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Immobilization of Invertase on Mesoporous Silicas to Obtain Hyper Active Biocatalysts

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Abstract

Comparative studies of invertase immobilized on two mesoporous cellular foams (MCF) and two supports of SBA-15 type with different pore sizes, using three highly recommended methods of protein bonding showed that activity of aminated MCF-based biocatalysts is significantly higher than that of SBA-15 counterparts, with the same textural properties. Specific activities of invertase covalently attached via GLA spacer was about 73–111% of a native enzyme. A unique microenvironment of functionalized cage-like pores of aminated MCFs is deemed to be responsible for this ultra high activity of invertase.

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Acknowledgements

The support of the Polish Ministry for Science and Higher Education for this work under Grants: 1T09C 30 30 and 3T09C 038 28 is gratefully acknowledged. The authors wish to thank Professor J. Wiedermann (Institute for Ferrous Metallurgy, Gliwice) for providing TEM images and helpful discussions and Dr J. Malinowski (Institute of Chemical Engineering, PAS, Gliwice) for nitrogen adsorption analysis.

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Correspondence to Andrzej B. Jarzębski.

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Szymańska, K., Bryjak, J. & Jarzębski, A.B. Immobilization of Invertase on Mesoporous Silicas to Obtain Hyper Active Biocatalysts. Top Catal 52, 1030–1036 (2009). https://doi.org/10.1007/s11244-009-9261-x

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Keywords

  • Invertase
  • Immobilization
  • Protein entrapment
  • Mesoporous materials