Investigation Biocatalysts of Immobilized Enzyme on New Supports with Ferri and Ferro Nuclei

Authors : Elvan HASANOĞLU ÖZKAN, Gamze KAYA YILMAZ, Nurdan KURNAZ YETİM, Nurşen SARI

Pages : 313-320

Doi:10.19113/sdufenbed.1237987

View : 49 | Download : 44

Publication Date : 2023-08-25

Article Type : Research Paper

Abstract :Ferri and ferro coordination polymers in sphere structure were synthesized. Scanning Electron Microscopy insert ignore into journalissuearticles values(SEM); Energy Dispersive X-Ray Spectroscopy insert ignore into journalissuearticles values(EDX);, Gel Permeation Chromatography insert ignore into journalissuearticles values(GPC);, elemental analysis, and Fourier Transform Infrared Spectroscopy insert ignore into journalissuearticles values(FT-IR); were performed for chemical and structural characterization of the coordination polymers. Glucose oxidase insert ignore into journalissuearticles values(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 insert ignore into journalissuearticles values(insert ignore into journalissuearticles values(PS-N-insert ignore into journalissuearticles values([Feinsert ignore into journalissuearticles values(CN);4L]K3);2); was bound per unit structure while 1 mol of Fe3+ ion insert ignore into journalissuearticles values(PS-N-insert ignore into journalissuearticles values([Feinsert ignore into journalissuearticles values(CN);2L]K);); is attaching. Km values of were found as 15.32 and 10.93 for insert ignore into journalissuearticles values(PS-N-Fe2+);-GOD and insert ignore into journalissuearticles values(PS-N-Fe3+);-GOD, respectively. Km value for insert ignore into journalissuearticles values(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 insert ignore into journalissuearticles values(PS-N-Fe3+); polymer retained 45.47% activity, while GOD immobilized on insert ignore into journalissuearticles values(PS-N-Fe2+); polymer retained 57.86% activity.
Keywords : Ferrosiyanür, Ferrisiyanür, Enzim İmmobilizasyonu, Koordinasyon Polimerleri, Glukoz oksidaz, SEM EDS