Biofunctionalization of Magneto-Plasmonic Fe3O4@SiO2-NH2-Au Heterostructures with the Cellulase from Trichoderma reesei
The study focuses on the synthesis of Fe<sub>3</sub>O<sub>4</sub>@SiO<sub>2</sub>-NH<sub>2</sub>-Au heterostructures with magneto-plasmonic properties composed of well-defined cubic Fe<sub>3</sub>O<sub>4</sub> cores (79 nm) covered with 10 nm silica shell and gold nanoparticles (8 nm) fabricated on silica shell. The surface-anchored MHDA (16-mercaptohexadecanoic acid) linker facilitated cellulase bioconjugation, which was confirmed through Raman spectroscopy. The presence of gold nanoparticle islands on the heterostructure enabled surface-enhanced Raman scattering (SERS), demonstrating the potential for bioactive substance identification. Immobilization of cellulase allowed for pH enhancement and enzyme thermal stability. The optimal pH shifted from 4.0 (free enzyme) to 6.0 while thermal stability increased by 20 °C. The immobilized cellulase kept its 49% activity after five hydrolysis cycles, compared to significantly lower activity for free cellulase. The proposed heterostructures for cellulase immobilization demonstrate potential for practical applications.
Authors
- Renata Wojnarowska‐Nowak (ORCID: https://orcid.org/0000-0003-2550-227X)
- Klaudia Niemczyk
- Magdalena Kulpa-Greszta (ORCID: https://orcid.org/0000-0002-0874-4704)
- Anna Tomaszewska (ORCID: https://orcid.org/0000-0003-2548-0568)
- Daniel Broda (ORCID: https://orcid.org/0000-0003-0876-6951)
- Robert Pązik (ORCID: https://orcid.org/0000-0002-4662-6688)
- Oliwia Hryców
Institutions
- University of Rzeszów (PL)
Publication Details
- Journal
- Molecules
- Published
- 2025-02-06
- DOI
- https://doi.org/10.3390/molecules30030756
- Citations
- 2
- Primary Topic
- Enzyme Catalysis and Immobilization
- Type
- article
- Field-Weighted Citation Impact
- 1.61