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

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 che...

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Bibliographic Details
Published in:Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2005-02, Vol.40 (2), p.75-81
Main Authors: Cao, Xihui, Mabrouki, Mustapha, Mello, Sarita V., Leblanc, Roger M., Rastogi, Vipin K., Cheng, Tu-Chen, DeFrank, Joseph J.
Format: Article
Language:English
Subjects:
Adsorption
Air
Aryldialkylphosphatase - chemistry
Atomic force microscopy
Enzyme Stability
Hydrogen-Ion Concentration
Macromolecular Substances
Membrane Lipids - chemistry
Microscopy, Atomic Force - methods
Organophosphorus hydrolase
Paraoxon
Paraoxon - chemistry
Surface Properties
Water - chemistry
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Summary: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.
ISSN:0927-7765
1873-4367
DOI:10.1016/j.colsurfb.2004.05.009