화학공학소재연구정보센터
Applied Microbiology and Biotechnology, Vol.50, No.3, 323-330, 1998
Purification and properties of the raw-starch-digesting glucoamylases from Corticium rolfsii
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 a-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 GS 4.1. These glucoamylases showed nearly identical characteristics except that G4 and G5 were unable to hydrolyze ram starch.