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Issue 106, 2015
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Immobilizing and de-immobilizing enzymes on mesoporous silica

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Abstract

Beta glucosidase was immobilised as a model enzyme within mesoporous silica (MCF) at a high loading (80 mg g−1). The enzyme was further entrapped within the material by precipitating additional silica within the channels. This entrapment was performed by the polycondensation of tetraethoxysilane under very mild conditions (pure water). Although unreactive while entrapped, in this state the enzyme was highly stable towards heat treatments of 60–70 °C. Upon release from the matrix by a mild silica dissolution step involving a fluoride comprising buffer, the enzyme regained most of its original activity. With this we developed a novel protein entrapment/release scheme, which is designed along the principles of orthogonal protection group chemistry as the protection/deprotection steps do not affect the integrity of the (bio)molecule. The principle can be adopted to many previously developed mesoporous silica/enzyme biocomposites and will allow the application of enzyme dependent diagnostic devices in applications involving demanding environmental storage requirements.

Graphical abstract: Immobilizing and de-immobilizing enzymes on mesoporous silica

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Publication details

The article was received on 22 Sep 2015, accepted on 30 Sep 2015 and first published on 08 Oct 2015


Article type: Paper
DOI: 10.1039/C5RA19568C
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Citation: RSC Adv., 2015,5, 87706-87712
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    Immobilizing and de-immobilizing enzymes on mesoporous silica

    V. Zlateski, T. C. Keller, J. Pérez-Ramírez and R. N. Grass, RSC Adv., 2015, 5, 87706
    DOI: 10.1039/C5RA19568C

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