Stabilization of enzymes in nanoporous materials for biosensor applications

Biosens Bioelectron. 2005 Feb 15;20(8):1674-9. doi: 10.1016/j.bios.2004.07.019.

Abstract

In this study we present the results obtained from efforts to stabilize the inherently unstable m-AChE in nanoporous materials, for the development of biosensors with increased operational stability. Based on existing theoretical models, the entrapment of proteins into relatively small rigid cages drastically increases the stability of these proteins, as this is manifested by their decreased tendency to unfold. The use of two different meso/nanomaterials for the immobilization of the m-AChE shows that there is both a decrease in the leaching of the protein from the biosensor membrane to the test solution, as well as a drastic increase in the operational stability of the resulting biosensor.

Publication types

  • Comparative Study
  • Evaluation Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcholinesterase / analysis*
  • Acetylcholinesterase / chemistry*
  • Biosensing Techniques / methods*
  • Coated Materials, Biocompatible / analysis
  • Coated Materials, Biocompatible / chemistry
  • Enzyme Activation
  • Enzyme Stability
  • Enzymes, Immobilized / analysis
  • Enzymes, Immobilized / chemistry
  • Materials Testing
  • Nanostructures / chemistry*
  • Nanostructures / ultrastructure*
  • Porosity

Substances

  • Coated Materials, Biocompatible
  • Enzymes, Immobilized
  • Acetylcholinesterase