T.A. Kovaleva, M.G. Holyavka, M.I. Kalashnikova, D.A. Slivkin

Nowadays methods of the enzymes glycosilation with the purpose to increase the time of their functioning, and also ways of an attachment of a different sort of medical products to sugar-specific proteins are actively developed. Thus, the purpose of work is studying influence N-acetylglucosamine and mannose on enzymatic activity of inulinase. By 4-phasic purification, including sedimentation by acetone, fraction by sulfate of ammonium, gel-filtration on sefadex G-25 and ion-exchanges chromatography on a column with DEAE-cellulose, we has been received a preparation of inulinase from Aspergillus awamori with a 85-fold degree of purification and exit 5 %. It is shown, that N-acetylglucosamine in concentration 10-5 mol/l does not influence on catalytical ability of enzyme. At its concentration 10-4 mol/l inulinase activity increases for 5,5 %, at 10-3 mol/l - on 14 %, and at 10-2 mol/l - on 21 %. Mannose in concentration of 10-5 mol/l also does not influence on activity of enzyme. At its concentration 10-4 mol/l catalytical ability of inulinase increases for 5 %, at 10-3 and 10-2 mol/l - on 28 %. Obviously, that N- acetylglucosamine and man-nose show activator action on inulinase. It is established, that process enzymatic catalysis of inulin hydrolysis reaction at presence of N-acetylglucosamine and mannose submit to equation Michaelis-Menten. It is revealed, that Km for enzyme without modification, and also at presence N-acetylglucosamine and mannose is constant and makes 0,18 mm whereas values of Vmax are various. On the basis of the above-stated it is possible toconfirm, that N- acetylglucosamine and mannose show not competitive type of activation.