ArticleMicrobial cell factories2019
In vivo immobilization of an organophosphorus hydrolyzing enzyme on bacterial polyhydroxyalkanoate nano-granules.
Article in Microbial cell factories, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Phasin proteins expressed byJournal of applied biology & biotechnology · 2026Article
- Preparation and characterization of immobilized mannanase on polyhydroxyalkanoate (PHA).Bioresources and bioprocessing · 2025Article
- Recent perspectives on biotechnological production, modulation and applications of glycerophosphoryl diester phosphodiesterases.Biodegradation · 2025Review
- Paracoccus kondratievae produces poly(3-hydroxybutyrate) under elevated temperature conditions.Environmental microbiology reports · 2024Article
- Economical synthesis of γ-cyclodextrin catalyzed by oriented cyclodextrin glycosyltransferase displayed on bacterial polyhydroxyalkanoate nanogranules.Microbial cell factories · 2023Article
- Peptide conformational imprints enhanced the catalytic activity of papain for esterification.Frontiers in bioengineering and biotechnology · 2022Article
- Protein scaffolds: A tool for multi-enzyme assembly.Biotechnology reports (Amsterdam, Netherlands) · 2021Review
- Bioengineered Polyhydroxyalkanoates as Immobilized Enzyme Scaffolds for Industrial Applications.Frontiers in bioengineering and biotechnology · 2020Review
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4 authors.
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Abstract
backgroundPolyhydroxyalkanoate (PHA) are nano-granules naturally produced by bacteria. Two types of proteins, PHA synthase (PhaC) and phasins (PhaPs), are attached to the PHA surface by covalent and hydrophobic interactions. Utilizing these anchored proteins, functionalized PHA nano-granules displaying proteins of interest can be easily prepared by fermentation.
resultsIn this study, a one-step fabrication method was developed for stable and efficient immobilization of an organophosphorus degrading enzyme on PHA nano-granules. The nano-biocatalysts were produced in recombinant Escherichia coli cells into which the polyhydroxyalkanoate synthesis pathway from Cupriavidus necator had been introduced. Two different strategies, covalent attachment and hydrophobic binding, were investigated by fusing bacterial organophosphorus anhydride hydrolase (OPAA4301) with PhaC and PhaP, respectively. Using both methods, the tetrameric enzyme successfully self-assembled and was displayed on the PHA surface. The display density of the target fused enzyme was enhanced to 6.8% of total protein on decorated PHA by combination of covalent and non-covalent binding modes. Immobilization of the enzyme on PHA granules resulted in higher catalytic efficiency, increased stability and excellent reusability. The k
conclusionsThis study provides a promising approach for cost-efficient in vivo immobilization of a tetrameric organophosphorus degrading enzyme. The immobilization process expands the utility of the enzyme, and may inspire further commercial developments of PHA nano-biocatalysts. As revealed by our results, combination of covalent and non-covalent binding is recommended for display of enzymes on PHA granules.
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