Scholarly record

CHARACTERIZATION OF THE FTIR SPECTRA OF BIOCATALYSTS BASED ON IMMOBILIZED HORSERADISH ROOT PEROXIDASE

Ольга Валентиновна Гребенникова, Александрина Михайловна Сульман, Valentina G. Matveeva, N. Lakina, Irina P. Shkileva

Abstract

In this research work, we examined the types and nature of bonds that are formed upon immobilization of peroxidase on three types of carriers: SiO2, Al2O3, Fe3O4. To solve this problem, the method of FTIR spectroscopy was used. As a result of the analysis, many spectra were obtained at all stages of enzyme immobilization. Analyzing the spectra of pure carriers and the spectra obtained after modification of the carriers,it can be said that polystyrene sulfonic acid does not form any chemical bonds with the carriers or forms, but in small quantities. It is held on the surface of the carrier by electrostatic forces. Polystyrenesulfonic acid charges the surface of the carrier negatively (SO3-). Also, with the help of electrostatic forces, chitosan having a positive charge (NH 4 +) is held by polystyrene sulfonic acid. This follows from the fact that no new bonds, except for those characteristics for polystyrene sulfonic acid and chitosan, are manifested in the spectra. After treating SiO2 and Al2O3 with glutaraldehyde, it is seen that an azomethine bond is formed (C = N). Using the same bond, the modified carrier is bound by a covalent bond to the enzyme. Upon immobilization of peroxidase on a pre-modified surface of Fe3O4, bonds are also formed that indicate the presence of the enzyme on the surface of the carrier.

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