Purification and some properties of endoinulinase from Chrysosporium pannorum

Abstract

One endoinulinase (2,1-β- d-fructan fructanohydrolase EC 3.2.1.7) was purified from Chrysosporium pannorum AHU 9700. The enzyme was a glycoprotein having an isoelectric point around pH 3.8. The molecular weight was 58,000 and 56,000 by SDS-polyacrylamide gel electrophoresis and gel filtration on Sephacryl S-200, respectively. The endoinulinase was most active between pH 6.0–7.0 at 50°C, and was stable at 45°C (10 min) and from pH 4.5 to 8.5 (24 h). This enzyme was active only on inulin, not on levan, sucrose, raffinose, or melezitose. The main products from inulin were inulotriose, inulotetraose, and inulopentaose.