T.A. Kovaleva, E.L. Makarova, A.I. Slivkin, E.V. Korotkova

Increased interest in amylases as effective biocatalysts is due to their use in medicine, organic synthesis, food and light industry. During the process of production of heterogeneous drugs based on immobilized glucoamylase leading criterion is not the percentage of preservation of activity, but the degree of strength of the enzyme-carrier. Application of natural biopolymers, fully recyclable by the body, e.g. digested and substituted by tissues of the body, eliminates the risk of accumulation of the matrix carrier in the human body. Among other proteins collagen is the least immunogenic, and its unique physical and chemical properties satisfy numerous requirements for carriers to create new medications. Therefore we performed immobilization of glucoamylase on collagen, where heterogeneous biocatalyst retains 67% of the catalytic activity of the free enzyme. The physical-chemical properties of glucoamylase associated with collagen by adsorption were investigated. It was established that the immobilized enzyme exhibits maximum catalytic activity at 550С, which is 50С higher than the temperature for the free enzyme. The expansion of pH range (4.5-5.0) in which maximal activity can be detected was observed for glucoamylase immobilized on collagen. The adsorption of glucoamylase on collagen is promising for further research aimed at developing optimal conditions for obtaining highly active pharmaceutical medications with durable action.