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.

glucosidase, α-L-fucosidase, β-fructofuranosidase, fucoidan, a fucose, fucooligosaccharides, sucrose, invert syrup, adsorption, immobilization, chitosan fiber ion exchanger hydrolysis substrate

1. Korneeva O. S. Carbohydrate: preparative synthesis, structure and mechanism of action on oligo - and polysaccharides. Voronezh: Voronezh state University, 2001. 184 p. (In Russ.).

2. Luther K.B., Haltiwanger R.S. Role of unusual O-glycans in intercellular signaling. The International Journal of Biochemistry & Cell Biology, 2009, vol. 41, pp. 1011– 1024.

3. Sanina T.V. et al. The study bifidogenic activity fucose and its polymers. Herald of the Voronezh state University. Series: Chemistry. Biology. Pharmacy, 2011, no. 1, pp. 141-143. (In Russ.).

4. Cherenkov D. A. et al. Fucose: biological role, ways of production and utilization. Biotechnology, 2010, no. 6, pp. 63-71. (In Russ.).

5. Intra J., Cenni F., Perotti M.-E. An a-LFucosidase Potentially Involved in Fertilization Is Present on Drosophila Spermatozoa Surface. Molecular reproduction and development, 2006, vol. 73, pp. 1149–1158.

6. Cherenkov D. A., Anokhina E. P., Kirianova S. V., Korneeva O. S. Antioxidant activity of the hydrolysis products of natural polymers (mannan and fucoidan). Herald of the Voronezh state University of engineering technologies, 2012, no. 1, pp. 151-153. (In Russ.).

7. Kretovich V. L. Fundamentals of biochemistry. M.: Higher school, 1986. 547 p. (In Russ.).

8. GOST 10896-78. Ion exchangers. Preparation for the test. Introduced 01.01.1980. M: IPC standards Publishing house, 1991. 7 p. (In Russ.).

9. Dische Z., Shettles L. B. A specific color reaction of methylpentoses and a spectrophotometric micromethod for their determination. J. Biol. Chem, 1948, vol. 175, no 2, pp. 595-603.

10. Ermakov A. I. Methods of biochemical studies of plants. L.: Agropromizdat Leningrad branch, 1976. 430 p. (In Russ.).

11. Polygaline G.V., Cherednichenko V. S., Rimareva L. V. Determination of enzyme activity. The Handbook. M: Delhi print, 2003. 375 p. (In Russ.).

12. Meshcheriakova O. L. et al. Immobilization of β-fructofuranosidase on the fibrous carrier. Biotechnology, 2012, no. 4, pp. 58-62. (In Russ.).

13. Levenkov S. V., Iakush E. V. Adsorption properties of chitosan with respect to protein substances. Proceedings of the Pacific research fisheries center, 2001, no 1, pp. 121-128. (In Russ.).

14. Ushakov V. M. et al. Method of extraction of invertase from yeast cells in the process of their cultivation. Biotechnology, 1992, no. 1, pp. 43-45. (In Russ.).

15. Kovalenko G. A. et al. Carbon-containing microstructurally ceramic media for adsorptive immobilization of enzymes and microorganisms. III. Biocatalytic properties of adsorbed invertase. Biotechnology, 2003, no. 4, pp. 52-62. (In Russ.).

16. Kovalenko G. A. et al. Biocatalytic properties of adsorbed yeast membranes. Biotechnology, 2004, no. 6, pp. 34-45. (In Russ.).

17. Meshcheriakova O. L. et al. Comparative characteristics of the properties of free and immobilized β-fructofuranosidase. Modern problems of science and education, 2012, no. 2, pp. 356. (In Russ.).

18. Trevin M. Immobilized enzymes. M.: Mir, 1987. 513 p. (In Russ.).