Endoinulinase was purified from a commercial inulin preparation produced by Aspergillus ficuum using ion exchange chromatography on CM-Sephadex C-50 and DEAE-Sepharose 6B, HPLC gel filtration on a Protein Pak 125 Colum and HPLC ion exchange chromatography on a TSK DEAE-5pw Column. The endoinulinase had a molecular weight of 72,000${pm}$1,000 and was glycoprotein with 23 to 25% w/w sugar content. The enzyme was much more active on inulin with random cleavage mode than on sucrose and on palatinose: The ration of activity on inulin and sucrose (I/S ratio) was 10~14.