Next Article in Journal
Mutagenicity of New Lead Compounds to Treat Sickle Cell Disease Symptoms in a Salmonella/Microsome Assay
Next Article in Special Issue
Miniaturization in Biocatalysis
Previous Article in Journal
Lipid Vesicle Aggregation Induced by Cooling
Article Menu

Export Article

Open AccessArticle
Int. J. Mol. Sci. 2010, 11(2), 762-778; doi:10.3390/ijms11020762

Covalent Anchoring of Chloroperoxidase and Glucose Oxidase on the Mesoporous Molecular Sieve SBA-15

Erlangen Catalysis Resource Center, Universität Erlangen Nürnberg, Egerlandstr. 3, 91058 Erlangen, Germany
Author to whom correspondence should be addressed.
Received: 4 January 2010 / Revised: 9 February 2010 / Accepted: 9 February 2010 / Published: 24 February 2010
(This article belongs to the Special Issue Biocatalysis)
View Full-Text   |   Download PDF [375 KB, uploaded 19 June 2014]   |  


Functionalization of porous solids plays an important role in many areas, including heterogeneous catalysis and enzyme immobilization. In this study, large-pore ordered mesoporous SBA-15 molecular sieves were synthesized with tetraethyl orthosilicate (TEOS) in the presence of the non-ionic triblock co-polymer Pluronic P123 under acidic conditions. These materials were grafted with 3 aminopropyltrimethoxysilane (ATS), 3-glycidoxypropyltrimethoxysilane (GTS) and with 3 aminopropyltrimethoxysilane and glutaraldehyde (GA-ATS) in order to provide covalent anchoring points for enzymes. The samples were characterized by nitrogen adsorption, powder X-ray diffraction, solid-state NMR spectroscopy, elemental analysis, diffuse reflectance fourier transform infrared spectroscopy and diffuse reflectance UV/Vis spectroscopy. The obtained grafted materials were then used for the immobilization of chloroperoxidase (CPO) and glucose oxidase (GOx) and the resulting biocatalysts were tested in the oxidation of indole. It is found that enzymes anchored to the mesoporous host by the organic moieties can be stored for weeks without losing their activity. Furthermore, the covalently linked enzymes are shown to be less prone to leaching than the physically adsorbed enzymes, as tested in a fixed-bed reactor under continuous operation conditions.
Keywords: functionalization; mesoporous silica; enzyme immobilization functionalization; mesoporous silica; enzyme immobilization

This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Jung, D.; Streb, C.; Hartmann, M. Covalent Anchoring of Chloroperoxidase and Glucose Oxidase on the Mesoporous Molecular Sieve SBA-15. Int. J. Mol. Sci. 2010, 11, 762-778.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top