@article{article_1237987, title={Investigation Biocatalysts of Immobilized Enzyme on New Supports with Ferri and Ferro Nuclei}, journal={Süleyman Demirel Üniversitesi Fen Bilimleri Enstitüsü Dergisi}, volume={27}, pages={313–320}, year={2023}, DOI={10.19113/sdufenbed.1237987}, url={https://izlik.org/JA39CC53LW}, author={Hasanoğlu Özkan, Elvan and Kaya Yılmaz, Gamze and Kurnaz Yetim, Nurdan and Sarı, Nurşen}, keywords={Ferrosiyanür, Ferrisiyanür, Enzim İmmobilizasyonu, Koordinasyon Polimerleri, Glukoz oksidaz, SEM-EDS}, abstract={Ferri and ferro coordination polymers in sphere structure were synthesized. Scanning Electron Microscopy (SEM) Energy Dispersive X-Ray Spectroscopy (EDX), Gel Permeation Chromatography (GPC), elemental analysis, and Fourier Transform Infrared Spectroscopy (FT-IR) were performed for chemical and structural characterization of the coordination polymers. Glucose oxidase (GOD) enzyme immobilized to compare of kinetic parameters deal with glucano-1,5 lacton formation. Analyses results illustrate that structures coordination of ions Fe2+ and Fe3+ are different to the same support. It was seen that 2 mol of Fe2+ ion ((PS-N-([Fe(CN)4L]K3)2) was bound per unit structure while 1 mol of Fe3+ ion (PS-N-([Fe(CN)2L]K)) is attaching. Km values of were found as 15.32 and 10.93 for (PS-N-Fe2+)-GOD and (PS-N-Fe3+)-GOD, respectively. Km value for (PS-N-Fe3+)-GOD was found to be 0.5 times higher, possible reason of such a case is the larger reduction potential of Fe3+. As the charge on the coordination structure increased, the enzyme’s affinity for the substrate increased. After 20 repeated measurements, GOD immobilized on (PS-N-Fe3+) polymer retained 45.47% activity, while GOD immobilized on (PS-N-Fe2+) polymer retained 57.86% activity.}, number={2}, organization={Gazi Üniversitesi}