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In this study, a L-asparagine (L-Asn) imprinted membranes (L-Asn-MIPs) were synthesized via molecular imprinting for selective and efficient removal of L-Asn. The L-Asn-MIP membrane was prepared by using acrylamide (AAm) and hydroxyethyl methacrylate (HEMA) as a functional monomer and a comonomer, respectively. The membrane was characterized by scanning electron microscopy (SEM) and Fourier Transform infrared spectroscopy (FTIR). The L-Asn adsorption capacity of the membrane was investigated in detail. The maximum L-Asn adsorption capacity was determined as 408.2 mg/g at pH: 7.2, 24 °C. Determination of L-Asn binding behaviors of L-Asn-MIPs also shown with Scatchard analyses. The effect of pH on L-Asn adsorption onto the membrane and also the selectivity and reusability of the L-Asn-MIPs for L-Asn adsorption were determined through L-asparaginase (L-ASNase) enzyme activity measurements. The selectivity of the membrane was investigated by using two different ternary mixtures; L-glycine (L-Gly)/L-histidine (L-His)/L-Asn and L-tyrosin (L-Tyr)/L-cystein(L-Cys)/L-Asn. The obtained results showed that the L-Asn-MIP membranes have a high selectivity towards L-Asn., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 Elsevier B.V. All rights reserved.)

Magnetic-propelled carriers comprising magnetic Fe 3 O 4 -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 Fe 3 O 4 -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., Competing Interests: The authors report no declarations of interest., (This journal is © The Royal Society of Chemistry.)