Purification and characterization of a thermostable glucoamylase from a Myrothecium isolate
1994
Ali, S. | Malek, S. | Hossain, Z.
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 72 000 +/- 2500 for gluc I and 96 000 +/- 4000 for gluc II. The temperature optima of the enzymes were both about 70 degrees C and their pH optima were around 4.0. Both enzymes were glycoprotein and preferentially hydrolysed high molecular mass substrates. Hg2+ was a potent inhibitor of both glucoamylases. Gluc II had higher debranching activity than gluc I.
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