In this work, the synthesis and study of the physics–chemical catalytic properties of the multicomponent biocatalyst based on the horseradish peroxidase immobilized on the modified titanium dioxide (TiO2) were carried out. Hydrochloric acid, chitosan, aminopropyltriethoxysilane and glutaric dialdehyde were used in order to modify the titanium dioxide. The horseradish peroxidase was obtained by extraction of the horseradish root (Armoracia rusticana) with the following centrifugation and separation of the filtrate. Immobilization of enzyme was performed by sequential application method with intermediate washing with distilled water from the non-specifically bounded reagents. In order to confirm the presence of the functional groups formed by the modifying agents the samples of the modified titanium dioxide and biocatalyst were analyzed by FTIR–spectroscopy. The results of FTIR–study illustrate the presence of functional; groups required for the covalent bonding. This confirms the effectivity of the method chosen for the modification of inorganic support. The study of the biocatalyst by the method of low–temperature nitrogen physisorption shows that the support modification by the chosen method increases the reactivity of the surface and promotes the maximal accessibility of the active sites of the immobilized enzymes. In this paper, the experimental confirmation of the structure of the multicomponent biocatalyst on the basis of the horseradish peroxidase immobilized on the modified TiO2 is shown for the first time. All hypotheses and conclusions expressed in this paper are based on scientific and technical literature on methods of immobilization of enzymes, methods of inorganic carriers modifying, the scientific basis of FTIR–spectroscopy and low-temperature nitrogen physisorption.

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