Catalytical properties of N-glycosylated Gluconacetobacter diazotrophicus levansucrase produced in yeast
Electron. j. biotechnol
; Electron. j. biotechnol;7(2): 115-123, Aug. 2004. ilus, tab, graf
Article
in En
| LILACS
| ID: lil-387552
Responsible library:
CL1.1
ABSTRACT
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.
Full text:
1
Collection:
01-internacional
Database:
LILACS
Main subject:
Oligosaccharides
/
Pichia
/
Gluconacetobacter
/
Fructose
/
Hexosyltransferases
Language:
En
Journal:
EJB
/
Electron. j. biotechnol
/
Electronic journal of biotechnology
Journal subject:
BIOTECNOLOGIA
Year:
2004
Document type:
Article
/
Project document
Affiliation country:
Cuba
Country of publication:
Chile