Abstract
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(4)] and 1,2,3-trimethylimidazolium methyl sulfate [TMIM][MeSO(4)]. 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 (cat) was obtained. The results demonstrate that highly thermostable glycosidases are more suitable for biocatalytic reactions in water-miscible ILs.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Biocatalysis
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Biotechnology
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Enzyme Stability
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Geobacillus stearothermophilus / enzymology
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Geobacillus stearothermophilus / genetics
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Glycoside Hydrolases / chemistry
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Glycoside Hydrolases / genetics
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Glycoside Hydrolases / metabolism*
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Hydrophobic and Hydrophilic Interactions
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Imidazoles
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Ionic Liquids
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Kinetics
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Temperature
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Thermotoga maritima / enzymology
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Thermotoga maritima / genetics
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Thermus thermophilus / enzymology
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Thermus thermophilus / genetics
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Water
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alpha-Galactosidase / chemistry
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alpha-Galactosidase / genetics
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alpha-Galactosidase / metabolism
Substances
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1,3-dimethylimidazolium
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Bacterial Proteins
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Imidazoles
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Ionic Liquids
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Recombinant Proteins
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Water
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Glycoside Hydrolases
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alpha-Galactosidase