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. 1991 Aug;57(8):2317–2323. doi: 10.1128/aem.57.8.2317-2323.1991

Purification and Properties of a Thermoactive Glucoamylase from Clostridium thermosaccharolyticum

Ulrike Specka 1, Frank Mayer 1, Garabed Antranikian 1,*
PMCID: PMC183570  PMID: 16348541

Abstract

A bacterial glucoamylase was purified from the anaerobic thermophilic bacterium Clostridium thermosaccharolyticum and characterized. The enzyme, which was purified 63-fold, with a yield of 36%, consisted of a single subunit with an apparent molecular mass of 75 kDa. The purified enzyme was able to attack α-1,4- and α-1,6-glycosidic linkages in various α-glucans, liberating glucose with a β-anomeric configuration. The purified glucoamylase, which was optimally active at 70°C and pH 5.0, attacked preferentially polysaccharides such as starch, glycogen, amylopectin, and maltodextrin. The velocity of oligosaccharide hydrolysis decreased with a decrease in the size of the substrate. The Km values for starch and maltose were 18 mg/ml and 20 mM, respectively. Enzyme activity was not significantly influenced by Ca2+, EDTA, or α- or β-cyclodextrins.

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Selected References

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