Immobilization of lipase onto micron-size magnetic beads.
A novel and economical magnetic poly(methacrylate-divinylbenzene) microsphere (less than 8 microm in diameter) was synthesized by the modified suspension polymerization of methacrylate and cross-linker divinylbenzene in the presence of magnetic fluid. Then, surface aminolysis was employed to obtain a high content of surface amino groups (0.40-0.55 mmolg(-1) supports). The morphology and properties of these magnetic supports were characterized with scanning electron microscopy, transmission electron microscopy, Fourier transform infrared spectroscopy and a vibrating sample magnetometer. These magnetic supports exhibited superparamagnetism with a high specific saturation magnetization (sigma(s)) of 14.6 emicrog(-1). Candida cylindracea lipase was covalently immobilized on the amino-functionalized magnetic supports with the activity recovery up to 72.4% and enzyme loading of 34.0 mgg(-1) support, remarkably higher than the previous studies. The factors involved in the activity recovery and enzymatic properties of the immobilized lipase prepared were studied in comparison with free lipase, for which olive oil was chosen as the substrate. The results show that the immobilized lipase has good stability and reusability after recovery by magnetic separation within 20s.
Liu
Xianqiao
X
Laboratory of Separation Science and Engineering, State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, P.O. Box 353, Beijing 100080, PR China.
Guan
Yueping
Y
Shen
Rui
R
Liu
Huizhou
H
D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry*; D008049:Lipase / Q000737:chemistry* / Q000378:metabolism; D008280:Magnetics; D008855:Microscopy, Electron, Scanning; D046529:Microscopy, Electron, Transmission; D008863:Microspheres; D013696:Temperature
D004800:Enzymes, Immobilized; D008049:Lipase