(366c) Immobilization of Lipase on Hydrophobically Modified Siliceous Mesocellular Foam Under High Flow Condition
AIChE Annual Meeting
Wednesday, November 7, 2007 - 9:08am to 9:26am
Siliceous mesocellular foam (MCF) has well-defined and ultralarge cage-like pores with a mean pore diameter of 24 nm. A lipase (CALB) was entrapped in the pores of hydrophobically modified MCF by the assistance of high flow using the HPLC pump system. A very high enzyme loading of up to 280 mg/g was achieved. The window pore size of MCF was adjusted to the size of CALB to minimize enzyme leaching during catalytic reactions. The immobilized enzymes showed superior recyclability compared to commercial Novozyme 435 in the kinetic resolution reaction of 1-phenylethanol. In addition, the thermal stability of enzyme was also significantly improved by the novel immobilization approach. The CALB immobilized on octadecylsilyl-capped MCF by this method was successfully applied to a packed bed reactor for a continuous flow reaction. A small packed bed reactor (4.6 mm x 250 mm) showed full conversion of (R)-1-phenylethanol to (R)-1-phenylethyl acetate at a high flow rate of 1.5 ml/min. This approach may be applied to immobilize other enzymes onto MCF with tailored window pore size.
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