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Oxford University Press (OUP), Protein Engineering, Design & Selection, 1-2(24), p. 21-26

DOI: 10.1093/protein/gzq085



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Engineering the stability and the activity of a glycoside hydrolase

This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Glycosidases, the enzymes responsible in nature for the catabolism of carbohydrates, are well-studied catalysts widely used in industrial biotransformations and oligosaccharide synthesis, which are also attractive targets for drug development. Glycosidases from hyperthermophilic organisms (thriving at temperatures > 85 °C) are also interesting models to understand the molecular basis of protein stability and to produce robust tools for industrial applications. Here, we review the results obtained in the last two decades by our group on a β-glycosidase from the hyperthermophilic Archaeon Sulfolobus solfataricus. Our findings will be presented in the general context of the stability of proteins from hyperthermophiles and of the chemo-enzymatic synthesis of oligosaccharides.