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Immobilisation of tyrosinase on siliceous cellular foams affording highly effective and stable biocatalysts

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Abstract

Tyrosinase from Agaricus bisporus was immobilised covalently on mesostructured siliceous foam (MCF) and three mesoporous silicas of SBA-15 type of different pore sizes, regarded as the reference, to reveal that MCF was the superior enzyme support. All the carriers were functionalised using 3-aminopropyltrimethoxysilane and the enzyme was attached covalently via glutaraldehyde or by simple adsorption and it was also cross-linked with glutaraldehyde in selected samples. The experiments indicated that only tyrosinase attached covalently was highly active and that postimmobilisation cross-linking slightly reduced its activity with no improvement in stability. MCF-bound tyrosinase was the best biocatalyst with monophenolase and diphenolase activities of 3627 U mL−1 and 53040 U mL−1 of carrier sediment, respectively. Inactivation studies at 55°C showed that MCF-bound tyrosinase was 20 times more stable than the native enzyme, whereas for typical SBA-15 it was only 12 times. A comparative study with other, non-siliceous enzyme supports indicated that aminated MCF appeared to be the carrier of choice for the covalent attachment of tyrosinase.

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Authors and Affiliations

  1. Department of Bioorganic Chemistry, Faculty of Chemistry, Wrocław University of Technology, Norwida 4/6, 50-373, Wrocław, Poland

    Karolina Labus & Jolanta Bryjak

  2. Department of Chemical Engineering, Faculty of Chemistry, Silesian University of Technology, M. Strzody 7, 44-100, Gliwice, Poland

    Katarzyna Szymańska & Andrzej B. Jarzębski

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  1. Karolina Labus
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  2. Katarzyna Szymańska
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  3. Jolanta Bryjak
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  4. Andrzej B. Jarzębski
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Correspondence to Jolanta Bryjak.

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Labus, K., Szymańska, K., Bryjak, J. et al. Immobilisation of tyrosinase on siliceous cellular foams affording highly effective and stable biocatalysts. Chem. Pap. 69, 1058–1066 (2015). https://doi.org/10.1515/chempap-2015-0115

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