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Journals / Iğdır Üniversitesi Fen Bilimleri Enstitüsü Dergisi / 2026 / Cilt: 16 Sayı: 3

Covalent Immobilization and Characterization of Xylanase from Aspergillus oryzae on ReliZyme EA403 Support

Aspergillus oryzae Kaynaklı Ksilanazın ReliZyme EA403 Desteği Üzerine Kovalent İmmobilizasyonu ve Karakterizasyonu

Ali Toprak(NEVSEHIR HACI BEKTAS VELI UNIVERSITY, ACIGÖL VOCATIONAL HIGHER SCHOOL OF TECHNICAL SCIENCES)0000-0002-6520-3226
Pages
1101–1114
Publication Date
2026-09-01
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AI Summary & Key Takeaways

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

These outcomes highlight the suitability of the prepared immobilized xylanase for repeated utilization in industrial processes that operate under high-temperature conditions.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:This research focused on developing a stabilized biocatalyst by fixing xylanase, derived from Aspergillus oryzae, onto a ReliZyme EA403 carrier through covalent bonds.
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Key Findings & Data:A comprehensive evaluation was then conducted to compare the operational properties of the enzyme before and after immobilization, including its optimal working conditions, kinetic behavior, heat tolerance, and performance over multiple reaction cycles.
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Conclusion & Impact:These outcomes highlight the suitability of the prepared immobilized xylanase for repeated utilization in industrial processes that operate under high-temperature conditions.
🔬Design:Araştırma Makalesi
📍Scope:Comprehensive Sample
⚙️Variables:Ksilanaz · ReliZyme EA403 · Glutaraldehit

Abstract

This research focused on developing a stabilized biocatalyst by fixing xylanase, derived from Aspergillus oryzae, onto a ReliZyme EA403 carrier through covalent bonds. The support was first activated with glutaraldehyde to facilitate the binding of the enzyme. A comprehensive evaluation was then conducted to compare the operational properties of the enzyme before and after immobilization, including its optimal working conditions, kinetic behavior, heat tolerance, and performance over multiple reaction cycles. As a result of the immobilization process, the optimum pH value for both the free and immobilized enzyme was determined to be maintained at pH 6.0. According to kinetic analysis, the Km values were found to be 10.66 mg/mL for the free xylanase and 17.21 mg/mL for the immobilized xylanase, while the Vmax values were calculated as 1660.5 U/mg protein and 112.5 U/mg protein, respectively. Furthermore, a significant enhancement in the thermal stability of the immobilized enzyme was observed as a consequence of the immobilization. The half-life of the immobilized xylanase at 80°C was approximately 12.5-fold higher compared to its free counterpart. Operational stability tests further revealed that the immobilized biocatalyst maintained 82% of its initial catalytic efficiency after being reused twelve times in a batch system. These outcomes highlight the suitability of the prepared immobilized xylanase for repeated utilization in industrial processes that operate under high-temperature conditions.

Özet

Bu çalışmanın amacı, Aspergillus oryzae kaynaklı ksilanaz enzimini ReliZyme EA403 desteği üzerine kovalent olarak immobilize etmek ve immobilize enzimin biyokimyasal özelliklerini karakterize etmektir. Enzim immobilizasyonu, glutaraldehit ile aktive edilmiş ReliZyme EA403 desteği kullanılarak gerçekleştirilmiştir. Optimum immobilizasyon koşulları belirlenmiş ve serbest ile immobilize enzimin optimum sıcaklık, optimum pH, kinetik parametreler, termal kararlılık ve tekrar kullanım kararlılığı karşılaştırmalı olarak incelenmiştir. İmmobilizasyon işlemi sonucunda hem serbest hem de immobilize enzimin optimum pH değerinin 6 olduğu tespit edilmiştir. Kinetik parametrelerden Km değerleri serbest ksilanaz için 10.66 mg/mL ve immobilize ksilanaz için 17.21 mg/mL olarak bulunurken, Vmax değerleri sırasıyla 1660.5 U/mg protein ve 112.5 U/mg protein olarak hesaplanmıştır. İmmobilize enzimin termal kararlılığında önemli bir artış gözlemlenmiştir. İmmobilize enzimin 80°C'deki yarılanma ömrü serbest enzime kıyasla yaklaşık 12.5 kat artmıştır. Ayrıca, immobilize ksilanazın kesikli bir reaktör sisteminde 12 kullanım döngüsünden sonra başlangıç aktivitesinin %82'sini koruduğu tespit edilmiştir. Elde edilen bulgular, ReliZyme EA403 üzerine kovalent olarak immobilize edilen ksilanazın, yüksek sıcaklık gerektiren endüstriyel uygulamalarda ve tekrarlı kullanımda etkin bir biyokatalizör olarak potansiyelini ortaya koymaktadır.

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Cite This Article

Toprak, A. (2026). Covalent Immobilization and Characterization of Xylanase from Aspergillus oryzae on ReliZyme EA403 Support. Iğdır Üniversitesi Fen Bilimleri Enstitüsü Dergisi, Cilt: 16 Sayı: 3, 1101–1114. https://doi.org/10.21597/jist.1819342

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