Enhanced Stability and Activity of Catechol 2,3-Dioxygenase Immobilized on Iron Oxide and Silica Nanoparticles
BioNanoScience, cilt.16, sa.4, 2026 (ESCI, Scopus)
- Yayın Türü: Makale / Tam Makale
- Cilt numarası: 16 Sayı: 4
- Basım Tarihi: 2026
- Doi Numarası: 10.1007/s12668-026-02502-y
- Dergi Adı: BioNanoScience
- Derginin Tarandığı İndeksler: Emerging Sources Citation Index (ESCI), Scopus, Compendex, EMBASE, INSPEC
- Anahtar Kelimeler: Catechol 2,3-dioxygenase, Enzyme immobilization, Enzyme stability, Iron oxide nanoparticles (Fe₃O₄), Silica nanoparticles (SiO₂)
- Atatürk Üniversitesi Adresli: Evet
Özet
Catechol 2,3-dioxygenase is a key enzyme involved in the biodegradation of aromatic pollutants, catalyzing the conversion of catechol to 2-hydroxymuconic semialdehyde. In this study, recombinant catechol 2,3-dioxygenase from Aneurinibacillus migulanus Znu12 was expressed and covalently immobilized on iron oxide nanoparticles and silica nanoparticles using carbodiimide–N-hydroxysuccinimide chemistry to enhance enzymatic activity, stability, and reusability. Scanning electron microscopy and dynamic light scattering analyses confirmed uniform nanoscale dimensions, with silica nanoparticles measuring 30–40 nm before conjugation and 32–45 nm after enzyme attachment, while iron oxide nanoparticles ranged from 20 to 27 nm and increased to approximately 40 nm following immobilization. Fourier-transform infrared spectroscopy revealed characteristic protein-related bands, confirming successful enzyme attachment. Optimization of immobilization conditions resulted in maximal enzyme loading at an optimal cross-linker concentration for each nanoparticle system, along with appropriate nanoparticle dosages, while maintaining high catalytic activity. The silica-immobilized enzyme exhibited maximum activity in the neutral pH range, whereas immobilization on iron oxide nanoparticles extended the active pH range toward alkaline conditions. Substrate specificity assays demonstrated catechol as the preferred substrate compared with phenol and pyrogallol, indicating enhanced catalytic efficiency after immobilization. Overall, this study presents an environmentally friendly strategy for enzyme stabilization using nanoparticle supports, offering a robust and sustainable platform for bioremediation applications in environmental biotechnology.