Purification and properties of the raw-starch-digesting glucoamylases from Corticium rolfsii |
| |
| Authors: | Y. Nagasaka K. Kurosawa A. Yokota F. Tomita |
| |
| Affiliation: | (1) Laboratory of Applied Microbiology, Department of Bioscience and Chemistry, Faculty of Agriculture, Hokkaido University, Sapporo 060, Japan Fax: +81 11 706 4961, JP |
| |
| Abstract: | Corticium rolfsii AHU 9627, isolated from a tomato stem, is one of the strongest producers of a raw-starch-digesting amylase. The amylase system secreted by C. rolfsii AHU 9627 consisted of five forms of glucoamylase (G1–G5) and a small amount of α-amylase. Among these amylases, G1, G2 and G3 were able to hydrolyze raw starch. Five forms of glucoamylase were separated from each other and purified to an electrophoretically homogeneous state. The molecular masses were: G1 78 kDa, G2 78 kDa, G3 79 kDa, G4 70 kDa, and G5 69 kDa. The isoelectric points were: G1 3.85, G2 3.90, G3 3.85, G4 4.0, and G5 4.1. These glucoamylases showed nearly identical characteristics except that G4 and G5 were unable to hydrolyze raw starch. Received: 16 December 1997 / Received last revision: 6 May 1998 / Accepted: 1 June 1998 |
| |
| Keywords: | |
| 本文献已被 SpringerLink 等数据库收录！ |
|
