Characterization of extracellular glucoamylase from the ectomycorrhizal mushroom Lyophyllum shimeji
Year: 2004
Type: article
Abstract: To investigate the function of amylases in the fruit-body formation of an ectomycorrhizal fungus, Lyophyllum shimeji, we purified the extracellular amylase in the medium of this fungus. The purified enzyme was obtained from 1.7l stationary culture filtrate, with 4.2% recovery, and showed a single protein band on SDS-PAGE. The molecular mass was about 25kDa. The enzyme was most active at around 40°C and pH 5.0 and stable over pH 4.5–6.5 for 30min at 37°C. This amylase was remarkably activated by the presence of Ca2+ ion (7.7 times that of the control), but Ba2+ and Ag+ completely inhibited the activity. The amylase readily hydrolyzed the α-1,4 glucosidic linkage such as dextrin and amylose A (MW, 2900), converting into glucose, and hydrolyzed the α-1,6 glucosidic linkage of isomaltohexaose and amylopectin. However, the enzyme did not hydrolyze the cyclic polysaccharides. On the other hand, when a low molecular mass amylose A was hydrolyzed by this amylase, β-anomer glucose was produced. From these results, we concluded that the amylase from L. shimeji seems to be a glucoamylase.
Source: Mycoscience
Authors: Mizuho Kusuda, Mitsuhiro Ueda, Masami Nakazawa, Kazutaka Miyatake, Yasuhito Konishi, Norifumi Shirasaka, Takao Terashita, Kazuyuki Matsuzawa
Institutions: Osaka Prefecture University, Kindai University
Language: English
Subfield: Biotechnology
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W1968558063