Detection of organophosphorus compounds by covalently immobilized organophosphorus hydrolase.
As a consequence of organophosphorus (OP) toxins posing a threat to human life globally, organophosphorus hydrolase (OPH) has become the enzyme of choice to detoxify such compounds. Organophosphorus hydrolase was covalently immobilized onto a quartz substrate for utilization in paraoxon detection. The substrate was cleaned and modified prior to chemical attachment. Each modification step was monitored by imaging ellipsometry as the thickness increased with each modification step. The chemically attached OPH was labeled with a fluorescent dye (7-isothiocyanato-4-methylcoumarin) for the detection of paraoxon in aqueous solution, ranging from 10(-9) to 10(-5) M. UV-visible spectra were also acquired for the determination of the hydrolysis product of para-oxon, namely p-nitrophenol.
Orbulescu
Jhony
J
Department of Chemistry, University of Miami, Coral Gables, Florida 33146, USA.
Constantine
Celeste A
CA
Rastogi
Vipin K
VK
Shah
Saumil S
SS
Defrank
Joseph J
JJ
Leblanc
Roger M
RM
D043303:Aryldialkylphosphatase / Q000737:chemistry*; D004800:Enzymes, Immobilized / Q000737:chemistry*; D009943:Organophosphorus Compounds / Q000032:analysis*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D017550:Spectroscopy, Fourier Transform Infrared
D004800:Enzymes, Immobilized; D009943:Organophosphorus Compounds; D043303:Aryldialkylphosphatase