal of animal science and biotechnology · 2025Review
- Magnetizing Biotech-Advances in (In Vivo) Magnetic Enzyme Immobilization.Engineering in life sciences · 2025Review
- Article
- Self-assembled particulate vaccine elicits strong immune responses and reduces Mycobacterium avium subsp. paratuberculosis infection in mice.Scientific reports · 2020Article
- Proteasome Biology: Chemistry and Bioengineering Insights.Polymers · 2020Review
- Bioengineered Polyhydroxyalkanoates as Immobilized Enzyme Scaffolds for Industrial Applications.Frontiers in bioengineering and biotechnology · 2020Review
- Tailoring the properties of (catalytically)-active inclusion bodies.Microbial cell factories · 2019Article
- Plasmid Display for Stabilization of Enzymes Inside the Cell to Improve Whole-Cell Biotransformation Efficiency.Frontiers in bioengineering and biotechnology · 2019Article
- Enzyme Engineering for In Situ Immobilization.Molecules (Basel, Switzerland) · 2016Review
- Smart polyhydroxyalkanoate nanobeads by protein based functionalization.Nanomedicine : nanotechnology, biology, and medicine · 2015Review
- New skin test for detection of bovine tuberculosis on the basis of antigen-displaying polyester inclusions produced by recombinant Escherichia coli.Applied and environmental microbiology · 2014Article
- Controlled localization of functionally active proteins to inclusion bodies using leucine zippers.PloS one · 2014Article
- Protein bodies in nature and biotechnology.Molecular biotechnology · 2013Article
- Self-assembled amyloid-like oligomeric-cohesin Scaffoldin for augmented protein display on the saccharomyces cerevisiae cell surface.Applied and environmental microbiology · 2012Article
- Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A novel strategy for in vivo immobilization of enzymes on the surfaces of inclusion bodies has been established. It relies on expression in Escherichia coli of the polyhydroxybutyrate synthase PhaC from Cupriavidus necator, which carries at its amino terminus an engineered negatively charged alpha-helical coil (Ecoil) and forms inclusion bodies upon high-level expression. Coexpression in the same cell of galactose oxidase (GOase) from Fusarium spp. carrying a carboxy-terminal positively charged coil (lysine-rich coil [Kcoil]) sequence results in heterodimeric coiled-coil formation in vivo and in the capture of the enzyme in active form on the surface of the inclusion body particle. These round-shaped enzyme-decorated microparticles, with sizes of approximately 0.7 mum, can be isolated from lysed cells simply by centrifugation. The cost-effective one-step generation and isolation of enzymes immobilized on inclusion body particles may become useful for various applications in bioprocessing and biotransformation.
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Registered trials
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