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Title: Chloro-Modified Magnetic Fe{sub 3}O{sub 4}@MCM-41 Core–Shell Nanoparticles for L-Asparaginase Immobilization with Improved Catalytic Activity, Reusability, and Storage Stability

Journal Article · · Applied Biochemistry and Biotechnology
; ; ;  [1]
  1. Inonu University, Department of Chemistry, Faculty of Science and Arts (Turkey)

This paper describes a new support that permits to efficient immobilization of L-asparaginase (L-ASNase). For this purpose, Fe{sub 3}O{sub 4} magnetic nanoparticles were synthesized and coated by MCM-41. 3-chloropropyltrimethoxysilane (CPTMS) was used as a surface modifying agent for covalent immobilization of L-ASNase on the magnetic nanoparticles. The chemical structure; thermal, morphological, and magnetic properties; chemical composition; and zeta potential value of Fe{sub 3}O{sub 4}@MCM-41-Cl were characterized by Fourier transform infrared spectroscopy (FTIR), thermogravimetric analysis (TGA), differential thermal analysis (DTA), differential scanning calorimetry (DSC), vibrating sample magnetometer (VSM), scanning electron microscope (SEM), energy dispersive X-ray (EDX), X-ray diffraction patterns (XRD), and zeta-potential measurement. The immobilization efficiency onto Fe{sub 3}O{sub 4}@MCM-41-Cl was detected as 63%. The reusability, storage, pH, and thermal stabilities of the immobilized L-ASNase were investigated and compared to that of soluble one. The immobilized enzyme maintained 42.2% of its original activity after 18 cycles of reuse. Furthermore, it was more stable towards pH and temperature compared with soluble enzyme. The Michaelis–Menten kinetic properties of immobilized L-ASNase showed a lower V{sub max} and a similar K{sub m} compared to soluble L-ASNase. Immobilized enzyme had around 47 and 32.5% residual activity upon storage a period of 28 days at 4 and 25 °C, respectively. In conclusion, the Fe{sub 3}O{sub 4}@MCM-41-Cl@L-ASNase core–shell nanoparticles could successfully be used in industrial and medical applications.

OSTI ID:
22927819
Journal Information:
Applied Biochemistry and Biotechnology, Vol. 187, Issue 3; Other Information: Copyright (c) 2019 Springer Science+Business Media, LLC, part of Springer Nature; Country of input: International Atomic Energy Agency (IAEA); ISSN 0273-2289
Country of Publication:
United States
Language:
English