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dc.creatorTrujillo Toledo,Luis Enrique
dc.creatorGómez Riera,Raúl
dc.creatorBanguela Castillo,Alexander
dc.creatorSoto Romero,Melvis
dc.creatorArrieta Sosa,Juan Gabriel
dc.creatorHernández García,Lázaro
dc.date2004-08-01
dc.date.accessioned2019-05-03T12:44:07Z
dc.date.available2019-05-03T12:44:07Z
dc.identifierhttps://scielo.conicyt.cl/scielo.php?script=sci_arttext&pid=S0717-34582004000200005
dc.identifier.urihttp://revistaschilenas.uchile.cl/handle/2250/84777
dc.descriptionThe 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
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dc.languageen
dc.publisherPontificia Universidad Católica de Valparaíso
dc.relation10.4067/S0717-34582004000200005
dc.rightsinfo:eu-repo/semantics/openAccess
dc.sourceElectronic Journal of Biotechnology v.7 n.2 2004
dc.titleCatalytical properties of N-glycosylated Gluconacetobacter diazotrophicus levansucrase produced in yeast


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