Catalytical properties of N-glycosylated Gluconacetobacter diazotrophicus levansucrase produced in yeast

The influence of N-glycosylation on the kinetic and catalytical properties of a bacterial fructosyltransferase (LsdA) produced in Pichia pastoris was studied. The glycosylated enzyme behaved similarly to non-glycosylated LsdA when substrate specificity, fructo-oligosaccharide (FOS) production, sucro...

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Autores principales: Trujillo Toledo,Luis Enrique, Gómez Riera,Raúl, Banguela Castillo,Alexander, Soto Romero,Melvis, Arrieta Sosa,Juan Gabriel, Hernández García,Lázaro
Lenguaje:English
Publicado: Pontificia Universidad Católica de Valparaíso 2004
Acceso en línea:http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582004000200005
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Sumario:The influence of N-glycosylation on the kinetic and catalytical properties of a bacterial fructosyltransferase (LsdA) produced in Pichia pastoris was studied. The glycosylated enzyme behaved similarly to non-glycosylated LsdA when substrate specificity, fructo-oligosaccharide (FOS) production, sucrose hydrolysis or levan formation reactions were carried out under different experimental conditions. The kinetic parameters for native or yeast-expressed LsdA determined at 60ºC, condition for the highest hydrolytic activity, followed a conventional Michaelis-Menten kinetics. Synthase activity of this levansucrase increased in water-restricted environments by addition of salt or organic solvent to the reaction mixtures