Engineering the stability and the activity of a glycoside hydrolase.
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.
Cobucci-Ponzano
Beatrice
B
Institute of Protein Biochemistry, Consiglio Nazionale delle Ricerche, Via P. Castellino 111, 80131 Naples, Italy.
Perugino
Giuseppe
G
Rossi
Mosè
M
Moracci
Marco
M
D004795:Enzyme Stability; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D009844:Oligosaccharides / Q000378:metabolism*; D011487:Protein Conformation; D015202:Protein Engineering; D048229:Sulfolobus solfataricus / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism
D009844:Oligosaccharides; D006026:Glycoside Hydrolases