Comparative study of ASNase immobilization on tannic acid-modified magnetic Fe3O4/SBA-15 nanoparticles to enhance stability and reusability. (28th February 2020)
- Record Type:
- Journal Article
- Title:
- Comparative study of ASNase immobilization on tannic acid-modified magnetic Fe3O4/SBA-15 nanoparticles to enhance stability and reusability. (28th February 2020)
- Main Title:
- Comparative study of ASNase immobilization on tannic acid-modified magnetic Fe3O4/SBA-15 nanoparticles to enhance stability and reusability
- Authors:
- Noma, Samir Abbas Ali
Ulu, Ahmet
Acet, Ömür
Sanz, Raúl
Sanz-Pérez, Eloy S.
Odabaşı, Mehmet
Ateş, Burhan - Abstract:
- Abstract : Herein, we report the preparation of tannic acid-modified magnetic Fe3 O4 /SBA-15 nanoparticles and their application as a carrier matrix for immobilization of ASNase, an anticancer enzyme-drug. Abstract : In this work, l -asparaginase was immobilized on tannic acid-modified magnetic mesoporous particles. In brief, Fe3 O4 /SBA-15/tannic acid magnetic particles were synthesized, and their structures and morphologies were fully characterized using various methods. The properties of the free and immobilized enzyme were examined in terms of pH, temperature, thermal stability, storage stability, and reusability. Moreover, the effects of metal ions, inhibitors and organic solvents on the activity of the immobilized enzyme were investigated. Compared to the free enzyme, the immobilized enzyme possessed better tolerance to changes in ambient temperature and pH. Additionally, thermal incubation results showed that the free enzyme lost its activity, while the immobilized enzyme exhibited the opposite behavior. Most strikingly, the immobilized l -asparaginase exhibited a high degree of activity (70%) after being reused 16 times while also demonstrating 71% and 63% storage stability of the initial activity even after 28 days at 4 °C and room temperature, respectively. Together with these results, l -asparaginase was successfully immobilized upon Fe3 O4 /SBA-15/tannic acid magnetic nanoparticles with improved stability properties. This support holds great potential and opensAbstract : Herein, we report the preparation of tannic acid-modified magnetic Fe3 O4 /SBA-15 nanoparticles and their application as a carrier matrix for immobilization of ASNase, an anticancer enzyme-drug. Abstract : In this work, l -asparaginase was immobilized on tannic acid-modified magnetic mesoporous particles. In brief, Fe3 O4 /SBA-15/tannic acid magnetic particles were synthesized, and their structures and morphologies were fully characterized using various methods. The properties of the free and immobilized enzyme were examined in terms of pH, temperature, thermal stability, storage stability, and reusability. Moreover, the effects of metal ions, inhibitors and organic solvents on the activity of the immobilized enzyme were investigated. Compared to the free enzyme, the immobilized enzyme possessed better tolerance to changes in ambient temperature and pH. Additionally, thermal incubation results showed that the free enzyme lost its activity, while the immobilized enzyme exhibited the opposite behavior. Most strikingly, the immobilized l -asparaginase exhibited a high degree of activity (70%) after being reused 16 times while also demonstrating 71% and 63% storage stability of the initial activity even after 28 days at 4 °C and room temperature, respectively. Together with these results, l -asparaginase was successfully immobilized upon Fe3 O4 /SBA-15/tannic acid magnetic nanoparticles with improved stability properties. This support holds great potential and opens up a novel perspective for growing applications. … (more)
- Is Part Of:
- New journal of chemistry. Volume 44:Number 11(2020)
- Journal:
- New journal of chemistry
- Issue:
- Volume 44:Number 11(2020)
- Issue Display:
- Volume 44, Issue 11 (2020)
- Year:
- 2020
- Volume:
- 44
- Issue:
- 11
- Issue Sort Value:
- 2020-0044-0011-0000
- Page Start:
- 4440
- Page End:
- 4451
- Publication Date:
- 2020-02-28
- Subjects:
- Chemistry -- Periodicals
Chimie -- Périodiques
540 - Journal URLs:
- http://www.rsc.org/ ↗
http://www.rsc.org/is/journals/current/newjchem/njc.htm ↗ - DOI:
- 10.1039/d0nj00127a ↗
- Languages:
- English
- ISSNs:
- 1144-0546
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6084.319900
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 13866.xml