The intracellular exoinulinase from Scytalidium acidophilum was purified to the specific activity of about 1,000 U/㎎ by ammonium sulfate precipitation, DEAE-Sepharose CL-6B, CM-Sephadex C-50, and HPLC gel filtration column. The maximum activity of t...
The intracellular exoinulinase from Scytalidium acidophilum was purified to the specific activity of about 1,000 U/㎎ by ammonium sulfate precipitation, DEAE-Sepharose CL-6B, CM-Sephadex C-50, and HPLC gel filtration column. The maximum activity of the enzyme was observed between pH 3-3.5, which was the most acidic range among the optimum pHs of inulinases so far reported. Also, the enzyme could maintain 85% of its original activity after 6 h of incubation at 65℃, which had the industrial potential for inulin hydrolysis.