Bioengineered Polyhydroxyalkanoates as Immobilized Enzyme Scaffolds for Industrial Applications
Open Access
- 4 March 2020
- journal article
- review article
- Published by Frontiers Media SA in Frontiers in Bioengineering and Biotechnology
- Vol. 8, 156
- https://doi.org/10.3389/fbioe.2020.00156
Abstract
Enzymes function as biocatalysts and are extensively exploited in industrial applications. Immobilization of enzymes using support materials has been shown to improve enzyme properties, including stability and functionality in extreme conditions and recyclability in biocatalytic processing. This review focuses on the recent advances utilizing the design space of in vivo self-assembled polyhydroxyalkanoate (PHA) particles as biocatalyst immobilization scaffolds. Self-assembly of biologically active enzyme-coated PHA particles is a one-step in vivo production process, which avoids the costly and laborious in vitro chemical cross-linking of purified enzymes to separately produced support materials. The homogeneous orientation of enzymes densely coating PHA particles enhances the accessibility of catalytic sites, improving enzyme function. The PHA particle technology has been developed into a remarkable scaffolding platform for the design of cost-effective designer biocatalysts amenable toward robust industrial bioprocessing. In this review, the PHA particle technology will be compared to other biological supramolecular assembly-based technologies suitable for in vivo enzyme immobilization. Recent progress in the fabrication of biological particulate scaffolds using enzymes of industrial interest will be summarized. Additionally, we outline innovative approaches to overcome limitations of in vivo assembled PHA particles to enable fine-tuned immobilization of multiple enzymes to enhance performance in multi-step cascade reactions, such as those used in continuous flow bioprocessing.Keywords
This publication has 177 references indexed in Scilit:
- Functional Expression of Thyroid-Stimulating Hormone Receptor on Nano-Sized Bacterial Magnetic Particles in Magnetospirillum magneticum AMB-1International Journal of Molecular Sciences, 2013
- M13 Bacteriophage Display Framework That Allows Sortase-Mediated Modification of Surface-Accessible Phage ProteinsBioconjugate Chemistry, 2012
- Classification, Functions, and Clinical Relevance of Extracellular VesiclesPublished by American Society for Pharmacology & Experimental Therapeutics (ASPET) ,2012
- Interenzyme Substrate Diffusion for an Enzyme Cascade Organized on Spatially Addressable DNA NanostructuresJournal of the American Chemical Society, 2012
- Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesinProceedings of the National Academy of Sciences, 2012
- In Vivo Enzyme Immobilization by Inclusion Body DisplayApplied and Environmental Microbiology, 2010
- Polyhydroxyalkanoates: bioplastics with a green agendaCurrent Opinion in Microbiology, 2010
- Bioorthogonal Chemistry: Fishing for Selectivity in a Sea of FunctionalityAngewandte Chemie-International Edition, 2009
- One-Step Production of Immobilized α-Amylase in Recombinant Escherichia coliApplied and Environmental Microbiology, 2009
- Formation of magnetite by bacteria and its applicationJournal of The Royal Society Interface, 2008