Enzymes from Sulfolobus shibatae for the production of trehalose and glucose from starch
| Autor: | Isabella Di Lernia, M. De Rosa, Mosè Rossi, Alessandra Morana, Stefania Fusco, Antonio Ottombrino |
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| Přispěvatelé: | DI LERNIA, I, Morana, A, Ottombrino, A, Fusco, S, Rossi, M, DE ROSA, Mario |
| Jazyk: | angličtina |
| Rok vydání: | 1998 |
| Předmět: |
chemistry.chemical_classification
Sulfolobus shibatae Molecular mass ved/biology Starch fungi ved/biology.organism_classification_rank.species Trehalose General Medicine Polysaccharide Microbiology Sulfolobus Catalysis chemistry.chemical_compound Hydrolysis Glucose Enzyme chemistry Biochemistry Glucosyltransferases Molecular Medicine |
| Popis: | Enzymes that convert starch and dextrins to alpha,alpha-trehalose and glucose were found in cell homogenates of the hyperthermophilic acidophilic archaeon Sulfolobus shibatae DMS 5389. Three enzymes were purified and characterized. The first, the S. shibatae trehalosyl dextrin-forming enzyme (SsTDFE), transformed starch and dextrins to the corresponding trehalosyl derivatives with an intramolecular transglycosylation process that converted the glucosidic linkage at the reducing end from alpha-1,4 to alpha-1,1. The second, the S. shibatae trehalose-forming enzyme (SsTFE), hydrolyzed the alpha-1,4 linkage adjacent to the alpha-1,1 bond of trehalosyl dextrins, forming trehalose and lower molecular weight dextrins. These two enzymes had molecular masses of 80 kDa and 65 kDa, respectively, and showed the highest activities at pH 4.5. The apparent optimal temperature for activity was 70 degrees C for SsTDFE and 85 degrees C for SsTFE. The third enzyme identified was an alpha-glycosidase (Ss alpha Gly), which catalyzed the hydrolysis of the alpha-1,4 glucosidic linkages in starch and dextrins, releasing glucose in a stepwise manner from the nonreducing end of the polysaccharide chain. The enzyme had a molecular mass of 313 kDa and showed the highest activity at pH 5.5 and at 85 degrees C. |
| Databáze: | OpenAIRE |
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