Purification and characterization of a thermostable glucoamylase from a Myrothecium isolate |
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| Authors: | S Ali S Malek Z Hossain |
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| Institution: | Department of Biochemistry, University of Dhaka, Dhaka, Bangladesh |
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| Abstract: | 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. Hg2+ was a potent inhibitor of both glucoamylases. Glue II had higher debranching activity than gluc I. |
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