Magnetically separable biocatalysts based on glucose oxidase for d-glucose oxidation

Biocatalytic systems based on glucose oxidase immobilized on the surface of magnetically separable oxides SiO 2 and Al 2 O 3 were studied. Silicon and aluminum oxides acquired magnetic properties due to the introduction of magnetic nanoparticles Fe 3 O 4 into their pores. The support surface was modified with reactive amino groups using (3-aminopropyl)triethoxysilane and was activated using glutaraldehyde to achieve covalent bonding of the enzyme to the magnetically separable supports. Glucose oxidase was immobilized on the modified and activated magnetically separable supports. These biocatalytic systems were studied using low-temperature nitrogen adsorption, transmission electron microscopy, and X-ray photoelectron spectroscopy. All the biocatalytic systems were tested in the reaction of oxidation of d -glucose to d -gluconic acid. The highest relative activity (95%) was demonstrated by the biocatalyst based on glucose oxidase immobilized on the surface of magnetically separable silica.