Hyperthermophilic microorganisms thrives at temperatures higher than 80 degrees C and proteins and enzymes extracted from these sources are optimally stable and active in the presence of temperatures close to the boiling point of water and of other denaturants, i.e. chaotropic agents, pH, organic solvents, detergents, etc. Therefore, hyperstable enzymes are considered attractive alternatives in biocatalysis and in chemo-enzymatic synthesis. In addition, the molecular bases of the extreme stability to heat and to the ability to work optimally at high temperatures are not completely understood and intrigued biochemists, enzymologists, and biophysics in the last twenty years. In particular, hyperstable glycosidases, enzymes catalysing the hydrolysis of O- and N-glycosidic bonds, have been studied in detail as they are simple model systems promoting single-substrate reactions, and, more importantly, can be exploited for the enzymatic synthesis of oligosaccharides. The importance of these molecules increased enormously in recent years for their potential application in biomedicine. Hyperstable glycosidases, working in transglycosylation mode, can be excellent alternatives to the classical chemical methods helping in the control of regio- and stereoselectivity as conventional enzymes, but also resisting to the organics used in chemical synthesis. We will review here recent advances in the isolation and characterization of glycosidases from hyperthermophilic microorganisms and the methods used for their application in oligosaccharide synthesis.
GLYCOSIDE HYDROLASES FROM HYPERTHERMOPHILES: STRUCTURE, FUNCTION AND EXPLOITATION IN OLIGOSACCHARIDE SYNTHESIS
CobucciPonzano Beatrice;Moracci Marco
2010
Abstract
Hyperthermophilic microorganisms thrives at temperatures higher than 80 degrees C and proteins and enzymes extracted from these sources are optimally stable and active in the presence of temperatures close to the boiling point of water and of other denaturants, i.e. chaotropic agents, pH, organic solvents, detergents, etc. Therefore, hyperstable enzymes are considered attractive alternatives in biocatalysis and in chemo-enzymatic synthesis. In addition, the molecular bases of the extreme stability to heat and to the ability to work optimally at high temperatures are not completely understood and intrigued biochemists, enzymologists, and biophysics in the last twenty years. In particular, hyperstable glycosidases, enzymes catalysing the hydrolysis of O- and N-glycosidic bonds, have been studied in detail as they are simple model systems promoting single-substrate reactions, and, more importantly, can be exploited for the enzymatic synthesis of oligosaccharides. The importance of these molecules increased enormously in recent years for their potential application in biomedicine. Hyperstable glycosidases, working in transglycosylation mode, can be excellent alternatives to the classical chemical methods helping in the control of regio- and stereoselectivity as conventional enzymes, but also resisting to the organics used in chemical synthesis. We will review here recent advances in the isolation and characterization of glycosidases from hyperthermophilic microorganisms and the methods used for their application in oligosaccharide synthesis.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
