Purification and characterization of sago starch-degrading glucoamylase from Acremonium sp. endophytic fungus

摘要

A novel sago strarch degrading glucoamylase which had a strong amylopectin-hydrolyzing-activity was purified to homogeneity from a culture filtrate of Acremonium sp. isolated from forest trees. The purified enzyme was an oligomeric protein of two sub-units with molecular weights of 22 and 39 kDa. Optimum temperature and pH for enzyme activity were around 55 deg C and 5.5, respectively. The enzyme was stable in a pH range of 3.0-7.0 and temperatures up to 60 deg C.