Abstract
Proteins adsorbed on nanoparticles (NPs) are being used in biotechnology, biosensors and drug delivery. However, understanding the effect of NPs on the structure of proteins is still in a nascent state. In the present paper tin oxide (SnO2) NPs were synthesized by the reaction of SnCl 45H2O in methanol via the sol-gel method and characterized by x-ray diffraction (XRD), Fourier transform infrared spectroscopy (FT-IR) and transmission electron microscopy (TEM). The binding of these SnO 2-NPs with α-amylase was investigated by using UV-vis, fluorescence and circular dichroism (CD) spectroscopic techniques. A strong quenching of tryptophan fluorescence intensity in α-amylase was observed due to formation of a ground state complex with SnO2-NPs. Far-UV CD spectra showed that the secondary structure of α-amylase was changed in the presence of NPs. The Michaelis-Menten constant (Km), was found to be 26.96 and 28.45mgml- 1, while Vmax was 4.173 and 3.116mgml- 1min- 1 for free and NP-bound enzyme, respectively. © 2011 IOP Publishing Ltd.
| Original language | English (US) |
|---|---|
| Journal | Nanotechnology |
| Volume | 22 |
| Issue number | 45 |
| DOIs | |
| State | Published - Nov 11 2011 |
| Externally published | Yes |
Bibliographical note
Generated from Scopus record by KAUST IRTS on 2023-09-23ASJC Scopus subject areas
- Bioengineering
- Mechanics of Materials
- General Materials Science
- General Chemistry
- Mechanical Engineering
- Electrical and Electronic Engineering