Abstract
Immobilized enzymes are drawing significant attention for potential commercial applications as biocatalysts by reducing operational expenses and by increasing process utilization of the enzymes. Typically, immobilized enzymes have greater thermal and operational stability at various pH values, ionic strengths and are more resistant to denaturation that the soluble native form of the enzyme. Also, immobilized enzymes can be recycled by utilizing the physical or chemical properties of the supporting material. Magnetic nanoparticles provide advantages as the supporting material for immobilized enzymes over competing meterials such as: higher surface area that allows for greater enzyme loading, lower mass transfer resistance, less fouling effect, and selective, nonchemical separation from the reaction mixture by an applied a magnetic field. Various surface modifications of magnetic nanoparticles, such as silanization, carbodiimide activation, and PEG or PVA spacing, aid in the binding of single or multienzyme systems to the particles, while cross-linking using glutaraldehyde can also stabilize the attached enzymes.
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Johnson, P.A., Park, H.J., Driscoll, A.J. (2011). Enzyme Nanoparticle Fabrication: Magnetic Nanoparticle Synthesis and Enzyme Immobilization. In: Minteer, S. (eds) Enzyme Stabilization and Immobilization. Methods in Molecular Biology, vol 679. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-60761-895-9_15
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DOI: https://doi.org/10.1007/978-1-60761-895-9_15
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