Abstract
Culture supernatants of Saccharomyces diastaticus contain high-molecular-weight enzymes able to convert starch, but not pullulan, into D-glucose. The enzyme fraction demonstrating glucoamylase activity was purified to homogeneity utilizing multiple ion-exchange/size-exclusion chromatography steps after ammonium-sulfate fractionation, thus avoiding the harsh acetone precipitation procedure employed by others. The glucoamylase enzyme purified from S. diastaticus (STA2 variant) was found to have native and subunit molecular weights of 306,000 and 186,000 daltons, respectively, and an activity temperature optimum of 60 degree C. Preliminary characterization of the STA2 glucoamylase found important differences with the glucoamylase enzymes reported from the DEX series strains.
| Original language | American English |
|---|---|
| Pages | 279-293 |
| Number of pages | 15 |
| State | Published - 1984 |
| Event | Sixth Symposium on Biotechnology for Fuels and Chemicals - Gatlinburg, Tennessee Duration: 15 May 1984 → 18 May 1984 |
Conference
| Conference | Sixth Symposium on Biotechnology for Fuels and Chemicals |
|---|---|
| City | Gatlinburg, Tennessee |
| Period | 15/05/84 → 18/05/84 |
NREL Publication Number
- ACNR/CP-232-5983