Purification and some properties of endoinulinase from Chrysosporium pannorum |
| |
| Affiliation: | 1. Department of Pharmaceutical Technology, Faculty of Pharmacy, Silpakorn University, Nakhon Pathom, Thailand;2. Pharmaceutical Biopolymer Group (PBiG), Faculty of Pharmacy, Silpakorn University, Nakhon Pathom, Thailand;3. Department of Thai Medicine, Faculty of Traditional Thai Medicine, Prince of Songkla University, Songkhla, Thailand;4. Laboratory of Pharmaceutical Engineering, Gifu Pharmaceutical University, Gifu, Japan;1. Department of Agricultural and Biosystems Engineering, Iowa State University, Ames, IA 50011-3080, USA;2. Department of Energy, Power Engineering and Environment, Faculty of Mechanical Engineering and Naval Architecture, University of Zagreb, Ivana Lucica 5, HR-10000 Zagreb, Croatia;3. Department of Civil, Construction and Environmental Engineering, Iowa State University, Ames, IA 50011-3232, USA;4. Department of Food Science and Human Nutrition, Iowa State University, Ames, IA 50011-3080, USA;5. Department of Civil and Environmental Engineering, Urban Water Research Center, University of California, Irvine, Irvine, CA 92697-2175, USA |
| |
| 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. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
