Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8329411 | International Journal of Biological Macromolecules | 2017 | 24 Pages |
Abstract
Amino-functionalized magnetic nanoparticles (Fe3O4) have been investigated as a support for covalent immobilization of lipase. The nanoparticles were prepared by chemical coprecipitation method and subsequently were coated with 3-aminopropyltriethoxysilane (APTES) via silanization reaction. With glutaraldehyde, as the coupling agent, the lipase from Rhizopus oryzae was successfully immobilized onto the amino-functionalized magnetic nanoparticles. The synthesized support was characterized by transmission electron microscopy and Fourier transform infrared spectroscopy. The results showed that the load of immobilized protein could reach as high as 7 mg protein gâ1 support. The optimum pH for maximal catalytic activity of the immobilized enzyme was 8.0 at 40 °C. The Km values were found as 0.66 and 0.57 mg mLâ1 for the free and immobilized enzymes, respectively. The Vmax values for the free and immobilized enzymes were calculated as 0.14 and 0.47 μmol mgâ1 minâ1, in turn, when p-nitrophenyl butyrate (pNPB) was used as the substrate. A quick separation of lipase from the reaction mixture was achieved when a magnetically active support was applied. In comparison to the free enzyme, the immobilized enzyme was thermally stable and was reusable for 10 cycles while retaining 64% of its initial activity.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Kh. Pashangeh, M. Akhond, H.R. Karbalaei-Heidari, G. Absalan,