Development of an amperometric biosensor based on acetylcholine esterase covalently bound to a new support material

Khayyami, Masoud; Pita, Marcos; Gaspar, Ignacio De; Johansson, Gillis; Danielsson, Bengt; Larsson, Per‐Olof

doi:10.1016/s0039-9140(97)00182-3

Cited by 51 publications

(13 citation statements)

References 7 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Thiocholine is electrochemically active and can be determined by anodic oxidation, producing dithiobischoline, at 0.6 V on Ag/AgCl electrode [91]. Several electrochemical mediators, such as Meldola Blue, hexacyanoferrate or cobalt phthalocyanine, can be used in order to enhance signal detection and to decrease the contribution from other electroactive compounds presents in the sample [84,85,[92][93][94].…”

Section: Transducer Systemsmentioning

confidence: 99%

Use of Esterase Activities for the Detection of Chemical Neurotoxic Agents

Manco¹,

Nucci²,

Febbraio

2009

PPL

View full text Add to dashboard Cite

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.

show abstract

Section: Transducer Systemsmentioning

confidence: 99%

Use of Esterase Activities for the Detection of Chemical Neurotoxic Agents

Manco¹,

Nucci²,

Febbraio

2009

PPL

View full text Add to dashboard Cite

show abstract

“…The use of electrochemical mediators, such as Meldola Blue (MB), hexacyanoferrate (III) or cobalt phthalocyanine (CoPC), allows for a lower working potential, minimising the contribution from other possible electroactive compounds of the sample [39-41]. …”

Section: Flow-based Enzymatic Sensing Systemsmentioning

confidence: 99%

“…Khayyami et al used Meldola Blue (MB) as electron mediator [39]. Although MB allows working at -0.1 V vs. Ag/AgCl, they applied a working potential of +0.25 V in order to accelerate the oxidation rate.…”

Section: Flow-based Enzymatic Sensing Systemsmentioning

confidence: 99%

Trends in Flow-based Biosensing Systems for Pesticide Assessment

Prieto‐Simón

Campàs

Andreescu

et al. 2006

Sensors

View full text Add to dashboard Cite

This review gives a survey on the state of the art of pesticide detection using flow-based biosensing systems for sample screening. Although immunosensor systems have been proposed as powerful pesticide monitoring tools, this review is mainly focused on enzyme-based biosensors, as they are the most commonly employed when using a flow system. Among the different detection methods able to be integrated into flow-injection analysis (FIA) systems, the electrochemical ones will be treated in more detail, due to their high sensitivity, simple sample pretreatment, easy operational procedures and real-time detection. During the last decade, new trends have been emerging in order to increase the enzyme stability, the sensitivity and selectivity of the measurements, and to lower the detection limits. These approaches are based on (i) the design of novel matrices for enzyme immobilisation, (ii) new manifold configurations of the FIA system, sometimes including miniaturisation or lab-on-chip protocols thanks to micromachining technology, (iii) the use of cholinesterase enzymes either from various commercial sources or genetically modified with the aim of being more sensitive, (iv) the incorporation of other highly specific enzymes, such as organophosphate hydrolase (OPH) or parathion hydrolase (PH) and (v) the combination of different electrochemical methods of detection. This article discusses these novel strategies and their advantages and limitations.

show abstract

“…Carbon nanotubes (CNTs) have emerged as a new class of nanomaterials that are receiving considerable interest owing to their ability to enhance the electrochemical reactivity and promote electron transfer reactions with enzymes [30,31]. Agarose is a kind of natural polysaccharide, and has been widely used for immobilization of enzymes [32], antibodies [33] and chemical molecules [34] due to its attractive properties of excellent film forming ability, high permeability toward water, biocompatibility, non-toxicity, high mechanical strength and cheapness. The striking properties of the CNTs combined with the advantages of agarose essentially suggest a new platform to fabricate the enzyme biosensors.…”

Section: Introductionmentioning

confidence: 99%

Metal chelate affinity to immobilize horseradish peroxidase on functionalized agarose/CNTs composites for the detection of catechol

Luo

et al. 2011

Sci. China Chem.

View full text Add to dashboard Cite

The paper reports a novel amperometric biosensor for catechol based on immobilization of a highly sensitive horseradish peroxidase by affinity interactions on metal chelate-functionalized agarose/carbon nanotubes composites. Metal chelate affinity takes advantage of the affinity of Ni 2+ ions to bind strongly and reversibly to histidine or cysteine tails found on the surface of the horseradish peroxidase. Thus, enzymes with such residues in their molecules can be easily attached to functionalized agarose/carbon nanotubes composites support containing a nickel chelate. Linear sweep voltammograms and amperometry are used to study the proposed electrochemical biosensor. Catechol is determined by direct reduction of biocatalytically liberated quinone species at −0.05 V (vs. SCE). The effect of pH, applied electrode potential and the concentration of H 2 O 2 on the sensitivity of the biosensor has been investigated. The performance of the proposed biosensor is tested using four different phenolic compounds, showing very high sensitivity, in particular, the linearity of catechol is observed from 2.0 × 10 −8 to 1.05 × 10 −5 M with a detection limit of 5.0 × 10 −9 M. amperometric biosensor, carbon nanotubes, metal chelation, agarose, catechol

show abstract

Development of an amperometric biosensor based on acetylcholine esterase covalently bound to a new support material

Cited by 51 publications

References 7 publications

Use of Esterase Activities for the Detection of Chemical Neurotoxic Agents

Use of Esterase Activities for the Detection of Chemical Neurotoxic Agents

Trends in Flow-based Biosensing Systems for Pesticide Assessment

Metal chelate affinity to immobilize horseradish peroxidase on functionalized agarose/CNTs composites for the detection of catechol

Contact Info

Product

Resources

About