title: Lipase immobilized on magnetic multi-walled carbon nanotubes.
abstract: Magnetic iron oxide nanoparticles were loaded onto the surfaces of multiwalled carbon nanotubes (MWNTs) by the impregnation method. The obtained magnetic nanotubes were characterized with high-resolution transmission electron microscopy (HRTEM), X-ray photoelectron spectroscopy (XPS), and X-ray diffraction (XRD). Yarrowia lipolytica lipase was covalently immobilized on the magnetic MWNTs (M-MWNTs). M-MWNT-lipase was characterized with XPS spectra and XRD patterns. The structural change of the immobilized lipase was analyzed through circular dichroism spectroscopy. M-MWNT-lipase was utilized for the resolution of (R, S)-1-phenyl ethanol in the organic solvent of heptane. Compared to the native lipase, the lipase immobilized on M-MWNTs has significantly improved its enzymatic activity for the resolution of (R, S)-1-phenyl ethanol in heptane. M-MWNT-lipase can be easily recovered after catalysis. In addition, the effect of sonication time on the catalytic activity was also investigated. It is found that, up to 30min sonication, the catalysis by M-MWNT-lipase is almost not affected. While, the catalytic activity of the native lipase is decreased with sonication time.
authors: Department of Biochemical Engineering, Beijing University of Chemical Technology, Beijing, China.
authors: Huishan
authors: H
authors: Tan
authors: Wei
authors: W
authors: Feng
authors: Peijun
authors: P
authors: Ji
mesh_terms: D002942:Circular Dichroism; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006868:Hydrolysis; D008049:Lipase / Q000378:metabolism*; D008280:Magnetics; D037742:Nanotubes, Carbon / Q000737:chemistry*; D010626:Phenylethyl Alcohol / Q000378:metabolism; D013010:Sonication; D013696:Temperature; D013997:Time Factors; D025062:Yarrowia / Q000201:enzymology*
chemical_list: D004800:Enzymes, Immobilized; D037742:Nanotubes, Carbon; D008049:Lipase; D010626:Phenylethyl Alcohol