Abstract: | Glucoamylase from Aspergillus niger was immobilized by entrapping in glutaraldehyde crosslinked gelatin. Preparations were prepared in the form of beads and thin layers on activated glass, polyester and aluminium foils. Immobilization did not cause changes of pH and temperature optimum. However, it increased thermal stability additionally stabilized by the presence of a substrate. The most stable preparations acted without change in activity for 34 days at a temperature of 50°C. Obtained preparations hydrolyzed α-amylase liquefied starch to a DE value of about 97%. The preparations of glucoamylase immobilized in a thin layer of gelatin on the polyester and aluminium foil were used in a thin layer flow reactor for hydrolysis of 10% starch solution. |