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Purification and characterization of a thermostable glucoamylase from a Myrothecium isolate
Author(s) -
Ali S.,
Malek S.,
Hossain Z.
Publication year - 1994
Publication title -
journal of applied bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 0021-8847
DOI - 10.1111/j.1365-2672.1994.tb01618.x
Subject(s) - molecular mass , concanavalin a , hydrolysis , enzyme , chemistry , glycoprotein , biochemistry , chromatography , cellulose , microbiology and biotechnology , biology , in vitro
Two glucoamylases, gluc I and gluc II, were purified to homogeneity from the culture filtrate of a Myrothecium strain M1 by chromatography on DEAE‐cellulose and concanavalin A‐sepharose. Molecular masses deduced by SDS‐PAGE were 72000 ± 2500 for gluc I and 96 000 ± 4000 for glue II. The temperature optima of the enzymes were both about 70°C and their pH optima were around 4.0. Both enzymes were glycoprotein and preferentially hydrolysed high molecular mass substrates. Hg 2+ was a potent inhibitor of both glucoamylases. Glue II had higher debranching activity than gluc I.