Enzyme Nanoparticle Fabrication: Magnetic Nanoparticle Synthesis and Enzyme Immobilization

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 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.

Targeted delivery of tissue plasminogen activator by binding to silica-coated magnetic nanoparticle

“…48 In the current study, the stability of tPA in solution at 4°C was enhanced 9.5-fold as a result of binding to SiO 2 -MNP. Possible mechanisms leading to enhanced storage stability of tPA could be ascribed to the restriction of the conformation change of the drug after covalent binding with SiO 2 -MNP, thus preventing distortion and activity loss of the enzyme molecule.…”

Lipase NS81006 immobilized on Fe3O4 magnetic nanoparticles for biodiesel production

“…Magnetic nanoparticles are most popular materials due to their high surface to volume ratio for loading a larger amount of lipase, lower mass transfer resistance for reacting with substrates and ease the way of separation from the reaction mixture by external magnetic field [7]. Naked-magnetic nanoparticles are not applicable directly for lipase immobilization and some suitable surface modification or functionalization on the nakedmagnetic nanoparticles are necessary before immobilizing lipase onto the nanoparticles [7][8][9].…”

“…Naked-magnetic nanoparticles are not applicable directly for lipase immobilization and some suitable surface modification or functionalization on the nakedmagnetic nanoparticles are necessary before immobilizing lipase onto the nanoparticles [7][8][9]. It has been found that some organosilane compounds like 3-aminopropyltriethyloxysilane (APTES), paminophenyltrimethoxysilane (APTS) and mercaptopropyltriethoxysilane (MPTES) can be used as the potential candidates for functionalizing or modifying the surface of the naked magnetic nanoparticles.…”

NADH Oxidation in a Microreactor with an Oscillating Magnetic Field

“…The use of magnetic nanoparticles as a support for immobilized enzymes has many advantages, for instance, higher specific surface area is obtained for binding a larger amount of enzymes, lower mass transfer resistance and less fouling are achieved, and immobilized enzymes can be selectively separated from a reaction mixture by magnetic field application [11]. Various surface modifications of magnetic nanoparticles, such as silanization, carbodiimide activation, and polyethylene glycol or polyvinyl alcohol spacing, aid binding of single or multienzyme systems to particles, whereas cross-linking using glutaraldehyde can also stabilize the attached enzymes [12]. To date, several attempts have been made to immobilize enzyme alcohol dehydrogenase (ADH) on superparamagnetic magnetite (Fe 3 O 4 ) nanoparticles using the glutaraldehyde covalent immobilization [13][14][15][16].…”