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Magnetic-propelled Fe3O4–chitosan carriers enhance l-asparaginase catalytic activity: a promising strategy for enzyme immobilization

Magnetic-propelled carriers comprising magnetic Fe3O4–chitosan nanoparticles were immobilized with l-asparaginase (l-ASNase). The enzyme displayed enhanced catalytic activity in a weak magnetic field, and thermal and pH stabilities. The conjugated l-ASNase presented higher thermostability and wider...

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Bibliographic Details
Published in:RSC advances 2018-01, Vol.8 (63), p.36063-36075
Main Authors: Ates, Burhan, Ulu, Ahmet, Köytepe, Suleyman, Samir Abbas Ali Noma, Veli Serkan Kolat, Tekin Izgi
Format: Article
Language:English
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Summary:Magnetic-propelled carriers comprising magnetic Fe3O4–chitosan nanoparticles were immobilized with l-asparaginase (l-ASNase). The enzyme displayed enhanced catalytic activity in a weak magnetic field, and thermal and pH stabilities. The conjugated l-ASNase presented higher thermostability and wider range of pH stability in comparison with those of free l-ASNase. Moreover, the reusability of conjugated l-ASNase significantly improved after immobilization and it retained 60.5% of its initial activity after undergoing 16 cycles. The conjugated l-ASNase maintained more than 50% and 48% initial activity after 4 weeks of storage at 4 °C and room temperature, respectively. Furthermore, we reveal that the activity of conjugated l-ASNase onto magnetic Fe3O4–chitosan particles increased by about 3-fold in the weak magnetic field at certain frequencies and flux density compared with that of free l-ASNase. Considering these excellent attributes, the magnetic-propelled mechanism in the transporting and activation of l-ASNase can be used by enhancing the catalytic activity, stability, and efficiency in vital implications for medicinal biotechnology.
ISSN:2046-2069
DOI:10.1039/c8ra06346j