Enzyme microcapsules with substrate selective permeability constructed via layer-by-layer polyelectrolyte self-assembly

Polyelectrolyte multilayer microcapsules with entrapped horseradish peroxidase (HRP) have been prepared via a layer-by-layer (LbL) self-assembly strategy of polycation and polyanion on CaCO3 microparticles as templates. Preparation conditions have been studied and optimized. Within the investigated ranges, use of buffer solutions with lower pH value or lower ionic strength in the buffer solution for polyelectrolyte self-assembly has resulted in thinner polyelectrolyte film and higher permeability of the microcapsules. For dissolving the CaCO3 templates, use of weakly acidic (pH 4.0) buffer solution in place of routinely used EDTA reagent has improved the catalytic activity of microcapsules. The HRP-containing microcapsules have exhibited catalytic activity to pyrogallol as substrate, while the catalytic activity to 2,2′-azino-bis(3-ethylbenz-thiazoline-6-sulfonic acid) (ABTS) was severely suppressed. No less than 90% of the maximum enzymatic activity to pyrogallol has remained after 30 days. Promising prospects in various biocatalysis applications have been expected for the enzyme microcapsules, due to their selective permeability, stability and reusability.

► Preparation method for enzyme-containing microcapsules was improved. ► Selective permeability to different substrates for one enzyme was firstly shown. ► Enzymatic activity was improved by replacement of the metal chelating reagent EDTA. ► More than 90 % of the maximum enzymatic activity remained after 30 days storage.