Sert, BuseAcet, ÖmürNoma, Samir Abbas AliOsman, BilgenOdabaşı, MehmetOcakoğlu, Kasim2024-11-142024-11-142023-07-081011-372Xhttps://doi.org/10.1007/s10562-023-04405-zhttps://link.springer.com/article/10.1007/s10562-023-04405-zhttps://hdl.handle.net/11452/47853Recently, 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 degrees 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.[GRAPHICS].eninfo:eu-repo/semantics/closedAccessGraphitic carbon nitridePhotocatalystsProteinsGraphite carbon nitrideNanolayersL-asnaseEnzyme activityImmobilizationChemistryArticle00102570580000115471557154410.1007/s10562-023-04405-z