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

Hasanoğlu Özkan E., Kaya Yılmaz G., Kurnaz Yetim N., Sarı N.

Süleyman Demirel Üniversitesi Fen Bilimleri Enstitüsü Dergisi, cilt.27, sa.2, ss.313-320, 2023 (Hakemli Dergi) identifier

Özet

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-NFe2+)-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.