Immobilized glucose oxidase on magnetic silica and alumina: Beyond magnetic separation
| dc.contributor.author | Jaquish, Rigel | |
| dc.contributor.author | Reilly, Austin | |
| dc.contributor.author | Lawson, Bret | |
| dc.contributor.author | Golikova, Ekaterina | |
| dc.contributor.author | Sulman, Aleksandrina | |
| dc.contributor.author | Stein, Barry D | |
| dc.contributor.author | Lakina, Natalya | |
| dc.contributor.author | Tkachenko, Olga | |
| dc.contributor.author | Sulman, Esther | |
| dc.contributor.author | Matveeva, Valentina | |
| dc.contributor.author | Bronstein, Lyudmila M. | |
| dc.date.accessioned | 2025-02-20T16:36:27Z | |
| dc.date.available | 2025-02-20T16:36:27Z | |
| dc.date.issued | 2018-12-01 | |
| dc.description | This record is for a(n) postprint of an article published in International Journal of Biological Macromolecules on 2018-12-01; the version of record is available at https://doi.org/10.1016/j.ijbiomac.2018.08.097. | |
| dc.description.abstract | Here we report immobilization of glucose oxidase (GOx) on magnetic silica (Fe3O4-SiO2) and alumina (Fe3O4-Al2O3) functionalized with amino groups using glutaraldehyde as a linker. Magnetic support based biocatalysts demonstrate high catalytic activity in d-glucose oxidation to D-gluconic acid at pH 5–7.5 and temperature of 30–50 °C with the best activities of 95% and 91% for magnetic silica and alumina, respectively. A comparison of magnetic and non-magnetic alumina and silica shows a significant enhancement of the relative catalytic activity for magnetic supports, while the silica based biocatalysts show a higher activity than the biocatalysts based on alumina. A noticeably higher activity of GOx immobilized on magnetic supports is explained by synergy of the GOx inherent activity and enzyme-like activity of iron oxide nanoparticles, while the enhancement with silica based catalysts is most likely due to a larger pore size and stronger Brønsted acid sites. Excellent relative activity of Fe3O4-SiO2-GOx (95% of native GOx) in a tolerant pH and temperature range as well as high stability in a repeated use (6% relative activity loss after five catalytic cycles) makes this catalyst promising for practical applications. | |
| dc.description.version | postprint | |
| dc.identifier.citation | Jaquish, Rigel, et al. "Immobilized glucose oxidase on magnetic silica and alumina: Beyond magnetic separation." International Journal of Biological Macromolecules, vol. 120, pp. 896-905, 2018-12-01, https://doi.org/10.1016/j.ijbiomac.2018.08.097. | |
| dc.identifier.issn | 0141-8130 | |
| dc.identifier.other | BRITE 1854 | |
| dc.identifier.uri | https://hdl.handle.net/2022/31090 | |
| dc.language.iso | en | |
| dc.relation.isversionof | https://doi.org/10.1016/j.ijbiomac.2018.08.097 | |
| dc.relation.journal | International Journal of Biological Macromolecules | |
| dc.rights | This work may be protected by copyright unless otherwise stated. | |
| dc.title | Immobilized glucose oxidase on magnetic silica and alumina: Beyond magnetic separation |
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