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Appl Environ Microbiol. 1975 August; 30(2): 163-166
Copyright © 1975 American Society for Microbiology. All Rights Reserved.

Isolation and Some Properties of Glucoamylase from Cephalosporium charticola Lindau

Laboratory of Enzymology, Institute of Physiology and Cytology, University of Lodz, 90-237 Lodz, Poland

ABSTRACT

High glucoamylase (-D-/1 4/glucan glucohydrolase, EC 3.2.1.3.) activity was obtained in the cell-free culture fluid of Cephalosporium charticola. Glucoamylase seems to be the only amylolytic enzyme produced by C. charticola. The enzyme, purified on diethylaminoethyl-cellulose, was homogeneous by disc gel electrophoresis. The optimum pH on starch was 5.4, and optimum temperature was 60 C. Starch was degraded more rapidly than several other substrates; maltose was hydrolyzed about one-fifth as rapidly as starch. The molecular weight was 69,000, as determined by Sephadex G-100 filtration. The enzyme is a glycoprotein and contains about 6.6% sugars (mannose and glucosamine).