کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
168242 1423405 2014 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Lipase Immobilization onto the Surface of PGMA-b-PDMAEMA-grafted Magnetic Nanoparticles Prepared via Atom Transfer Radical Polymerization
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی مهندسی شیمی (عمومی)
پیش نمایش صفحه اول مقاله
Lipase Immobilization onto the Surface of PGMA-b-PDMAEMA-grafted Magnetic Nanoparticles Prepared via Atom Transfer Radical Polymerization
چکیده انگلیسی

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 pH stability than the free lipase at pH 9.0. After six consecutive cycles, the residual activity of the immobilized lipase is still over 55% of its initial activity.

Graphical AbstractA 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 employed to immobilize the lipase from Burkholderia cepacia successfully by physical adsorption and covalent bonding. Biochemical characterization shows that the immobilized lipase exhibits improved thermal stability, good tolerance to organic solvents with high log P, and higher pH stability than the free lipase at pH 9.0. After six consecutive cycles, the residual activity of the immobilized lipase is still over 55% of its initial activity.Figure optionsDownload as PowerPoint slide

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Chinese Journal of Chemical Engineering - Volume 22, Issues 11–12, November 2014, Pages 1333–1339
نویسندگان
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