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    A New Design to Enhance the Enzyme Activities: Investigation of L-Asparaginase Catalytic Performance by IMAC Effect on g-C3N4 Nanolayers
    (Springer, 2024) Sert, Buse; Acet, Ömür; Noma, Samir Abbas Ali; Osman, Bilgen; Odabaşı, Mehmet; Ocakoğlu, Kasım
    Recently, graphite carbon nitride (g-C3N4) has come to the fore as a new material with its carbon-based two-dimensional structure, simple preparation procedure, and excellent physicochemical stability properties. This study aims to investigate the activity and kinetic studies of the L-asparaginase enzyme via immobilized metal ion affinity chromatography (IMAC) process of g-C3N4 nanolayers. Firstly, g-C3N4 nanolayers were synthetized and Ni2+ ions were binded their surfaces. The synthesized samples were investigated by SEM, ICP-MS, XRD, and FTIR. The highest L-ASNase adsorption on Ni2+-g-C3N4 nanostructures was 444.1 mg/g, at 3 mg/mL L-ASNase concentration. Optimal medium conditions for L-ASNase adsorption occurred at pH 8.0 and 25 °C. The immobilized enzyme showed improved stability relating to the soluble enzyme in extreme situations. On the other hand, the storage stability and reusability of the immobilized enzyme were found to be approximately 64 and 53% of the original activity after 29 days at room temperature and 10 cycles, respectively. From the Michaelis–Menten constants Km and Vmax, both of them decreased after immobilization compare to the free one. The obtained outcomes showed that the g-C3N4 is a suitable matrix for L-asparaginase immobilization with ideal catalytic efficiency and improved stability.
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    A rational approach for 3D recognition and removal of L-asparagine via molecularly imprinted membranes
    (Elsevier B.V., 2023) Acet, Ömür; Ali Noma, Samir Abbas; Önal Acet, Burcu; Dikici, Emrah; Osman, Bilgen; Odabaşı, Mehmet
    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.