Title : Use of esterase activities for the detection of chemical neurotoxic agents - Manco_2009_Protein.Pept.Lett_16_1225
Author(s) : Manco G , Nucci R , Febbraio F
Ref : Protein Pept Lett , 16 :1225 , 2009
Abstract :

The quest for a quick and easy detection of the neurotoxin levels in the environment has fostered the search for systems alternative to currently employed analytical methods such as spectrophotometer, gas-liquid chromatography, thin-layer chromatography, and more recently mass spectrometry. These drawbacks lead to intense research efforts to develop biosensor devices for the determination of these compounds. In this review, we present an overview of the actual development of research in neurotoxin detection by using enzymatic biosensors based on esterase activity, in particular cholinesterases, and carboxylesterases. Detection by enzymatic activity could be carried out measuring the hydrolysis products or the residual enzymatic activity after inhibition, using a transducer system that makes possible the correlation between the determined activity and the analyte concentration. Several transducer systems were adopted for the neurotoxins identification using esterases, including electrochemical, optical, conductimetric and piezoelectric procedures. The differences in the used transducer determine the final sensitivity and specificity of the biosensor. Moreover, a brief description of immobilization procedure, that is an important step in the biosensor development and could affect the final characteristic of biosensor (sensibility, stability, response time and reproducibility), was accomplished. Final considerations on advantages and problems, related to actual development of these technologies, and its prospective were discussed.

PubMedSearch : Manco_2009_Protein.Pept.Lett_16_1225
PubMedID: 19508179

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Citations formats

Manco G, Nucci R, Febbraio F (2009)
Use of esterase activities for the detection of chemical neurotoxic agents
Protein Pept Lett 16 :1225

Manco G, Nucci R, Febbraio F (2009)
Protein Pept Lett 16 :1225