Marty JL


Full name : Marty Jean-Louis

First name : Jean-Louis

Mail : Universite de Perpignan Via Domitia, IMAGES EA4218, Building S, 52 Avenue Paul Alduy, 66860 Perpignan Cedex

Zip Code :

City :

Country : France

Email :

Phone : (33) 68 67 12 13

Fax : (33) 68 67 1221

Website :

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References (33)

Title : Advances in Enzyme-Based Biosensors for Pesticide Detection - Bucur_2018_Biosensors.(Basel)_8_
Author(s) : Bucur B , Munteanu FD , Marty JL , Vasilescu A
Ref : Biosensors (Basel) , 8 : , 2018
Abstract : The intensive use of toxic and remanent pesticides in agriculture has prompted research into novel performant, yet cost-effective and fast analytical tools to control the pesticide residue levels in the environment and food. In this context, biosensors based on enzyme inhibition have been proposed as adequate analytical devices with the added advantage of using the toxicity of pesticides for detection purposes, being more "biologically relevant" than standard chromatographic methods. This review proposes an overview of recent advances in the development of biosensors exploiting the inhibition of cholinesterases, photosynthetic system II, alkaline phosphatase, cytochrome P450A1, peroxidase, tyrosinase, laccase, urease, and aldehyde dehydrogenase. While various strategies have been employed to detect pesticides from different classes (organophosphates, carbamates, dithiocarbamates, triazines, phenylureas, diazines, or phenols), the number of practical applications and the variety of environmental and food samples tested remains limited. Recent advances focus on enhancing the sensitivity and selectivity by using nanomaterials in the sensor assembly and novel mutant enzymes in array-type sensor formats in combination with chemometric methods for data analysis. The progress in the development of solar cells enriched the possibilities for efficient wiring of photosynthetic enzymes on different surfaces, opening new avenues for development of biosensors for photosynthesis-inhibiting herbicides.
ESTHER : Bucur_2018_Biosensors.(Basel)_8_
PubMedSearch : Bucur_2018_Biosensors.(Basel)_8_
PubMedID: 29565810

Title : Biosensor based on electrospun blended chitosan-poly (vinyl alcohol) nanofibrous enzymatically sensitized membranes for pirimiphos-methyl detection in olive oil - El-Moghazy_2016_Talanta_155_258
Author(s) : El-Moghazy AY , Soliman EA , Ibrahim HZ , Marty JL , Istamboulie G , Noguer T
Ref : Talanta , 155 :258 , 2016
Abstract : An ultra-sensitive electrochemical biosensor was successfully developed for rapid detection of pirimiphos-methyl in olive oil, based of genetically-engineered acetylcholinesterase (AChE) immobilization into electrospun chitosan/poly (vinyl alcohol) blend nanofibers. Due to their unique properties such as spatial structure, high porosity, and large surface area, the use of nanofibers allowed improving the biosensor response by two folds. The developed biosensor showed a good performance for detecting pirimiphos-methyl, with a limit of detection of 0.2nM, a concentration much lower than the maximum residue limit allowed set by international regulations (164nM). The biosensor was used for the detection of pirimiphos-methyl in olive oil samples after a simple liquid-liquid extraction, and the recovery rates were close to 100%.
ESTHER : El-Moghazy_2016_Talanta_155_258
PubMedSearch : El-Moghazy_2016_Talanta_155_258
PubMedID: 27216682

Title : Ultra-sensitive biosensor based on genetically engineered acetylcholinesterase immobilized in poly (vinyl alcohol)\/Fe-Ni alloy nanocomposite for phosmet detection in olive oil - El-Moghazy_2016_Food.Chem_203_73
Author(s) : El-Moghazy AY , Soliman EA , Ibrahim HZ , Noguer T , Marty JL , Istamboulie G
Ref : Food Chem , 203 :73 , 2016
Abstract : An ultra-sensitive screen-printed biosensor was successfully developed for phosmet detection in olive oil, based on a genetically-engineered acetylcholinesterase (AChE) immobilized in a azide-unit water-pendant polyvinyl alcohol (PVA-AWP)/Fe-Ni alloy nanocomposite. Fe-Ni not only allowed amplifying the response current but also lowering the applied potential from 80mV to 30mV vs Ag/AgCl. The biosensor showed a very good analytical performance for phosmet detection, with a detection limit of 0.1nM. This detection limit is lower than the allowable concentrations set by international regulations. In addition to the good reproducibility, operational and storage stability, the developed biosensor was successfully used for the determination of phosmet in olive oil samples without any laborious pre-treatment. The phosmet recovery rate was about 96% after a simple liquid-liquid extraction.
ESTHER : El-Moghazy_2016_Food.Chem_203_73
PubMedSearch : El-Moghazy_2016_Food.Chem_203_73
PubMedID: 26948591

Title : Detection of glycoalkaloids using disposable biosensors based on genetically modified enzymes - Espinoza_2014_Anal.Biochem_457_85
Author(s) : Espinoza MA , Istamboulie G , Chira A , Noguer T , Stoytcheva M , Marty JL
Ref : Analytical Biochemistry , 457 :85 , 2014
Abstract : In this work we present a rapid, selective, and highly sensitive detection of alpha-solanine and alpha-chaconine using cholinesterase-based sensors. The high sensitivity of the devices is brought by the use of a genetically modified acetylcholinesterase (AChE), combined with a one-step detection method based on the measurement of inhibition slope. The selectivity was obtained by using butyrylcholinesterase (BChE), an enzyme able to detect these two toxins with differential inhibition kinetics. The enzymes were immobilized via entrapment in PVA-AWP polymer directly on the working electrode surface. The analysis of the resulting inhibition slope was performed employing linear regression function included in Matlab. The high toxicity of alpha-chaconine compared to alpha-solanine due to a better affinity to the active site was proved. The inhibition of glycoalkaloids (GAs) mixture was performed over AChE enzyme wild-type AChE and BChE biosensors resulting in the detection of synergism effect. The developed method allows the detection of (GAs) at 50 ppb in potato matrix.
ESTHER : Espinoza_2014_Anal.Biochem_457_85
PubMedSearch : Espinoza_2014_Anal.Biochem_457_85
PubMedID: 24747413

Title : Design of a macroalgae amperometric biosensor\; application to the rapid monitoring of organophosphate insecticides in an agroecosystem - Nunes_2014_Chemosphere_111_623
Author(s) : Nunes GS , Lins JA , Silva FG , Araujo LC , Silva FE , Mendonca CD , Badea M , Hayat A , Marty JL
Ref : Chemosphere , 111 :623 , 2014
Abstract : The immobilization of enzymes onto transducer support is a mature technology and has been successfully implemented to improve biocatalytic processes for diverse applications. However, there exists still need to design more sophisticated and specialized strategies to enhance the functional properties of the biosensors. In this work, a biosensor platform based on innovative fabrication strategy was designed, and employed for the detection of organophosphate (OP) in natural waters. The biosensor was prepared by incorporating acetylcholinesterase enzyme (AChE) to the graphite paste modified with tetracyanoquinodimethane (TCNQ) mediator, along with the use of a macroalgae (Cladaphropsis membranous) as a functional immobilization support. The novel immobilization design resulted in a synergic effect, and led to enhanced stability and sensitivity of the biosensor. The designed biosensor was used to analyze methyl parathion OP insecticide in water samples collected from a demonstrably contaminated lake of Sao Luis Island, Maranhao, Northeast of Brazil. Water analysis revealed that the aquatic ecosystem was polluted by sub-ppm concentrations of the OP insecticide, and a good correlation was found between values obtained through biosensor and GC-MS techniques. Our results demonstrated that macroalgae-biosensor could be used as a low-cost and sensitive screening method to detect target analyte.
ESTHER : Nunes_2014_Chemosphere_111_623
PubMedSearch : Nunes_2014_Chemosphere_111_623
PubMedID: 24997974

Title : A novel automated flow-based biosensor for the determination of organophosphate pesticides in milk - Mishra_2012_Biosens.Bioelectron_32_56
Author(s) : Mishra RK , Dominguez RB , Bhand S , Munoz R , Marty JL
Ref : Biosensors & Bioelectronics , 32 :56 , 2012
Abstract : This work describes the development of an automated flow-based biosensor that employs genetically modified acetylcholinesterase (AChE) enzymes B394, B4 and wild type B131. The biosensor was based on a screen printed carbon electrode (SPE) that was integrated into a flow cell. Enzymes were immobilised on cobalt (II) phthalocyanine (CoPC) modified electrodes by entrapment in a photocrosslinkable polymer (PVA-AWP). The automated flow-based biosensor was successfully used to quantify three organophosphate pesticides (OPs) in milk samples. The OPs used were chlorpyriphos-oxon (CPO), ethyl paraoxon (EPOx) and malaoxon (MOx). The total analysis time for the assay was less than 15 min. Initially, the biosensor performance was tested in phosphate buffer solution (PBS) using B394, B131 and B4 biosensors. The best detection limits were obtained with B394; therefore, this biosensor was used to produce calibration data in milk with three OPs in the concentration range of 5 x 10(-6)M to 5 x 10(-12)M. The limit of detection (LOD) obtained in milk for CPO, EPOx and MOx were 5 x 10(-12)M, 5 x 10(-9)M and 5 x 10(-10)M, respectively, with a correlation coefficient R(2)=0.9910. The automated flow-based biosensor successfully quantified the OPs in different fat-containing milk samples. There were no false positives or false negatives observed for the analytical figures of merit for the constructed biosensors. This method is inexpensive, sensitive, portable, non-invasive and provides real-time results. This analytical system can provide rapid detection of highly toxic OPs in food matrices such as milk.
ESTHER : Mishra_2012_Biosens.Bioelectron_32_56
PubMedSearch : Mishra_2012_Biosens.Bioelectron_32_56
PubMedID: 22221795

Title : Structural and functional characterisation of a biohybrid material based on acetylcholinesterase and layered double hydroxides - Hidouri_2011_Talanta_85_1882
Author(s) : Hidouri S , Baccar ZM , Abdelmelek H , Noguer T , Marty JL , Campas M
Ref : Talanta , 85 :1882 , 2011
Abstract : This work describes the use of layered double hydroxides (LDHs) for the immobilisation of acetylcholinesterase (AChE) on insulator/semiconductor solid supports. Different LDHs have been synthesised by a co-precipitation method. Afterwards, biohybrid materials based on AChE-LDH mixtures have been produced using wild and recombinant enzymes. Spectroscopic techniques have confirmed the LDH phase identity and the links created between the LDH and AChE. Spectrophotometric assays have demonstrated that most of the biohybrid materials are functional and stable. Several configurations have been used for AChE immobilisation. The highest catalytic responses have been observed when using wild enzyme and immobilising AChE-LDH mixtures on LDHs previously deposited on the solid supports. LDHs have been demonstrated to be suitable host matrices for AChE immobilisation on electrodes for the subsequent development of electrochemical biosensors.
ESTHER : Hidouri_2011_Talanta_85_1882
PubMedSearch : Hidouri_2011_Talanta_85_1882
PubMedID: 21872033

Title : Site-specific immobilization of a (His)6-tagged acetylcholinesterase on nickel nanoparticles for highly sensitive toxicity biosensors - Ganesana_2011_Biosens.Bioelectron_30_43
Author(s) : Ganesana M , Istarnboulie G , Marty JL , Noguer T , Andreescu S
Ref : Biosensors & Bioelectronics , 30 :43 , 2011
Abstract : This paper reports site-specific affinity immobilization of (His)6-tagged acetylcholinesterase (AChE) onto Ni/NiO nanoparticles for the development of an electrochemical screen-printed biosensor for the detection of organophosphate pesticides. The method is based on the specific affinity binding of the His-tagged enzyme to oxidized nickel nanoparticle surfaces in the absence of metal chelators. This approach allows stable and oriented attachment of the enzyme onto the oxidized nickel through the external His residue in one-step procedure, allowing for fast and sensitive detection of paraoxon in the concentration range from 10(-8) to 10(-13) M. A detection limit of 10(-12) M for paraoxon was obtained after 20 min incubation. This method can be used as a generic approach for the immobilization of other His-tagged enzymes for the development of biosensors.
ESTHER : Ganesana_2011_Biosens.Bioelectron_30_43
PubMedSearch : Ganesana_2011_Biosens.Bioelectron_30_43
PubMedID: 21937214

Title : Screen-printed poly(3,4-ethylenedioxythiophene) (PEDOT): A new electrochemical mediator for acetylcholinesterase-based biosensors - Istamboulie_2010_Talanta_82_957
Author(s) : Istamboulie G , Sikora T , Jubete E , Ochoteco E , Marty JL , Noguer T
Ref : Talanta , 82 :957 , 2010
Abstract : This work describes the use of a PEDOT:PSS-based conductive polymer for designing AChE-based biosensors. The transducers were obtained directly by screen-printing a PEDOT:PSS suspension on the surface of thick film carbon electrodes. The obtained working electrodes showed a high conductivity when compared with electrodes modified with conventional mediators like cobalt phthalocyanine or tetracyanoquinodimethane. The PEDOT:PSS polymer was shown to be suitable for thiocholine oxidation, allowing the measurement of AChE activity at 100 mV vs Ag/AgCl. The high conductivity of PEDOT:PSS allowed the accurate detection of the organophosphate insecticide chlorpyrifos-oxon at concentrations as low as 4x10(-9)M, corresponding to an inhibition ratio of 5%.
ESTHER : Istamboulie_2010_Talanta_82_957
PubMedSearch : Istamboulie_2010_Talanta_82_957
PubMedID: 20678652

Title : Kinetic insight into the mechanism of cholinesterasterase inhibition by aflatoxin B1 to develop biosensors - Hansmann_2009_Biosens.Bioelectron_24_2119
Author(s) : Hansmann T , Sanson B , Stojan J , Weik M , Marty JL , Fournier D
Ref : Biosensors & Bioelectronics , 24 :2119 , 2009
Abstract : In this paper, the inhibition effect of aflatoxin B1 on different species of cholinesterases was investigated to unravel action mechanism. The inhibition curves of several cholinesterase mutants (obtained by spectrophotometric measurements of enzyme activity, pS curves) were analyzed. They showed that this toxin reversibly inhibits cholinesterases by binding to a peripheral site located at the entrance of the active site gorge without entering inside the site. Electric eel enzyme revealed the highest inhibition extent with a binding constant estimated to 0.35 microM. This binding prevents the entrance of substrate en route to the catalytic site and also decreases chemical steps of the reaction at the catalytic site: acetylation is reduced to the half and deacetylation is reduced to the third. Electric eel acetylcholinesterase was used to settle an amperometric biosensor. The best detection was obtained by using 0.3 mU enzyme on the electrode and 0.5mM ATCh in the solution. The limit of detection was 3 microM corresponding to 20% inhibition.
ESTHER : Hansmann_2009_Biosens.Bioelectron_24_2119
PubMedSearch : Hansmann_2009_Biosens.Bioelectron_24_2119
PubMedID: 19109006

Title : Automated resolution of dichlorvos and methylparaoxon pesticide mixtures employing a Flow Injection system with an inhibition electronic tongue - Valdes-Ramirez_2009_Biosens.Bioelectron_24_1103
Author(s) : Valdes-Ramirez G , Gutierrez M , Del Valle M , Ramirez-Silva MT , Fournier D , Marty JL
Ref : Biosensors & Bioelectronics , 24 :1103 , 2009
Abstract : An amperometric biosensor array has been developed to resolve pesticide mixtures of dichlorvos and methylparaoxon. The biosensor array has been used in a Flow Injection system, in order to operate automatically the inhibition procedure. The sensors used were three screen-printed amperometric biosensors that incorporated three different acetylcholinesterase enzymes: the wild type from Electric eel and two different genetically modified enzymes, B1 and B394 mutants, from Drosophila melanogaster. The inhibition response triplet was modelled using an Artificial Neural Network which was trained with mixture solutions that contain dichlorvos from 10(-4) to 0.1 microM and methylparaoxon from 0.001 to 2.5 microM. This system can be considered an inhibition electronic tongue.
ESTHER : Valdes-Ramirez_2009_Biosens.Bioelectron_24_1103
PubMedSearch : Valdes-Ramirez_2009_Biosens.Bioelectron_24_1103
PubMedID: 18644713

Title : Phosphotriesterase: a complementary tool for the selective detection of two organophosphate insecticides: chlorpyrifos and chlorfenvinfos - Istamboulie_2009_Talanta_77_1627
Author(s) : Istamboulie G , Fournier D , Marty JL , Noguer T
Ref : Talanta , 77 :1627 , 2009
Abstract : This work shows the possibility of combining the high sensitivity of genetically-modified Drosophila melanogaster acetylcholinesterase (B394) with the ability of phosphotriesterase (PTE) to hydrolyse organophosphate compounds, in the aim of developing a biosensor selective to two insecticides of interest: chlorpyrifos and chlorfenvinfos. The studies clearly demonstrate that chlorfenvinfos is a substrate that acts as competitive inhibitor of PTE, therefore preventing the efficient hydrolysis of other pesticides, including chlorpyrifos. A bi-enzymatic sensor was designed by immobilizing both B394 and PTE in a polyvinylalcohol matrix. The sensor was shown to be able to discriminate between chlorpyrifos and chlorfenvinfos inhibitions.
ESTHER : Istamboulie_2009_Talanta_77_1627
PubMedSearch : Istamboulie_2009_Talanta_77_1627
PubMedID: 19159775

Title : Sensitive amperometric biosensor for dichlorovos quantification: Application to detection of residues on apple skin - Valdes-Ramirez_2008_Talanta_74_741
Author(s) : Valdes-Ramirez G , Fournier D , Ramirez-Silva MT , Marty JL
Ref : Talanta , 74 :741 , 2008
Abstract : This paper presents the construction of an amperometric biosensor for the highly sensitive detection of the organophosphorus insecticide dichlorvos, based on the inhibition of acetylcholinesterase (AChE). The sensitivity of three AChEs from different sources were tested and compared: AChEs from Electric eel (Ee) and genetically engineered (B394) and wild type (B1) from Drosophila melanogaster (Dm). The enzymes were immobilized by entrapment in a photocrosslinkable PVA-SbQ polymer on a screen printed graphite electrode. The enzyme activity was estimated amperometrically at 100mV versus Ag/AgCl by measuring the thiocholine produced by the enzymatic hydrolysis of the acetylthiocholine substrate using cobalt phthalocyanine as electron mediator. The pesticide was measured in the presence of 5% acetonitrile without loss of enzyme activity. The best sensitivity was achieved with the Dm mutant B394 with a detection limit of 7x10(-11)M as compared to 1x10(-8)M with the B1 Dm and 6x10(-7)M with the Ee. The B394 biosensor was used to quantify dichlorvos in a sample of skin apple after extraction with acetonitrile.
ESTHER : Valdes-Ramirez_2008_Talanta_74_741
PubMedSearch : Valdes-Ramirez_2008_Talanta_74_741
PubMedID: 18371703

Title : Development of a portable biosensor for screening neurotoxic agents in water samples - Hildebrandt_2008_Talanta_75_1208
Author(s) : Hildebrandt A , Ribas J , Bragos R , Marty JL , Tresanchez M , Lacorte S
Ref : Talanta , 75 :1208 , 2008
Abstract : A high sensitive portable biosensor system capable of determining the presence of neurotoxic agents in water has been developed. The system consists of (i) a screen-printed electrode with acetylcholinesterase (AChE) immobilized on it, (ii) a self-developed portable potentiostat with an analog to digital (A/D) converter and a serial interface for transferring data to a portable PC and (iii) an own designed software, developed with Lab-Windows CVI, used to record and process the measurements. The system has been developed to perform high precision amperometrical measurements with low drifts, low noise and a good reproducibility. In the configuration depicted, the percentage of AChE inhibition is proportional to the content of neurotoxic agents in a sample. This type of measurement is performed by the steady-state method from the first steady current (by a phosphate buffer solution) and the second steady current (by an enzymatic reaction produced by the addition of acetylthiocholine chloride to the solution). Validation was performed by analyzing spiked water samples containing pesticides. The design is specially suited for screening purposes, does not need sample preconcentration, is totally autonomous and suitable for the field detection of neurotoxic agents in water.
ESTHER : Hildebrandt_2008_Talanta_75_1208
PubMedSearch : Hildebrandt_2008_Talanta_75_1208
PubMedID: 18585203

Title : Acetylcholinesterase-based biosensors for quantification of carbofuran, carbaryl, methylparaoxon, and dichlorvos in 5\% acetonitrile - Valdes-Ramirez_2008_Anal.Bioanal.Chem_392_699
Author(s) : Valdes-Ramirez G , Cortina M , Ramirez-Silva MT , Marty JL
Ref : Anal Bioanal Chem , 392 :699 , 2008
Abstract : Amperometric acetylcholinesterase biosensors have been developed for quantification of the pesticides carbofuran, carbaryl, methylparaoxon, and dichlorvos in phosphate buffer containing 5% acetonitrile. Three different biosensors were built using three different acetylcholinesterase (AChE) enzymes-AChE from electric eel, and genetically engineered (B394) and wild-type (B1) AChE from Drosophila melanogaster. Enzymes were immobilized on cobalt(II) phthalocyanine-modified electrodes by entrapment in a photocrosslinkable polymer (PVA-AWP). Each biosensor was tested against the four pesticides. Good operational stability, immobilisation reproducibility, and storage stability were obtained for each biosensor. The best detection limits were obtained with the B394 enzyme for dichlorvos and methylparaoxon (9.6 x 10(-11) and 2.7 x 10(-9) mol L(-1), respectively), the B1 enzyme for carbofuran (4.5 x 10(-9) mol L(-1)), and both the B1 enzyme and the AChE from electric eel for carbaryl (1.6 x 10(-7) mol L(-1)). Finally, the biosensors were used for the direct detection of the pesticides in spiked apple samples.
ESTHER : Valdes-Ramirez_2008_Anal.Bioanal.Chem_392_699
PubMedSearch : Valdes-Ramirez_2008_Anal.Bioanal.Chem_392_699
PubMedID: 18663432

Title : Highly sensitive detection of organophosphorus insecticides using magnetic microbeads and genetically engineered acetylcholinesterase - Istamboulie_2007_Biosens.Bioelectron_23_506
Author(s) : Istamboulie G , Andreescu S , Marty JL , Noguer T
Ref : Biosensors & Bioelectronics , 23 :506 , 2007
Abstract : This work presents a biosensor for organophosphorus pesticides based on immobilisation of a highly sensitive genetically engineered acetylcholinesterase (B394) by affinity interactions on metal chelate-functionalised magnetic microbeads. The developed sensor has been compared with those based on the widely used Electric eel cholinesterase and a classical entrapment procedure in a polyvinylalcohol-based matrix. The use of the B394 enzyme allowed lowering both IC50 and LOD by a factor of 100 when compared with Electric eel enzyme sensor. The oriented and site-specific immobilisation combined with the high specificity of the B349 mutant allows a more sensitive detection of insecticides, concentrations as low as 1.31(-11)M (IC10) being detected for both pesticides chlorpyriphos-oxon and chlorfenvinphos.
ESTHER : Istamboulie_2007_Biosens.Bioelectron_23_506
PubMedSearch : Istamboulie_2007_Biosens.Bioelectron_23_506
PubMedID: 17826976

Title : Twenty years research in cholinesterase biosensors: from basic research to practical applications - Andreescu_2006_Biomol.Eng_23_1
Author(s) : Andreescu S , Marty JL
Ref : Biomol Eng , 23 :1 , 2006
Abstract : Over the last decades, cholinesterase (ChE) biosensors have emerged as an ultra sensitive and rapid technique for toxicity analysis in environmental monitoring, food and quality control. These systems have the potential to complement or replace the classical analytical methods by simplifying or eliminating sample preparation protocols and making field testing easier and faster with significant decrease in costs per analysis. Over the years, engineering of more sensitive ChE enzymes, development of more reliable immobilization protocols and progress in the area of microelectronics could allow ChE biosensors to be competitive for field analysis and extend their applications to multianalyte screening, development of small, portable instrumentations for rapid toxicity testing, and detectors in chromatographic systems. In this paper, we will review the research efforts over the last 20 years in fabricating AChE biosensors and the recent trends and challenges encounter once the sensor is used outside research laboratory for in situ real sample applications. The review will discuss the generations of cholinesterase sensors with their advantages and limitations, the existing electrode configurations and fabrication techniques and their applications for toxicity monitoring. We will focus on low-cost electrochemical sensors and the approaches used for enzyme immobilization. Recent works for achieving high sensitivity and selectivity are also discussed.
ESTHER : Andreescu_2006_Biomol.Eng_23_1
PubMedSearch : Andreescu_2006_Biomol.Eng_23_1
PubMedID: 16443390

Title : Organophosphorus insecticides extraction and heterogeneous oxidation on column for analysis with an acetylcholinesterase (AChE) biosensor - Dondoi_2006_Anal.Chim.Acta_578_162
Author(s) : Dondoi MP , Bucur B , Danet AF , Toader CN , Barthelmebs L , Marty JL
Ref : Anal Chim Acta , 578 :162 , 2006
Abstract : This paper presents an analysis method for organophosphorus insecticides based on AChE biosensors coupled with a preconcentration and oxidation on a solid phase column. Three organic solvents, acetonitrile (ACN), ethanol and methanol were tested for their influence on AChE activity, insecticide inhibition and their ability to elute the adsorbed insecticides. Our results showed that ACN in a concentration of 5% (v/v) had the less negative effect on biosensor analysis and was the most appropriate organic solvent for the column elution. The presence of the organic solvent in the incubation media of the biosensor was found to induce a reduction of the inhibition percentages. The inhibition of the biosensors was performed in phosphate buffer with 5% (v/v) ACN, while the initial and remaining response of the biosensors were measured in PBS. In these conditions, the LODs of paraoxon and dichlorvos were measured with or without a preconcentration step. The LODs of the AChE biosensor without sample preconcentration were 8 x 10(-8) M for paraoxon and 1 x 10(-7) M dichlorvos and the LOD obtained after the preconcentration step were 2.5 x 10(-8) M for paraoxon and 2.5 x 10(-8) M for dichlorvos. Moreover, the use of the column allowed the heterogeneous oxidation of organophosphorus insecticides for improved LOD.
ESTHER : Dondoi_2006_Anal.Chim.Acta_578_162
PubMedSearch : Dondoi_2006_Anal.Chim.Acta_578_162
PubMedID: 17723708

Title : An electrochemical bioassay for dichlorvos analysis in durum wheat samples - Del Carlo_2006_J.Food.Prot_69_1406
Author(s) : Del Carlo M , Pepe A , De Gregorio M , Mascini M , Marty JL , Fournier D , Visconti A , Compagnone D
Ref : J Food Prot , 69 :1406 , 2006
Abstract : The use of an acetylcholinesterase inhibition assay for the detection of dichlorvos in durum wheat samples by a simplified extraction procedure is reported. After an incubation step, the residual activity was determined with an amperometric biosensor using a portable potentiostat. The use of electric eel and recombinant acetylcholinesterase was compared. The effect of the matrix extract was evaluated by using various sample:solvent ratios, 1:2.5, 1:5, 1:10, and 1:20. The optimal extraction ratio, considering the electrochemical interferences and the effect on enzyme activity and bioavailability of the pesticide, was 1:10. Calibrations were performed in buffer and durum wheat extract. The calculated detection limits in buffer solution were 10 ng/ ml and 0.045 ng/ml for electric eel and recombinant acetylcholinesterase, respectively, whereas operating in the matrix extract they increased up to 45 ng/ml and 0.07 ng/ml, corresponding to 0.45 mg/kg (extraction ratio 1:10) and 0.07 mg/kg in samples. These characteristics allowed the detection of contaminated samples at the maximum residue limit, which is 2 mg/kg and well below. Fortified samples of durum wheat were obtained with both dichlorvos and the commercial product Didivane, which contains dichlorvos as an active molecule. At all the tested levels, the occurrence of contaminant was detected with an average recovery of 75%. The total assay time, including the extraction step, was 30 min. Because several extractions as well as most of the assay steps can be run simultaneously, the throughput for one operator is 12 determinations per hour.
ESTHER : Del Carlo_2006_J.Food.Prot_69_1406
PubMedSearch : Del Carlo_2006_J.Food.Prot_69_1406
PubMedID: 16786864

Title : Comparative investigation between acetylcholinesterase obtained from commercial sources and genetically modified Drosophila melanogaster: application in amperometric biosensors for methamidophos pesticide detection - de Oliveira Marques_2004_Biosens.Bioelectron_20_825
Author(s) : de Oliveira Marques PR , Nunes GS , dos Santos TC , Andreescu S , Marty JL
Ref : Biosensors & Bioelectronics , 20 :825 , 2004
Abstract : Genetically modified acetylcholinesterase (AChE) from Drosophila melanogaster (dm) and from commercial sources, Electric eel (ee), Bovine erythrocites (be) and Human erythrocites (he), were investigated as biological receptors for the detection of methamidophos pesticide based on inhibition studies. Most engineered variant of AChE from dm showed enhanced sensitivity toward methamidophos pesticide. Among 24 dmAChE variants tested, 12 presented a sensitivity comparable to the commercially available eeAChE, but higher than AChEs from be and he. Four were found more sensitive and six others were insensitive to methamidophos insecticide. The D375G,Y370F,Y374A,F376L mutant was the most sensitive, with a ki value of 2.2 X 10(6) mol(-1) L min(-1), three orders of magnitude higher than eeAChE (1.1 X 10(3) mol(-1) L min(-1)). The sensor constructed with genetically modified enzyme showed better characteristics with respect to detection limit and sensitivity compared with those using commercial eeAChE. Differential pulse polarography and chronoamperometry were used as electrochemical techniques to characterize the AChE biosensors. The lower detection limit of 1 ppb was obtained with D375G,Y370F,Y374A,F376L mutant of dmAChE, compared to 90 ppb for the commercial eeAChE. This study may stimulate scientists to develop more sensitive and selective procedures for organophosphorus insecticides detection by using engineered variant of dmAChE.
ESTHER : de Oliveira Marques_2004_Biosens.Bioelectron_20_825
PubMedSearch : de Oliveira Marques_2004_Biosens.Bioelectron_20_825
PubMedID: 15522598

Title : Versatile method of cholinesterase immobilisation via affinity bonds using Concanavalin A applied to the construction of a screen-printed biosensor - Bucur_2004_Biosens.Bioelectron_20_217
Author(s) : Bucur B , Danet AF , Marty JL
Ref : Biosensors & Bioelectronics , 20 :217 , 2004
Abstract : Development of new and more reliable methods to immobilise biomolecules has emerged rapidly due to a continuous need for more stable, sensitive and reliable biosensors. This paper reports a new method of acetylcholine-esterase (AChE) immobilisation based on the high affinity interaction between the glycoproteic enzyme and Concanavalin A (Con A). In order to establish the nature of the link formed between the glycoenzyme, lectin and support, three different configurations are presented. The optimum immobilisation procedure was further used for biosensor manufacturing. The non-specific adsorption is around 3% and the chemical cross-linking of the proteins is avoided. The optimised method allows loading of the working electrode surface with different amounts of enzyme ranging from 0.3 to 3.3 mIU with a good operational stability. The sensor showed a linear response range to acetylthiocholine substrate between 10 and 110 micromol l(-1) with a sensitivity of 3.6 mA l mol(-1). The applicability of the method to the detection of organophosphorus insecticides resulted in a detection limit of 10(-8) mol l(-1) for chlorpyriphos.
ESTHER : Bucur_2004_Biosens.Bioelectron_20_217
PubMedSearch : Bucur_2004_Biosens.Bioelectron_20_217
PubMedID: 15308225

Title : New biosensors for improved detection of environmental and food contamination by anticholinesterase pesticides -
Author(s) : Toutant JP , Massoulie J , Fournier D , Marty JL , Schmid RD , Pfeiffer D , Selkirk ME , Sussman JL , Silman I , Talesa V , Wodak SJ , Stojan J , Magearu V
Ref : In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects , (Inestrosa NC, Campos EO) P. Universidad Catolica de Chile-FONDAP Biomedicina :233 , 2004

Title : Poster (26) Strategy for the development of biosensors based on bio-engineered acetylcholinesterases. -
Author(s) : Marty JL , Andreescu S , Bonnet C , Fournier D
Ref : In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects , (Inestrosa NC, Campos EO) P. Universidad Catolica de Chile-FONDAP Biomedicina :334 , 2004

Title : Development of an EnFET for the detection of organophosphorous and carbamate insecticides - Flores_2003_Anal.Bioanal.Chem_376_476
Author(s) : Flores F , Artigas J , Marty JL , Valdes F
Ref : Anal Bioanal Chem , 376 :476 , 2003
Abstract : A biosensor for the detection of insecticides based on an ion-sensitive field-effect transistor (ISFET) was developed. The resulting device combines the simplicity of potentiometric sensors and the use of associated electronic systems as powerful tools for the acquisition and the processing of data. The enzyme acetylcholinesterase (AChE) was entrapped in a membrane placed on the gate of the ISFET forming an enzyme field-effect transistor (EnFET). The biosensor is applied to the determination of pesticides in spiked real samples. Organophosphorous and carbamate insecticides were measured with a detection limit of 10(-8) mol L(-1). The measurement is based on the production of hydrogen ions due to the hydrolysis of acetylthiocholine by the enzyme. The resulting local pH change is picked up by the underlying pH-sensitive ISFET and transduced as potential variations. The preparation of the membrane is simple and reproducible. The analysis in spiked real samples was performed in tap water and showed detection limits comparable to those obtained by other researchers.
ESTHER : Flores_2003_Anal.Bioanal.Chem_376_476
PubMedSearch : Flores_2003_Anal.Bioanal.Chem_376_476
PubMedID: 12748754

Title : Flow-injection amperometric determination of pesticides on the basis of their inhibition of immobilized acetylcholinesterases of different origin - Jeanty_2002_Anal.Bioanal.Chem_373_691
Author(s) : Jeanty G , Wojciechowska A , Marty JL , Trojanowicz M
Ref : Anal Bioanal Chem , 373 :691 , 2002
Abstract : Determination of the organophosphorus pesticides paraoxon, chlorpyrifos oxon, and malaoxon has been performed by a method based on inhibition of acetylcholinesterase (AChE) and amperometric detection in a flow-injection system with enzymes obtained from the electric eel (eeAChE) and Drosophila melanogaster (dmAChE) and immobilized on the surface of platinum electrode within a layer of poly(vinyl alcohol) bearing styrylpyridinium groups. dmAChE is more sensitive than eeAChE to inhibition by chlorpyrifos oxon and paraoxon. The sensitivity difference was largest for chlorpyrifos oxon (detection limit approx. 17 times lower), and practically none for malaoxon. Determination of the analytes in spiked river water samples by use of the dmAChE biosensor resulted in recoveries from 50 to 90 % for chlorpyrifos oxon at levels of 20 to 40 nmol L(-1), 50 to 100 % for paraoxon at 0.6 to 0.8 micro mol L(-1), and 140 to 190 % for malaoxon at 0.6 to 1.2 micro mol L(-1).
ESTHER : Jeanty_2002_Anal.Bioanal.Chem_373_691
PubMedSearch : Jeanty_2002_Anal.Bioanal.Chem_373_691
PubMedID: 12194025

Title : Screen-printed electrode based on AChE for the detection of pesticides in presence of organic solvents - Andreescu_2002_Talanta_57_169
Author(s) : Andreescu S , Noguer T , Magearu V , Marty JL
Ref : Talanta , 57 :169 , 2002
Abstract : A screen-printed biosensor for the detection of pesticides in water miscible organic solvents is described based on the use of p-aminophenyl acetate as acetylcholinesterase substrate. The oxidation of p-aminophenol, product of the enzymatic reaction was monitored at 100 mV vs. Ag/AgCl screen-printed reference electrode. Miscible organic solvents as ethanol and acetonitrile were tested. The acetylcholinesterase (AChE) was immobilised on a screen-printed electrode surface by entrapment in a PVA-SbQ polymer and the catalytic activity of immobilised AChE was studied in the presence of different percentages of organic solvents in buffer solution. The sensor shows good characteristics when experiments were performed in concentrations of organic solvents below 10%. No significant differences were observed when working with 1 and 5% acetonitrile in the reaction media. Detection limits as low as 1.91x10(-8) M paraoxon and 1.24x10(-9) M chlorpyrifos ethyl oxon were obtained when experiments are carried out in 5% acetonitrile.
ESTHER : Andreescu_2002_Talanta_57_169
PubMedSearch : Andreescu_2002_Talanta_57_169
PubMedID: 18968616

Title : Detection of organophosphorus insecticides with immobilized acetylcholinesterase - comparative study of two enzyme sensors - Andreescu_2002_Anal.Bioanal.Chem_374_39
Author(s) : Andreescu S , Avramescu A , Bala C , Magearu V , Marty JL
Ref : Anal Bioanal Chem , 374 :39 , 2002
Abstract : Two-enzyme systems based on acetylcholinesterase (AChE) - a mono-enzyme system based on AChE, with p-aminophenyl acetate as substrate, and a bi-enzyme system based on AChE and tyrosinase, with phenyl acetate as substrate - have been studied for detection of organophosphate insecticides. The analytical performance and detection limits for determination of the pesticides were compared for the two AChE configurations. The enzyme loading, pH, and applied potential of the bi-enzyme system were optimised. When phenyl acetate was used as substrate for AChE activity the phenol generated by enzymatic hydrolysis was determined with a second enzyme, tyrosinase. Amperometric measurements were performed at 100 mV and -150 mV relative to the Ag/AgCl reference electrode for the mono-enzyme and bi-enzyme systems. Screen-printed sensors were used to detect the organophosphorus pesticides paraoxon and chlorpyrifos ethyl oxon; the detection limits achieved with phenyl acetate as substrate were 5.2x10(-3) mg L(-1) and 0.56x10(-3) mg L(-1), respectively.
ESTHER : Andreescu_2002_Anal.Bioanal.Chem_374_39
PubMedSearch : Andreescu_2002_Anal.Bioanal.Chem_374_39
PubMedID: 12207238

Title : Detection of anatoxin-a(s) in environmental samples of cyanobacteria by using a biosensor with engineered acetylcholinesterases - Devic_2002_Appl.Environ.Microbiol_68_4102
Author(s) : Devic E , Li D , Dauta A , Henriksen P , Codd GA , Marty JL , Fournier D
Ref : Applied Environmental Microbiology , 68 :4102 , 2002
Abstract : Bioassays are little used to detect individual toxins in the environment because, compared to analytical methods, these assays are still limited by several problems, such as the sensitivity and specificity of detection. We tentatively solved these two drawbacks for detection of anatoxin-a(s) by engineering an acetylcholinesterase to increase its sensitivity and by using a combination of mutants to obtain increased analyte specificity. Anatoxin-a(s), a neurotoxin produced by some freshwater cyanobacteria, was detected by measuring the inhibition of acetylcholinesterase activity. By using mutated enzyme, the sensitivity of detection was brought to below the nanomole-per-liter level. However, anatoxin-a(s) is an organophosphorous compound, as are several synthetic molecules which are widely used as insecticides. The mode of action of these compounds is via inhibition of acetylcholinesterase, which makes the biotest nonspecific. The use of a four-mutant set of acetylcholinesterase variants, two mutants that are sensitive to anatoxin-a(s) and two mutants that are sensitive to the insecticides, allows specific detection of the cyanobacterial neurotoxin.
ESTHER : Devic_2002_Appl.Environ.Microbiol_68_4102
PubMedSearch : Devic_2002_Appl.Environ.Microbiol_68_4102
PubMedID: 12147513

Title : Improved multianalyte detection of organophosphates and carbamates with disposable multielectrode biosensors using recombinant mutants of Drosophila acetylcholinesterase and artificial neural networks - Bachmann_2000_Biosens.Bioelectron_15_193
Author(s) : Bachmann TT , Leca B , Vilatte F , Marty JL , Fournier D , Schmid RD
Ref : Biosensors & Bioelectronics , 15 :193 , 2000
Abstract : Engineered variants of Drosophila melanogaster acetylcholinesterase (AChE) were used as biological receptors of AChE-multisensors for the simultaneous detection and discrimination of binary mixtures of cholinesterase-inhibiting insecticides. The system was based on a combination of amperometric multielectrode biosensors with chemometric data analysis of sensor outputs using artificial neural networks (ANN). The multisensors were fully manufactured by screen-printing, including enzyme immobilisation. Two types of multisensors were produced that consisted of four AChE variants each. The AChE mutants were selected in order to obtain high resolution, enhanced sensitivity and minimal assay time. This task was successfully achieved using multisensor I equipped with wild-type Drosophila AChE and mutants Y408F, F368L, and F368H. Each of the AChE variants was selected on the basis of displaying an individual sensitivity pattern towards the target analytes. For multisensor II, the inclusion of F368W, which had an extremely diminished paraoxon sensitivity, increased the sensor's capacity even further. Multisensors I and II were both used for inhibition analysis of binary paraoxon and carbofuran mixtures in a concentration range 0-5 microg/l, followed by data analysis using feed-forward ANN. The two analytes were determined with prediction errors of 0.4 microg/l for paraoxon and 0.5 microg/l for carbofuran. A complete biosensor assay and subsequent ANN evaluation was completed within 40 min. In addition, multisensor II was also investigated for analyte discrimination in real water samples. Finally, the properties of the multisensors were confirmed by simultaneous detection of binary organophosphate mixtures. Malaoxon and paraoxon in composite solutions of 0-5 microg/l were discriminated with predication errors of 0.9 and 1.6 microg/l, respectively.
ESTHER : Bachmann_2000_Biosens.Bioelectron_15_193
PubMedSearch : Bachmann_2000_Biosens.Bioelectron_15_193
PubMedID: 11286337

Title : Amperometric biosensors based on nafion coated screen-printed electrodes for the determination of cholinesterase inhibitors - Gogol_2000_Talanta_53_379
Author(s) : Gogol EV , Evtugyn GA , Marty JL , Budnikov HC , Winter VG
Ref : Talanta , 53 :379 , 2000
Abstract : Screen-printed electrodes coated with the nafion layer have been investigated for cholinesterase biosensor design. The butyrylcholinesterase (ChE) from horse serum was immobilised onto the nafion layer by cross-linking with glutaraldehyde vapours. The biosensors obtained showed better long-term stability and lower working potential in comparison to those obtained with no nafion coating. The sensitivity of a biosensor toward organophosphate pesticides is not affected by the nafion coating. The detection limits were found to be 3.5x10(-7) M for trichlorfon and 1.5x10(-7) M for coumaphos.
ESTHER : Gogol_2000_Talanta_53_379
PubMedSearch : Gogol_2000_Talanta_53_379
PubMedID: 18968123

Title : Flow analysis for determination of paraoxon with use of immobilized acetylcholinesterase reactor and new type of chemiluminescent reaction - Danet_2000_Biopolymers_57_37
Author(s) : Danet AF , Badea M , Marty JL , Aboul-Enein HY
Ref : Biopolymers , 57 :37 , 2000
Abstract : A highly sensitive flow analysis method for determination of acetylcholinesterase (AChE) inhibitors like organophosphorous pesticides using a new chemiluminescent reaction was developed and optimized. This method is fast, sensitive, and cheap, because it requires only one enzyme and its substrate. The system incorporates a reactor with immobilized AChE on controlled pore glass (CPG) and a chemiluminometric detector. Variations in enzyme activity due to inhibition are measured from the changes of concentrations of thiocholine produced when the substrate (acetylthiocholine chloride) is pumped before and after the passage of the solution containing the pesticide through the immobilized AChE reactor. Thiocholine is determined by a new chemiluminescent reaction with luminol in the presence of potassium ferricyanide. The percentage inhibition of enzyme activity is correlated to the pesticide concentration. The inhibited enzyme is reactivated by 10 mM pyridine-2-aldoxime methiodide (2-PAM). The experimental conditions were first optimized for activity determination of the effect of pH, flow rates, and Tris concentrations. For the measurement of AChE inhibition, the appropriate concentration of the substrate is selected such that the rate of noninhibited reaction can be considered unchanged and could be used as a reference. For optimization of experimental conditions for inhibition, several parameters of the system are studied and discussed: flow rate, enzyme-pesticide contact time, luminol concentration, ferricyanide concentration, 2-PAM concentration, and configuration of the FIA manifold. Paraoxon, an organophosphorous pesticide was tested. For an inhibition time of 10 min the calibration graph is linear from 0.1 to 1 ppm paraoxon with a relative standard deviation (n = 5) of 4.6% at 0.5 ppm. For an inhibition time of 30 min the calibration graph is linear from 25 to 250 ppb paraoxon.
ESTHER : Danet_2000_Biopolymers_57_37
PubMedSearch : Danet_2000_Biopolymers_57_37
PubMedID: 10679638

Title : Structure-functional effects of ethanol on Drosophila melanogaster acetylcholinesterase probed by kinetic studies with substrate and inhibitors - Ortega_1999_J.Enzyme.Inhib_14_125
Author(s) : Ortega F , Garcia D , Marty JL
Ref : J Enzyme Inhib , 14 :125 , 1999
Abstract : Ethanol is commonly used to extract and dissolve insecticides acting as inhibitors of acetylcholinesterase (EC Here, experiments were undertaken to investigate the influence of solvent on the reaction and inhibition of the enzyme from Drosophila melanogaster. Ethanol (up to 20% by volume) is shown to induce a dramatic reduction of the affinity of acetylcholinesterase for the acetylthiocholine iodide substrate and all the edrophonium chloride, paraoxon ethyl and propidium diiodide inhibitors, with little influence on the rate constants. Taken together, these results point to a main perturbation of active-center related components involved in the formation and/or stability of Michaelis complexes. Inactivation and ligand-stabilization studies of acetylcholinesterase activity further indicate the occurrence of specific "conformational scrambling" at catalytic and regulatory sites. It is proposed that ethanol affects the enzyme reactivity by modifying the conformation of the aromatic gorge containing the active centre and hence, interactions involved in the molecular recognition of substrates and ligands.
ESTHER : Ortega_1999_J.Enzyme.Inhib_14_125
PubMedSearch : Ortega_1999_J.Enzyme.Inhib_14_125
PubMedID: 10445039

Title : Poster: Detection of acetylcholine using enzyme sensor: application for the determination of organophosphorus and carbamates compounds -
Author(s) : Marty JL , Mionetto N , Rouillon R
Ref : In: Cholinesterases: Structure, Function, Mechanism, Genetics, and Cell Biology , (Massoulie J, Barnard EA, Chatonnet A, Bacou F, Doctor BP, Quinn DM) American Chemical Society, Washington, DC :297 , 1991