Enhanced stability of enzyme organophosphate hydrolase interfaced on the carbon nanotubes

Colloids Surf B Biointerfaces. 2010 May 1;77(1):69-74. doi: 10.1016/j.colsurfb.2010.01.009. Epub 2010 Jan 21.

Abstract

In this paper we demonstrate that SWNTs and a covalent immobilization strategy enable very sensitive sensors with excellent long term stability. Organophosphorus hydrolase (OPH) functionalized single and multi-walled carbon nanotube (CNT) conjugates were exploited for direct amperometric detection of paraoxon, a model organophosphate. The catalytic hydrolysis of paraoxon produces equimoles of p-nitrophenol; oxidation was monitored amperometrically in real time under flow-injection (FIA) mode. OPH covalently immobilized on single-walled carbon nanotubes (SWNTs) demonstrated much higher activity than OPH conjugated to multi-walled carbon nanotubes (MWNTs). The dynamic concentration range for SWNT-OPH was 0.5-8.5 micromolL(-1) with a detection limit of 0.01 micromolL(-1) (S/N=3). In addition to this high sensitivity, the immobilized OPH retained a significant degree of enzymatic activity, and displayed remarkable stability with only 25% signal loss over 7 months. These results suggest that covalent immobilization of OPH on CNTs can be used for specific immobilization with advantages of long term stability, high sensitivity, and simplicity.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Biocatalysis
  • Biosensing Techniques
  • Electrochemistry
  • Enzyme Stability
  • Hydrolysis
  • Limit of Detection
  • Microscopy, Electron, Scanning
  • Microscopy, Electron, Transmission
  • Nanotubes, Carbon*
  • Paraoxon / metabolism
  • Phosphoric Monoester Hydrolases / metabolism*

Substances

  • Nanotubes, Carbon
  • phosphorylphosphatase
  • Phosphoric Monoester Hydrolases
  • Paraoxon