Jump to main content
Jump to site search

Issue 106, 2015
Previous Article Next Article

Immobilizing and de-immobilizing enzymes on mesoporous silica

Author affiliations


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

Back to tab navigation

Supplementary files

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
Author version
Download author version (PDF)
Citation: RSC Adv., 2015,5, 87706-87712
  •   Request permissions

    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

Search articles by author