Abstract
The encapsulation of hemoglobin (Hb) on the mesoporous silicas SBA-15 and Au-doped SBA-15 (Au-SBA-15) has been studied as a model protein adsorption system. The influences of solution pH, structure of mesoporous silicas and gold nanoparticles incorporation on Hb immobilization are investigated in detail. The spectral characteristics of Hb/SBA-15 and Hb/Au-SBA-15 nanoconjugate show an absorption curve quite similar to that of native Hb, indicating that Hb retains its higher-order structure in the mesopores of SBA-15. Direct electrochemistry of Hb is obtained when Hb is adsorpted by mesoporous silicas SBA-15 or Au-SBA-15. Moreover, Hb/Au-SBA-15 exerts enhancing electron transfer ability because of the Au incorporation. Additionally, the Hb/Au-SBA-15 displays good electrocatalytic reduction of hydrogen peroxide with a detection limit of 1.0 μM, about 3 times as low as that for the Hb/SBA-15. The Hb/Au-SBA-15 exhibits higher peroxidase-like activity with the apparent Michaelis-Menton constant (Km) of 2.87 mM, significantly lower than the 7.78 mM value for the Hb/SBA-15.
| Original language | English |
|---|---|
| Pages (from-to) | 142-148 |
| Number of pages | 7 |
| Journal | Electrochemistry Communications |
| Volume | 9 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 2007 |
Keywords
- Au-SBA-15
- Direct chemistry
- Hemoglobin
- Hydrogen peroxide
- SBA-15