ПОЛУЧЕНИЕ И ХАРАКТЕРИСТИКА БИОКАТАЛИЗАТОРОВ НА ОСНОВЕ ИММОБИЛИЗОВАННЫХ ГЛИКОЗИДАЗ

Abstract

Summary. Enzymes subclass glycosidases cleaving poly- and oligosaccharides to simple sugars, are of great practical importance for a variety of industries. Such enzymes include α-L-fucosidase and β-fructofuranosidase. α-L-fucosidase splits fucoidan kelp to fucose and fucooligosaccharides. Fucose has prebiotic, immunotropic action, and a wide spectrum of biological activity in vertebrates, fucooligosaccharides - antioxidant and prebiotic properties. In this regard, and fucose polymers may be demanded in the food, feed and pharmaceutical industry. β-fructofuranosidase sucrose hydrolysis with the formation of invert syrup high quality and biological value that is of interest to the sugar industry. In order to intensify the processes of hydrolysis of fucoidan and sucrose due to the higher stability and reusability of enzyme preparations carried immobilization α-L-fucosidase on chitosan and β-fructofuranosidase of ion exchange brand FIBAN A-6 adsorption method. Activity of the immobilized α-L-fucosidase and β-fructofuranosidase were 80 and 70% of the activity of the free enzyme, respectively. Found that immobilized β-fructofuranosidase exhibits maximal activity at pH 4,0-4,1, the immobilized α-L-fucosidase - at pH 7,0. The optimal pH of immobilized enzymes similar to those for the free enzyme. Optimal temperature hydrolysis substrates immobilized α-L-fucosidase and β-fructofuranosidase was 50 and 70 ° C respectively, 10 ° C and 20 ° C higher compared to free enzymes. Studies have shown sufficient stability of immobilized glycosidases, so at 4-fold using their enzymatic activity decreased by 1.5 times; Biocatalysts obtained in storage in the refrigerator for 4-6 months retained 80% of the catalytic activity of enzymes.