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

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

Research output: Contribution to journalArticle

9 Citations (Scopus)

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

Fingerprint

Paraoxon
Langmuir Blodgett films
Hydrolases
Surface chemistry
Air
Pressure
Water
Biosensing Techniques
Enzymes
Spectrum Analysis
Enzyme activity
Ultraviolet spectroscopy
Biosensors
Isotherms
Monolayers

Keywords

  • Langmuir fims
  • Organophosphorous hydrolase
  • Paraoxon

ASJC Scopus subject areas

  • Analytical Chemistry
  • Spectroscopy

Cite this

Interaction between organophosphorous hydrolase and paraoxon studied by surface chemistry in situ at air-water interface. / Mello, Sarita V.; Coutures, Cyril; Leblanc, Roger; Cheng, Tu Chen; Rastogi, Vipin K.; DeFrank, Joseph J.

In: Talanta, Vol. 55, No. 5, 13.12.2001, p. 881-887.

Research output: Contribution to journalArticle

Mello, Sarita V. ; Coutures, Cyril ; Leblanc, Roger ; Cheng, Tu Chen ; Rastogi, Vipin K. ; DeFrank, Joseph J. / Interaction between organophosphorous hydrolase and paraoxon studied by surface chemistry in situ at air-water interface. In: Talanta. 2001 ; Vol. 55, No. 5. pp. 881-887.
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