| Autor: |
Ferdjani, Salim, Ionita, Marina, Roy, Bimalendu, Dion, Michel, Djeghaba, Zeineddine, Rabiller, Claude, Tellier, Charles |
| Předmět: |
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| Zdroj: |
Biotechnology Letters; Jun2011, Vol. 33 Issue 6, p1215-1219, 5p, 1 Chart, 1 Graph |
| Abstrakt: |
The activity and stability of a β-glycosidase ( Thermus thermophilus) and two α-galactosidases ( Thermotoga maritima and Bacillus stearothermophilus) were studied in different hydrophilic ionic liquid (IL)/water ratios. For the ILs used, the glycosidases showed the best stability and activity in 1,3-dimethylimidazolium methyl sulfate [MMIM][MeSO] and 1,2,3-trimethylimidazolium methyl sulfate [TMIM][MeSO]. A close correlation was observed between the thermostability of the enzymes and their stability in IL media. At high IL concentration (80%), a time-dependent irreversible denaturing effect was observed on glycosidases while, at lower concentration (<30%), a reversible inactivation affecting mainly the k was obtained. The results demonstrate that highly thermostable glycosidases are more suitable for biocatalytic reactions in water-miscible ILs. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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