The interaction between OPH and paraoxon at the air-water interface studied by AFM and epifluorescence microscopies

Colloids Surf B Biointerfaces. 2005 Feb 10;40(2):75-81. doi: 10.1016/j.colsurfb.2004.05.009.

Abstract

The paraoxon hydrolysis reaction catalyzed by organophosphorus hydrolase (OPH) monolayer at the air-water interface was studied. OPH-paraoxon interactions, occurring at the two-dimensional interface, by close-packed, highly orientated OPH monolayer, were investigated by several different surface chemistry techniques; e.g. surface pressure area isotherms, atomic force microscopy (AFM), and in situ epifluorescence microscopy. The characterization of OPH Langmuir and Langmuir-Blodgett films prepared in both the presence and absence of paraoxon, demonstrated significantly distinctive feature when compared with one another. Continuous growth of the OPH aggregates is a distinct phenomenon associated with hydrolysis, in addition to the pH changes in the local environment of the enzyme macromolecules.

Publication types

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

MeSH terms

  • Adsorption
  • Air*
  • Aryldialkylphosphatase / chemistry*
  • Enzyme Stability
  • Hydrogen-Ion Concentration
  • Macromolecular Substances
  • Membrane Lipids / chemistry
  • Microscopy, Atomic Force / methods
  • Paraoxon / chemistry*
  • Surface Properties
  • Water / chemistry*

Substances

  • Macromolecular Substances
  • Membrane Lipids
  • Water
  • Aryldialkylphosphatase
  • Paraoxon