Properties and Efficiency of a Biocatalyst Based on Immobilized Fungal Amyl

Abstract

Preparations based on native enzymes have found limited industrial application because of their instability and sensitivity to  changes in pH, temperature, and other external factors. Therefore, the acute task is to develop biocatalysts based on immobilized enzymes, which are more stable and therefore more effective in the practice. To stabilize the fungal amylase (KF 3.2.1.1.), we applied the covalent immobilization of the enzyme on chitosan-containing cellulose. It is shown that in comparison with native amylase, the thermal stability of the immobilized amylase increased 3,5-fold, and the resistance against pH inactivation increased as well. The decrease in the rate constants of inactivation of the immobilized enzyme indicates the increase in its stability due to steric factors associated with the formation of azomethine bonds with cellulose and chitosan. It is shown that when using an immobilized enzyme preparation in place of the native amylase, the product yield of the hydrolysis  of barley malt  increases by 1,5 times, which makes it of practical use in the food industry.