Ates, BurhanUlu, AhmetKoytepe, SuleymanAli Noma, Samir AbbasKolat, Veli SerkanIzgi, Tekin2024-08-042024-08-0420182046-2069https://doi.org/10.1039/c8ra06346jhttps://hdl.handle.net/11616/98526Magnetic-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 degrees 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.eninfo:eu-repo/semantics/openAccessCore-Shell NanoparticlesIron-Oxide NanoparticlesCovalent ImmobilizationChitosan NanoparticlesPerformanceStabilityLipaseNanospheresAdsorptionSeparationMagnetic-propelled Fe3O4-chitosan carriers enhance l-asparaginase catalytic activity: a promising strategy for enzyme immobilizationArticle86336063360753555846010.1039/c8ra06346j2-s2.0-85056115290Q2WOS:000448663500024Q2