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

• Luis Enrique Trujillo Toledo ^[1] ; Raúl Gómez Riera ^[2] ; Alexander Banguela Castillo ^[3] ; Melvis Soto Romero ^[4] ; Juan Gabriel Arrieta Sosa ^[4] ; Lázaro Hernández García ^[4]
  1. [1] Centro de Ingeniería Genética y Biotecnológica Laboratorio Interacciobes Planta-Microorganismos
  2. [2] Centro de Ingeniería Genética y Biotecnológica División Química Física
  3. [3] Centro de Ingeniería Genética y Biotecnológica Laboratorio Interacciones Planta Microorganismos
  4. [4] Centro de Ingeniería Genética y Biotecnológica Laboratorio Interacciones Planta Microorganismos División Plantas

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• Localización: Electronic Journal of Biotechnology, ISSN-e 0717-3458, Vol. 7, Nº. 2, 2004, págs. 115-123
• Idioma: inglés
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• Resumen

  • 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