Immobilizing Enzyme Biocatalysts onto Porous Polymer Monoliths Prepared from Cocontinuous Polymer Blends

Abstract

We demonstrate how macroporous poly(ε-caprolactone) monoliths, prepared from cocontinuous polymer blends, can be used to immobilize enzyme biocatalystsherein demonstrated with glucose oxidase (GOx) and peroxidase (POx). The pores are covered with a self-assembled layer of aminated sub-μm silica particles, over which a thin, low-fouling carboxymethylated dextran (CMD) layer is grafted. GOx or POx is finally grafted onto the CMD layer. Our materials display a combination of strong enzyme immobilization, low nonspecific adsorption, and significant enzymatic activity. This approach constitutes a versatile technological platform for the immobilization of biomolecules onto polymer-based monoliths with precisely controlled porosity parameters for both batch and continuous-flow bioprocesses.

Functionalized cellulose monolith based affinity chromatography columns for efficient separation of protein molecules

“…24 Polymer-based monoliths are relatively easy to modify with functional groups. 25,26 The choice of the polymer used for the fabrication of the monolith decides the desirable qualities of the carrier and hence its selection is extremely important.…”

Monolith-modified cellulose paper for biochemical sensing applications

“…30 Since many monomers are capable of forming monoliths with porous structures, there is high flexibility in choosing suitable monomers according to the final application. [31][32][33] Among all types of monoliths, the monolith formed by copolymerization of glycidyl methacrylate (GMA) and ethylene glycol dimethacrylate (EDMA) is promising for use in biomolecular separation and adsorption processes since it can covalently bond with thiol, amine, and carboxyl groups in biomolecules via the epoxy groups of GMA. 34,35 GMA would also form a branched structure during polymerization, preventing hydrolysis after long-term reactions or storage, 36 which can increase the separation efficiency.…”