Abstract
Carbon nanotubes (CNTs) did not exhibit strong interactions with Biliverdin IXB reductase enzyme (BVRB) in water. With the use of noncovalent functionalization by the surfactant Triton X-100, the surfaces of the CNTs were changed from hydrophobic to hydrophilic. The hydrophilic surface of the CNT-Triton conjugate interacts with the hydrophilic surface of BVRB, thus creating a water-soluble complex. Results from ultracentrifugation through a sucrose gradient and gel electrophoresis show the presence of the enzyme. Raman spectroscopy confirmed that the enzyme indeed interacts with CNT-Triton conjugates.
| Original language | English |
|---|---|
| Pages (from-to) | 209-213 |
| Number of pages | 5 |
| Journal | Journal of Nanoscience and Nanotechnology |
| Volume | 3 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Jun 2003 |
Keywords
- Carbon nanotubes
- Enzymes
- Functionalization
- Raman
- Sensing