Thermostable β-Glycosidase from Sulfolobus Solfataricus |
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Authors: | Marco Moracci Maria Ciaramella Roberto Nucci Laurence H. Pearl Ian Sanderson Antonio Trincone Mos Rossi |
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Affiliation: | a Institute of Protein Biochemistry and Enzymology, Naples, Italyb Department of Biochemistry and Molecular Biology, University College, London, UKc Istituto per la Chimica di Molecole di Interesse Biologico, Arco Felice, Naples, Italy |
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Abstract: | The Sulfolobus solfataricus β-glycosidase (Sβgly) is a thermostable and thermophilic glycosyl-hydrolase with broad substrate specificity. The enzyme hydrolizes β-D-gluco-, fuco-, and galactosides, and a large number of /Winked glycoside dimers and oligomers, linked β1-3, β1-4, and β1-6, It is able to hydrolize oligosaccharides with up to 5 glucose residues. Furthermore, it is also able to promote transglycosylation reactions. The corresponding gene has been cloned and overexpressed both in yeast and Escherichia coli. Based on sequence and functional data, the Sβgly has been assigned to the so-called BGA family of glycosyl-hydrolases, including β-glycosidases, β-galactosidases and phosho-β-galactosidases from mesophilic and thermophilic organisms of the three domains. The Sβgly has been crystallized and the resolution of its structure is in progress. Because of its special properties, the enzymes has considerable biotechnological potential. |
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Keywords: | archaea thermostable enzymes β-glucosidase expression in mesophilic hosts sequence homology crystal structure glycosides enzymatic synthesis |
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