摘要
A block copolymer of 2-dimethylaminoethyl methacrylate(DMAEMA) and glycidyl methacrylate(GMA)was grafted onto the surface of magnetic nanoparticles(Fe3O4) via atom transfer radical polymerization.The resultant PGMA-b-PDMAEMA-grafted-Fe3O4 magnetic nanoparticles with amino and epoxy groups were characterized by Fourier transform infrared spectroscopy, powder X-ray diffraction, thermo-gravimetric analysis, and scanning electron microscopy. Lipase from Burkholderia cepacia was successfully immobilized onto the magnetic nanoparticles by physical adsorption and covalent bonding. The immobilization capacity of the magnetic particles is 0.5 mg lipase per mg support, with an activity recovery of up to 43.1% under the optimum immobilization condition. Biochemical characterization shows that the immobilized lipase exhibits improved thermal stability, good tolerance to organic solvents with high lg P, and higher p H stability than the free lipase at p H 9.0. After six consecutive cycles, the residual activity of the immobilized lipase is still over55% of its initial activity.
A block copolymer of 2-dimethylaminoethyl methacrylate(DMAEMA) and glycidyl methacrylate(GMA)was grafted onto the surface of magnetic nanoparticles(Fe3O4) via atom transfer radical polymerization.The resultant PGMA-b-PDMAEMA-grafted-Fe3O4 magnetic nanoparticles with amino and epoxy groups were characterized by Fourier transform infrared spectroscopy, powder X-ray diffraction, thermo-gravimetric analysis, and scanning electron microscopy. Lipase from Burkholderia cepacia was successfully immobilized onto the magnetic nanoparticles by physical adsorption and covalent bonding. The immobilization capacity of the magnetic particles is 0.5 mg lipase per mg support, with an activity recovery of up to 43.1% under the optimum immobilization condition. Biochemical characterization shows that the immobilized lipase exhibits improved thermal stability, good tolerance to organic solvents with high lg P, and higher p H stability than the free lipase at p H 9.0. After six consecutive cycles, the residual activity of the immobilized lipase is still over55% of its initial activity.
基金
Supported by the National Basic Research Program of China(2009CB724706)
