CATALYTIC PROPERTIES OF SOYBEAN LIPOXYGENASE, IMMOBILIZED ON MODIFIED SILICA

Catalytic properties of soybean lipoxygenase immobilized on silica have been studied. Lipoxygenase had the highest activity in the case of covalent immobilization on aminosilica activated by glutaraldehyde or on carboxysilica activated by N-hydroxysuccinimide and after physical sorption on aminosilica. Kinetic properties of immobilized lipoxygenase in the reaction of oxygenation of linoleic acid proved to be as follows optimal pH 9.0; observed K(m) 0.104 +/- 0.20 mM. The observed residual activity of the immobilized enzyme was 4-16%. The immobilized lipoxygenase has been used for the synthesis of 13(S)-hydroperoxide of linoleic acid with a 96-98% yield. The product's structure was studied by UV and IR spectrometry, HPLC, TLC and polarimetry.