Correlation between thermostability and stability of glycosidases in ionic liquid
Résumé
The activity and stability of a β-glycosidase ( and two α-galactosidases ( and 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 was obtained. The results demonstrate that highly thermostable glycosidases are more suitable for biocatalytic reactions in water-miscible ILs.
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