Abstract
A unique mesoporous sol-gel glass possessing a highly ordered porous structure (with three pore sizes of about 50, 150, and 200 Å diameter) was used as a support material for immobilization of the enzyme chloroperoxidase (CPO). CPO was bound onto the glass via a bifunctional ligand, trimethoxysilylpropanal. In situ production of the cosubstrate, H 2O2 was achieved using glucose oxidase. Solvent stability in acetonitrile mixtures was enhanced when a pore size larger than the size of CPO was used (i.e., 200 Å). From these results, it appears that the glass-enzyme complex developed through the present work can be used as high-performance biocatalysts for various chemical-processing applications, particularly in harsh conditions.
| Original language | English |
|---|---|
| Pages (from-to) | 273-285 |
| Number of pages | 13 |
| Journal | Applied Biochemistry and Biotechnology |
| Volume | 113 |
| Issue number | 1-3 |
| DOIs | |
| State | Published - Mar 2004 |
Funding
We wish to acknowledge Dr. J. Dordick and D. Clark for helpful discussions and Ping Wang of the Department of Chemical Engineering, The University of Akron, Akron, OH for advice. Oak Ridge National Laboratory is operated by UT-Battelle, LLC for the Department of Energy under contract DE-AC05-00OR22725. This research was funded by the US Department of Energy, Office of Energy Efficiency and Renewable Energy. This article has been authored by a contractor of the US government under contract DE-AC05-00OR22725. Accordingly, the US government retains a nonexclusive, royalty-free license to publish or reproduce the published form of this contribution, or allow others to do so, for US government purposes.
| Funders | Funder number |
|---|---|
| U.S. Department of Energy | DE-AC05-00OR22725 |
| Office of Energy Efficiency and Renewable Energy |
Keywords
- Acetonitrile
- Chloroperoxidase
- Glucose oxidase
- Horseradish peroxidase
- Sol-gel glass
- Thermostability