PURIFICATION AND IMMOBILIZATION OF SCYTALIDIUM SP. α-AMYLASE AND ITS GENERAL PROPERTIES

An α-amylase of Scytalidium sp. was produced in shake flask cultures. The enzyme was purified to a homogeneous state on polyacrylamide gel electrophoresis by acetone precipitation, DEAE-cellulose column chromatography and Sephadex G-75 gel filtration. The molecular weight of the enzyme was about 87, 000 dalton. Metal ions such as Fe2+, Na+ and Cu2+ activated the enzyme activity while Hg2+ and Zn2+ were strongly inhibitory. The α-amylase was immobilized on DEAE-cellulose by adsorption. The optimum pH of the immobilized enzyme was 6.0, as compared with 8.0 for the free enzyme. The immobilized enzyme was optimally active at 50°C and retained 50% activity at 100°C (30min) as against 40°C and 40% (100°C, 30min) for the free enzyme.