Glycosynthases are mutant glycosidases, which in the presence of activated glycosides and suitable reaction conditions, synthesize oligosaccharides without hydrolysing them. This feature makes these catalysts promising tools for the large scale synthesis of carbohydrates. However, despite the popularity of the glycosynthetic approach, the number of enzymes effecting glycosynthetic reactions is still limited. We report here on the design of novel reaction conditions for a thermophilic α-l-fucosidase mutant, which might provide a route for the production of novel glycosynthases.

Design of new reaction conditions for characterization of a mutant thermophilic a-L-fucosidase / Cobucci Ponzano, B.; Conte, F.; Mazzone, M.; Bedini, Emiliano; Corsaro, MARIA MICHELA; Rossi, Mose'; Moracci, Marco. - In: BIOCATALYSIS AND BIOTRANSFORMATION. - ISSN 1024-2422. - STAMPA. - 26:(2008), pp. 18-24.

Design of new reaction conditions for characterization of a mutant thermophilic a-L-fucosidase

BEDINI, EMILIANO;CORSARO, MARIA MICHELA;ROSSI, MOSE';MORACCI, Marco
2008

Abstract

Glycosynthases are mutant glycosidases, which in the presence of activated glycosides and suitable reaction conditions, synthesize oligosaccharides without hydrolysing them. This feature makes these catalysts promising tools for the large scale synthesis of carbohydrates. However, despite the popularity of the glycosynthetic approach, the number of enzymes effecting glycosynthetic reactions is still limited. We report here on the design of novel reaction conditions for a thermophilic α-l-fucosidase mutant, which might provide a route for the production of novel glycosynthases.
2008
Design of new reaction conditions for characterization of a mutant thermophilic a-L-fucosidase / Cobucci Ponzano, B.; Conte, F.; Mazzone, M.; Bedini, Emiliano; Corsaro, MARIA MICHELA; Rossi, Mose'; Moracci, Marco. - In: BIOCATALYSIS AND BIOTRANSFORMATION. - ISSN 1024-2422. - STAMPA. - 26:(2008), pp. 18-24.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/348878
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