TY  - JOUR
TI  - Investigation Biocatalysts of Immobilized Enzyme on New Supports with Ferri and  Ferro Nuclei
AB  - 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.
AU  - HASANOĞLU ÖZKAN, ELVAN
AU  - Yılmaz, Gamze
AU  - KURNAZ YETIM, NURDAN
AU  - SARI, NURŞEN
DO  - 10.19113/sdufenbed.1237987
PY  - 2023
JO  - Süleyman Demirel Üniversitesi Fen Bilimleri Enstitüsü Dergisi
VL  - 27
IS  - 2
SN  - 1300-7688
SP  - 313
EP  - 320
DB  - TRDizin
UR  - http://search/yayin/detay/1193600
ER  -