Interaction between organophosphorous hydrolase and paraoxon studied by surface chemistry in situ at air-water interface

Sarita V. Mello, Cyril Coutures, Roger M. Leblanc, Tu Chen Cheng, Vipin K. Rastogi, Joseph J. DeFrank

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

Subphase conditions have been optimized to obtain stable organophosphorous hydrolase (OPH-EC 3.1.8.1) as Langmuir films. The Langmuir film was characterized by surface pressure and surface potential-area isotherms and UV-Vis spectroscopy in situ. The interaction of an organophosphorous compound, namely Paraoxon, with the OPH film was investigated for various surface pressures. The stability of the monolayer and the evidence of the enzyme activity at air-water interface support the use of enzyme LB films as biosensor.

Original languageEnglish (US)
Pages (from-to)881-887
Number of pages7
JournalTalanta
Volume55
Issue number5
DOIs
StatePublished - Dec 13 2001

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Keywords

  • Langmuir fims
  • Organophosphorous hydrolase
  • Paraoxon

ASJC Scopus subject areas

  • Analytical Chemistry
  • Spectroscopy

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