Preparation and characterization of amino and carboxyl functionalized core-shell Fe3O4/SiO2 for L-asparaginase immobilization: A comparison study. Issue 5 (2nd September 2020)
- Record Type:
- Journal Article
- Title:
- Preparation and characterization of amino and carboxyl functionalized core-shell Fe3O4/SiO2 for L-asparaginase immobilization: A comparison study. Issue 5 (2nd September 2020)
- Main Title:
- Preparation and characterization of amino and carboxyl functionalized core-shell Fe3O4/SiO2 for L-asparaginase immobilization: A comparison study
- Authors:
- Noma, Samir Abbas Ali
Ulu, Ahmet
Koytepe, Suleyman
Ateş, Burhan - Abstract:
- Abstract: Magnetic nanoparticles are well known as facile and effective support for enzyme immobilization since they have a high surface area, large surface-to-volume ratio, easy separation, a fast and high enzyme loading. This study aims to provide insights on whether acidic or basic modified particles are more effective for L-asparaginase (ASNase) immobilization. Therefore, amino (Fe3 O4 /SiO2 /NH2 ) and carboxyl-functionalized (Fe3 O4 /SiO2 /COOH) particles were prepared. The functional groups, crystalline structure, magnetic properties, morphology, chemical composition and thermal behaviour of the prepared modified nanoparticles were examined via Fourier-transform infra-red spectroscopy (FTIR), X-ray diffraction (XRD), vibrating-sample magnetometer (VSM), scanning electron microscopy (SEM) and energy-dispersive X-ray spectroscopy (EDAX). Under the optimum conditions, the immobilized enzymes were more stable within a certain range of temperatures and pH values in comparison to free enzyme. On the other hand, the immobilized enzymes showed greater stability after incubation for 3 h at 50 °C. The free enzyme maintained only 30% of its initial activity for 4 weeks at 4 °C, while Fe3 O4 /SiO2 /NH2 /ASNase and Fe3 O4 /SiO2 /COOH/ASNase retained more than 78.9% and 56.5% of initial activities under the same conditions, respectively. Moreover, Fe3 O4 /SiO2 /NH2 /ASNase (77.2%) and Fe3 O4 /SiO2 /COOH/ASNase (57.4%) displayed excellent operational stability after 17 repeatedAbstract: Magnetic nanoparticles are well known as facile and effective support for enzyme immobilization since they have a high surface area, large surface-to-volume ratio, easy separation, a fast and high enzyme loading. This study aims to provide insights on whether acidic or basic modified particles are more effective for L-asparaginase (ASNase) immobilization. Therefore, amino (Fe3 O4 /SiO2 /NH2 ) and carboxyl-functionalized (Fe3 O4 /SiO2 /COOH) particles were prepared. The functional groups, crystalline structure, magnetic properties, morphology, chemical composition and thermal behaviour of the prepared modified nanoparticles were examined via Fourier-transform infra-red spectroscopy (FTIR), X-ray diffraction (XRD), vibrating-sample magnetometer (VSM), scanning electron microscopy (SEM) and energy-dispersive X-ray spectroscopy (EDAX). Under the optimum conditions, the immobilized enzymes were more stable within a certain range of temperatures and pH values in comparison to free enzyme. On the other hand, the immobilized enzymes showed greater stability after incubation for 3 h at 50 °C. The free enzyme maintained only 30% of its initial activity for 4 weeks at 4 °C, while Fe3 O4 /SiO2 /NH2 /ASNase and Fe3 O4 /SiO2 /COOH/ASNase retained more than 78.9% and 56.5% of initial activities under the same conditions, respectively. Moreover, Fe3 O4 /SiO2 /NH2 /ASNase (77.2%) and Fe3 O4 /SiO2 /COOH/ASNase (57.4%) displayed excellent operational stability after 17 repeated cycles. These findings suggested that the Fe3 O4 /SiO2 /NH2 and Fe3 O4 /SiO2 /COOH may be utilized as efficient and sustainable supports to developed immobilized ASNase in several biotechnological applications. … (more)
- Is Part Of:
- Biocatalysis and biotransformation. Volume 38:Issue 5(2020)
- Journal:
- Biocatalysis and biotransformation
- Issue:
- Volume 38:Issue 5(2020)
- Issue Display:
- Volume 38, Issue 5 (2020)
- Year:
- 2020
- Volume:
- 38
- Issue:
- 5
- Issue Sort Value:
- 2020-0038-0005-0000
- Page Start:
- 392
- Page End:
- 404
- Publication Date:
- 2020-09-02
- Subjects:
- Magnetic nanoparticles -- silica coating -- L-asparaginase -- enzyme immobilization -- enhanced stability
Enzymes -- Biotechnology -- Periodicals
Enzymes -- Industrial applications -- Periodicals
Biotransformation (Metabolism) -- Periodicals
660.63 - Journal URLs:
- http://informahealthcare.com/journal/bab ↗
http://informahealthcare.com ↗
http://www.gbhap-us.com/journals/346/346-top.htm ↗ - DOI:
- 10.1080/10242422.2020.1767605 ↗
- Languages:
- English
- ISSNs:
- 1024-2422
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 2066.809100
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 13659.xml