Inorganic nanomaterial-based biocatalysts

Abstract

Over the years, nanostructures have been developed to enable to support enzyme usability to obtain highly selective and efficient biocatalysts for catalyzing processes under various conditions. This review summarizes recent developments in the nanostructures for enzyme supporters, typically those formed with various inorganic materials. To improve enzyme attachment, the surface of nanomaterials is properly modified to express specific functional groups. Various materials and nanostructures can be applied to improve both enzyme activity and stability. The merits of the incorporation of enzymes in inorganic nanomaterials and unprecedented opportunities for enhanced enzyme properties are discussed.

Enzymes immobilized in mesoporous silica: A physical–chemical perspective

“…The pore filling, P f , in equation 1 can be expressed in terms of the particle porosity Φ = V pore /V part (4) where V part is the volume of the entire particle. The porosity, Φ, can in turn be calculated from the specific pore volume, ν pore , of the particle and the density, ρ silica , of the silica itself, so that equation 4…”

“…hexagonal alignment or random arrangement of the pores), pore diameter and wall thickness, as well as thermal and mechanical stability [3]. Most particles are silica-based, but other types of material have been used such as alumina or titania [4]. Several reviews have summarized the use of mesoporous materials as immobilization support for enzymes and their use in biocatalytic applications [1,2,[4][5][6][7], but a recent review concludes that there is a gap of knowledge in the understanding of how the microenvironment and material properties of the mesoporous particles affect the activity of the immobilized enzymes [8].…”

“…Most particles are silica-based, but other types of material have been used such as alumina or titania [4]. Several reviews have summarized the use of mesoporous materials as immobilization support for enzymes and their use in biocatalytic applications [1,2,[4][5][6][7], but a recent review concludes that there is a gap of knowledge in the understanding of how the microenvironment and material properties of the mesoporous particles affect the activity of the immobilized enzymes [8]. Strategies for rational design of mesoporous materials for enzyme immobilization have been proposed based on electrostatic and hydrophobic interactions [9], but they are generally based on the properties of the proteins and particles as separate entities which disregards the possibility that the pore environment may affect the properties of the proteins.…”

Rapid and selective separation for mixed proteins with thiol functionalized magnetic nanoparticles

“…Besides their size-dependent properties, MNPs applications are affected by their surface functionalization. In this context, silica-coated MNPs (Si-MNPs) has several advantages arising from their stability under aqueous conditions (at least if the pH value is sufficiently low) and easy functionalization by hydroxyl group on the exposed silica surface surrounding MNPs [7,8]. A key consideration during protein separation process is to control the driving force of the sorbent surface behind the adsorption of proteins involves hydrophobic and electrostatic interactions [9].…”

Preparation of Polyphosphazene Hydrogels for Enzyme Immobilization

“…Enzymes that display high catalytic efficiency and selectivity under mild conditions are promising catalysts for use in many fields such as fine chemical synthesis, food processing, biosensor fabrication and bioremediation [1,2,3,4]. However, the practical applications of native enzymes suffer severely due to low enzyme stability upon exposure to heat, extreme pH values, and organic solvents.…”