CARB 79 |
| Galactosyltransferase enzyme was successfully immobilized onto the hydrophilic polysaccharide solid support, Sepharose CL-4B via covalent attachment with 99% efficiency. The activity of the bound enzyme system was tested using UDP-glucose as the substrate for transfer onto D-galactose in a purely aqueous system as well as in the ionic liquid, 1-butyl-3-methylimidazolium hexafluorophosphate and the formation of lactose monitored via HPLC. Kinetic studies indicate that the Km of the immobilized transferase is almost halved in the ionic liquid when compared with the aqueous system, indicating a doubling in the rate of the synthesis. The versatility of transferases was demonstrated in full form in our system, by the transfer of UDP-glucose to L-fucose giving rise to the disaccharide, D-Glub1→4Fucb (95% yield). Stability studies were also performed on the immobilized enzyme system over a period of six months. Enzyme activity is maintained up to 90% in [bmim][PF6] and up to 75% in the aqueous system, after the six month period.
|
|
General Posters
6:00 PM-8:00 PM, Tuesday, August 21, 2007 BCEC -- Exhibit Hall - B2, Poster
Division of Carbohydrate Chemistry |