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Journals / Süleyman Demirel Üniversitesi Fen Bilimleri Enstitüsü Dergisi / 2023 / Cilt: 27 Sayı: 2

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

Ferri ve Ferro çekirdekli Yeni Destekler Üzerinde İmmobilize edilen Enzimin Biyokatalizör Özelliğinin Araştırılması

Elvan Hasanoğlu Özkan(GAZI UNIVERSITY)0000-0001-7338-4015
Gamze Kaya Yılmaz(GAZI UNIVERSITY)0000-0003-0082-6059
Nurdan Kurnaz Yetim(KIRKLARELI UNIVERSITY)0000-0001-6227-0346
Nurşen Sarı(Gazi University)0000-0002-4764-7747
Pages
313–320
Publication Date
2023-08-25
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AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

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.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:Ferri and ferro coordination polymers in sphere structure were synthesized.
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Key Findings & Data:Glucose oxidase (GOD) enzyme immobilized to compare of kinetic parameters deal with glucano-1,5 lacton formation.
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Conclusion & Impact: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.
🔬Design:Araştırma Makalesi
📍Scope:Comprehensive Sample
⚙️Variables:Ferrosiyanür · Ferrisiyanür · Enzim İmmobilizasyonu

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.

Özet

Küre yapısındaki ferri ve ferro koordinasyon polimerleri sentezlendi. Koordinasyon polimerlerinin kimyasal ve yapısal karakterizasyonunda Taramalı Elektron Mikroskopisi (SEM), Enerji Dağılımlı X-Işını Spektroskopisi (EDX), Jel Geçirgenlik Kromatografisi (GPC), elemental analiz ve Fourier Dönüşümlü Kızılötesi Spektroskopisi (FT-IR) kullanılmıştır. Glukano-1,5 lakton oluşumu ile ilgili kinetik parametrelerin karşılaştırılmak için glukoz oksidaz (GOD) enzimi koordinasyon polimerlerine immobilize edilmiştir. Analiz sonuçları, Fe2+ ve Fe3+ iyonlarının aynı desteğe farklı yapılarda koordinasyon gösterdiğini ortaya koymuştur. Birim yapı başına 2 mol Fe2+ iyonu ((PS-N-([Fe(CN)4L]K3)2) bağlanırken, 1 mol Fe3+ iyonunun (PS-N-([Fe(CN)2L]K)) bağlandığı görülmüştür. Km değerleri (PS-N-Fe2+)-GOD ve (PS-N-Fe3+)-GOD için sırasıyla 15,32 ve 10,93 olarak bulunmuştur. (PS-N-Fe3+)-GOD için Km değeri 0,5 kat daha yüksek bulunmuştur, böyle bir durumun olası nedeni Fe3+'ün daha büyük indirgenme potansiyelidir. Tekrarlanan 20 ölçümden sonra, (PS-N-Fe3+) polimeri üzerine immobilize edilen GOD'un %45,47 aktivitesi korunurken, (PS-N-Fe2+) polimeri üzerine immobilize edilen GOD'un %57,86 aktivitesi korunmuştur.

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Cite This Article

Özkan, E. H., Yılmaz, G. K., Yetim, N. K., Sarı, N., *, N. S. (2023). Investigation Biocatalysts of Immobilized Enzyme on New Supports with Ferri and Ferro Nuclei. Süleyman Demirel Üniversitesi Fen Bilimleri Enstitüsü Dergisi, Cilt: 27 Sayı: 2, 313–320. https://doi.org/10.19113/sdufenbed.1237987

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