Enzyme nanoparticle fabrication: magnetic nanoparticle synthesis and enzyme immobilization.
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 materials 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.
Johnson
Patrick A
PA
Department of Chemical and Petroleum Engineering, University of Wyoming, Laramie, WY, USA.
Park
Hee Joon
HJ
Driscoll
Ashley J
AJ
D001709:Biotechnology / Q000379:methods*; D002384:Catalysis; D003432:Cross-Linking Reagents / Q000737:chemistry; D004798:Enzymes / Q000737:chemistry*; D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000648:ultrastructure; D005976:Glutaral; D008280:Magnetics; D046529:Microscopy, Electron, Transmission; D053758:Nanoparticles / Q000737:chemistry* / Q000648:ultrastructure
D003432:Cross-Linking Reagents; D004798:Enzymes; D004800:Enzymes, Immobilized; D005976:Glutaral