Purification et propriétés de la lévane-sucrase exocellulaire de Bacillus subtilis marburg
| Autor: | M. Pascal, R. Dedonder |
|---|---|
| Rok vydání: | 1972 |
| Předmět: |
chemistry.chemical_classification
Sucrose biology Organic Chemistry Levansucrase General Medicine Bacillus subtilis biology.organism_classification Biochemistry Analytical Chemistry Amino acid Sucrase chemistry.chemical_compound Enzyme chemistry biology.protein Enzyme inducer Polyacrylamide gel electrophoresis |
| Zdroj: | Carbohydrate Research. 24:365-377 |
| ISSN: | 0008-6215 |
| DOI: | 10.1016/s0008-6215(00)85070-3 |
| Popis: | Two inducible enzymes, namely a levansucrase and a sucrase, are responsible for the saccharolytic activity in Bacillus subtilis Marburg. In the strain QB 13 producing a high level of saccharolytic activity, up to 90% of this activity is excreted. The exocellular activity can be accounted for by levansucrase. This enzyme has been obtained in pure form from the supernatant of an induced culture by fractional precipitations with ethanol and ammonium sulfate, and chromatography on hydroxyapatite; mol. wt. is ca. 40,000; = 4.16 S. The enzyme consists of a single polypeptide chain with lysin as the N-terminal amino acid. This enzyme catalyzes transfructosylation reactions; sucrose and low-molecular-weight levans may act as D -fructosyl donors; water, D -glucose, sucrose, and levans act as acceptors. The apparent Michaelis constants of levansucrase for sucrose and low-molecular-weight levans (mol. wt. 10,000) are respectively 27mM and 3mM (30 g/l); the yield in levan of the reaction catalyzed by levansucrase reaches 90% in the presence of low-molecular-weight levans acting as initiators. The exocellular levansucrase of Bacillus subtilis Marburg QB 13 appears to be identical with the previously studied enzyme of Bacillus subtilis var. Nigra BS 5. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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