کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8329411 | 1540212 | 2017 | 24 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Biochemical characterization and stability assessment of Rhizopus oryzae lipase covalently immobilized on amino-functionalized magnetic nanoparticles
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 105, Part 1, December 2017, Pages 300-307
Journal: International Journal of Biological Macromolecules - Volume 105, Part 1, December 2017, Pages 300-307
نویسندگان
Kh. Pashangeh, M. Akhond, H.R. Karbalaei-Heidari, G. Absalan,