Characterization of (SBA-15)-Lipase Composite Material

Abstract

Santa Barbara Amorphous (SBA)-15 mesoporous material was synthesized by hydrothermal method using tri-block copolymer poly(ethylene glycol)-block-poly(propylene glycol)-block-poly(ethylene glycol) (Pluronic P123) as a structure-directing agent and then phenyltriethoxysilane was used to to obtain phenylated SBA-15. Then physical adsorptive method was employed to immobilize lipase to the host material. The immobilized efficiency of enzyme was improved to some extent for the phenylated SBA-15. For structural characterization of prepared samples, powder X-ray diffraction, Fourier transform infrared spectroscopy and low temperature N2 adsorptiondesorption at 77 K were used. The study confirmed that the enzyme went into the pore channels of the SBA-15. Scanning electron microscopic studies showed that the average particle diameter of (SBA-15)-lipase was 337 ± 10 nm, while the average particle diameter of (phenylated SBA-15)-lipase was 340 ± 10 nm. Luminescent spectra showed that the enzyme had already successfully been immobilized to the host materials and after the enzyme was immobilized into host materials the configuration had not been changed. The experimental results of activity on the hydrolysis of glycerol triacetate catalyzed by lipase indicated that compared the immobilized lipase with free lipase the catalytic activity was enhanced and the catalytic use rate of lipase was improved and the ability of resistance to temperature was improved. The repeated use number of the phenylated SBA-15 immobilized lipase as catalyst was improved compared with that of SBA-15 immobilized lipase.