Amperometric biosensor based on a high resolution photopolymer deposited onto a screen-printed electrode for phenolic compounds monitoring in tea infusions

Ibarra-Escutia, Pedro; Gómez, Jorge; Calas‐Blanchard, Carole; Marty, Jean Louis; Ramı́rez-Silva, Maria Teresa

doi:10.1016/j.talanta.2010.03.017

Cited by 91 publications

(58 citation statements)

References 69 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Recent advances in this field are related to the development of new support matrix as suitable platforms (most of them including nanomaterials) for enzymes immobilization, which lead to biosensors with improved analytical properties. So, in recent works, laccase has been immobilized by direct adsorption, covalent binding or entrapment onto: epoxy resin membranes [9], mesoporous materials with well-controlled pore structures [10,17], multi-walled carbon nanotubes paste electrodes [18], nanocomposites formed by chitosan and carbon nanotubes [19], copper-containing ordered mesoporous carbon chitosan matrix [8], pyrenehexanoic acid-modified hierarchical carbon microfibers/carbon nanotubes composite electrodes [16], polyvinyl alcohol photopolymers [20], sol-gel matrix of 5 diglycerylsilane [21], 3-mercaptopropionic acid self-assembled monolayer modified gold electrodes [22], cysteine self-assembled monolayer and quantum dots modified gold electrodes [23], nanocomposites of silver nanoparticles and zinc oxide nanoparticles electrochemically deposited onto gold electrodes [24], platinum nanoparticles and reduced graphene composites deposited onto screen printed electrodes [25], polyethyleneimine coated gold-nanoparticles modified glassy carbon electrodes…”

Section: Introductionmentioning

confidence: 99%

Laccase biosensors based on different enzyme immobilization strategies for phenolic compounds determination

Casero

Petit‐Domínguez

Vázquez

et al. 2013

Talanta

View full text Add to dashboard Cite

Different enzyme immobilization approaches of Trametes versicolor laccase (TvL)onto gold surfaces and their influence on the performance of the final bioanalytical platforms are described. The laccase immobilization methods include: i) direct adsorption onto gold electrodes (TvL/Au), ii) covalent attachment to a gold surface modified with a bifunctional reagent, 3,3'-Dithiodipropionic acid di (N-succinimidyl ester) (DTSP), and iii) integration of the enzyme into a sol-gel 3D polymeric network derived from (3-mercaptopropyl)-trimethoxysilane (MPTS) previously formed onto a gold surface (TvL/MPTS/Au). The characterization and applicability of these biosensors are described. Characterization is performed in aqueous acetate buffer solutions using atomic force microscopy (AFM), providing valuable information concerning morphological data at the nanoscale level.The response of the three biosensing platforms developed, TvL/Au, TvL/DTSP/Au and TvL/MPTS/Au, is evaluated in the presence of hydroquinone (HQ), used as a phenolic enzymatic substrate. All systems exhibit a clear electrocatalytic activity and HQ can be amperometrically determined at -0.10 V versus Ag/AgCl. However, the performance of biosensors -evaluated in terms of sensitivity, detection limit, linear 2 response range, reproducibility and stability-depends clearly on the enzyme immobilization strategy, which allows establishing its influence on the enzyme catalytic activity.

show abstract

Section: Introductionmentioning

confidence: 99%

Laccase biosensors based on different enzyme immobilization strategies for phenolic compounds determination

Casero

Petit‐Domínguez

Vázquez

et al. 2013

Talanta

View full text Add to dashboard Cite

show abstract

“…All tests were carried out at ambient temperature in 1 cm optical path quartz cells in an acetate bu er (0.1 M pH 4.5). e experimental conditions were chosen based on studies reported by our working group [22,23].…”

Section: Kinetic Analyses and Enzymatic Inhibitionmentioning

confidence: 99%

Laccase Inhibition by Mercury: Kinetics, Inhibition Mechanism, and Preliminary Application in the Spectrophotometric Quantification of Mercury Ions

Juárez-Gómez

Rosas-Tate

Roa‐Morales

et al. 2018

Journal of Chemistry

View full text Add to dashboard Cite

e noncompetitive inhibition of laccase by mercury ions is reported, in particular focusing their effect over the enzyme catalytic activity. e enzymatic kinetics were obtained for different substrates (caffeic acid, gallic acid, and catechol), where caffeic acid displayed the greatest enzymatic activity. e laccase inhibition by mercury ions permitted to establish the inhibition effect through a mixed model (that actually displayed a behavior closer to that of the noncompetitive inhibitors) when evaluated by means of UV-Vis spectrophotometry, using caffeic acid as an electron donor. A mercury concentration of 2 mM led to 35% enzymatic inhibition after only a 2-minute incubation period. is method was used for quantification of mercury ions in aqueous solution, showing a detection limit of 15 ± 1 ppm. erefore, this work presented a novel perspective for the determination of the toxic Hg(II) ions that can be readily implemented into environmental remediation methods.

show abstract

“…The efficiency of the constructed SPEs was confirmed by Fusco et al by using them successfully for phenolic analysis. [21][22][23] Electrodeposition is another simple method to immobilize an enzyme onto an electrode surface. The detection of phenol using SPEs modified with MWCNTs without their entrapment in a polymeric film or any other matrix was achieved through the electrodeposition of PPO with the addition of a Bi 3+ precursor onto the electrode.…”

Section: Electrochemical Detection Of Polyphenolsmentioning

confidence: 99%

Electrochemical Sensors in Environmental Analysis

Cristea

Feier

Săndulescu

2014

Environmental Analysis by Electrochemical Sensors and Biosensors

View full text Add to dashboard Cite

Amperometric biosensor based on a high resolution photopolymer deposited onto a screen-printed electrode for phenolic compounds monitoring in tea infusions

Cited by 91 publications

References 69 publications

Laccase biosensors based on different enzyme immobilization strategies for phenolic compounds determination

Laccase biosensors based on different enzyme immobilization strategies for phenolic compounds determination

Laccase Inhibition by Mercury: Kinetics, Inhibition Mechanism, and Preliminary Application in the Spectrophotometric Quantification of Mercury Ions

Electrochemical Sensors in Environmental Analysis

Contact Info

Product

Resources

About