Purification and characterization of an extracellular glucoamylase from the yeastCandida tsukubaensis CBS 6389 |
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| Authors: | R. De Mot E. Van Oudenduck H. Verachtert |
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| Affiliation: | (1) Laboratory of Industrial Microbiology and Biochemistry, University of Leuven, Kardinaal Mercierlaan 92, B-3030 Leuven, Belgium |
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| Abstract: | The starch-degrading yeastCandida tsukubaensis CBS 6389 secreted amylase at high activity when grown in a medium containing soluble starch. The extracellular α-amylase activity was very low. The major amylase component was purified by DEAE-Sephadex A-50 chromatography and Ultrogel AcA 44 gel filtration and characterized as a glucoamylase. The enzyme proved to be a glycoprotein with a molecular weight of 56000. The glucoamylase had a temperature optimum at 55°C and displayed highest activity in a pH range of 2.4–4.8. Acarbose strongly inhibited the purified glucoamylase. Debranching activity was present as demonstrated by the release of glucose from pullulan. |
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