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

S V Mello; C Coutures; R M Leblanc; T C Cheng; V K Rastogi; J J Defrank

doi:10.1016/s0039-9140(01)00499-4

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

Talanta. 2001 Dec 13;55(5):881-7. doi: 10.1016/s0039-9140(01)00499-4.

Authors

S V Mello¹, C Coutures, R M Leblanc, T C Cheng, V K Rastogi, J J Defrank

Affiliation

¹ Center for Supramolecular Science, Department of Chemistry, Room 315, Cox Science Building, University of Miami, P.O. Box 249118, 1301 Memorial Drive, Coral Gables, FL, 33124, USA.

PMID: 18968438
DOI: 10.1016/s0039-9140(01)00499-4

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.