PURIFICATION AND CHARACTERIZATION OF A THERMOSTABLE GLUCOAMYLASE FROMA MYROTHECIUM ISOLATE

Authors
ALI S MALEK S HOSSAIN Z
Citation
S. Ali et al., PURIFICATION AND CHARACTERIZATION OF A THERMOSTABLE GLUCOAMYLASE FROMA MYROTHECIUM ISOLATE, Journal of Applied Bacteriology, 76(3), 1994, pp. 210-215
Citations number
26
Categorie Soggetti
Microbiology,"Biothechnology & Applied Migrobiology
Journal title
Journal of Applied Bacteriology → ACNP
ISSN journal
00218847
Volume
76
Issue
3
Year of publication
1994
Pages
210 - 215
Database
ISI
SICI code
0021-8847(1994)76:3<210:PACOAT>2.0.ZU;2-M
Abstract
TWO glucoamylases, glue I and glue II, were purified to homogeneity fr om the culture filtrate of a Myrothecium strain M1 by chromatography o n DEAE-cellulose and concanavalin A-sepharose. Molecular masses deduce d by SDS-PAGE were 72 000 +/- 2500 for glue I and 96 000 +/- 4000 for glue II. The temperature optima of the enzymes were both about 70 degr ees C and their pH optima were around 4.0. Both enzymes were glycoprot ein and preferentially hydrolysed high molecular mass substrate. Hg2was a potent inhibitor of both glucoamylases. Glue II had higher debra nching activity than glue I.