| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 6531222 | Journal of Molecular Catalysis B: Enzymatic | 2014 | 7 Pages |
Abstract
- Various methods for immobilising threonine aldolases were investigated.
- Entrapment of the enzyme into three dimensional silicatic matrices was successful.
- Up to 30% of the residual enzyme activity were retained after immobilisation.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Catalysis
Authors
Sandra Kurjatschij, Michael Katzberg, Martin Bertau,