Immobilization and properties of Leuconostoc mesenteroids dextransucrase
β Scribed by Hossein Kaboli; Peter J. Reilly
- Publisher
- John Wiley and Sons
- Year
- 1980
- Tongue
- English
- Weight
- 572 KB
- Volume
- 22
- Category
- Article
- ISSN
- 0006-3592
No coin nor oath required. For personal study only.
β¦ Synopsis
Abstract
Dextransucrase from Leuconostoc mesenteroides (NRRL Bβ512F) was purified by ultrafiltration and gel filtration chromatography in 54% yield. The specific activity of a heart cut was 58.6 U/mg; cumulative purification of that preparation was 247βfold. Of 13 carriers surveyed, only alkylamine porous silica gave immobilization efficiencies consistently above 15 %. Immobilization to silica changed the properties of dextransucrase relatively little, the optimum pH for activity remaining at 5.2, while that for stability decreased from pH 5.5β6 to pH 5.2. In short assays, highest activities of both soluble and immobilized dextransucrase occurred at 30Β°C. Activation energies below that temperature were 8.6 kcal/mol for the former form and 1.7 kcal/mol for the latter. Maximum stabilization of soluble dextransucrase was attained by 5m__M__ Ca^2+^.
π SIMILAR VOLUMES