A disposable Laccase–Tyrosinase based biosensor for amperometric detection of phenolic compounds in must and wine

Montereali, Maria Rita; Seta, L. Della; Vastarella, W.; Pilloton, Roberto

doi:10.1016/j.molcatb.2009.07.014

Cited by 106 publications

(62 citation statements)

References 23 publications

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“…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

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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.

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Section: Introductionmentioning

confidence: 99%

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

Casero

Petit‐Domínguez

Vázquez

et al. 2013

Talanta

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“…The electrode containing both PPO and LAC immobilized in unmodified MMT gave a response 48.7 % greater than biosensor-LAC (b) and 56.9 % higher than biosensor-PPO (c), when employed under the same working conditions used for the mono-enzymatic electrodes. The results obtained can be attributed to the synergistic effect of the combined system of two enzymes, which is better than using each enzyme separately [46,47]. The bi-enzymatic biosensor containing PPO-LAC immobilized in the Ir-BMI.BF 4 -MMT matrix showed a response 38.5 % greater than the bi-enzymatic electrode with unmodified MMT (d).…”

Section: Voltammetric Behavior Of Rutin In the Biosensorsmentioning

confidence: 98%

“…The synergistic effect of combining two biocatalysts is a major advantage in the construction of bi-enzymatic biosensors, because the response with the application of two enzymes in the same electrode is additive [46]. PPO and LAC are oxidoreductases, and both of these enzymes catalyze the oxidation of phenol compounds to the corresponding quinone in the presence molecular oxygen [25].…”

Section: Principle Of the Bi-enzymatic Process Occurring On The Biosementioning

confidence: 99%

Bioelectroanalytical Determination of Rutin Based on bi‐Enzymatic Sensor Containing Iridium Nanoparticles in Ionic Liquid Phase Supported in Clay

et al. 2010

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A matrix comprising iridium nanoparticles and 1-butyl-3-methylimidazolium tetrafluoroborate ionic liquid (Ir-BMI.BF 4 ) supported in montmorillonite (MMT) was obtained through an efficient incorporation process. This modified clay matrix (Ir-BMI.BF 4 -MMT) was used for the immobilization of the enzymes laccase (LAC) and polyphenol oxidase (PPO) and employed in the construction of a bi-enzymatic biosensor for determination of rutin by square-wave voltammetry. Under optimized conditions, the analytical curve showed a linear range for rutin concentrations from 9.17 10 À8 to 3.10 10 À6 mol L À1 with a detection limit of 3.09 10 À8 mol L À1. The method was successfully applied to the determination of rutin content in pharmaceutical samples.

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“…14 Cross-sensitivity to selected phenolic compounds shown by phenol-degrading enzymes used in biosensors alone or associated in pair. Adapted from data in [52] 4-methylcatechol, 3-chlorophenol and catechol, with relative responses between the 12.7% for 4-tertbutylcatechol and 100% (max) for catechol [53]. Polyphenols are a group of naturally occurring compounds that can be found in fruits and vegetables or beverages like tea or wine.…”

Section: Coupling Different Enzymes In the Same Sensing Devicementioning

confidence: 99%

Bioelectronic Tongues Employing Electrochemical Biosensors

Valle

2016

Bioanalytical Reviews

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This chapter presents recent advances concerning work with electronic tongues that employ electrochemical biosensors, that is, bioelectronic tongues. (Bio)electronic tongues represent a new methodological use of (bio)sensors; they start by the use of biosensor arrays and assume the coupling of the obtained complex response with advanced chemometric data treatment; the goal is improving performance of existing sensors. Most of the bioelectronic tongues reported employ enzyme biosensors, essentially based on potentiometric or voltammetric/ amperometric transduction. This report is organized considering the different forms to incorporate biosensors, i.e. considering the number of biosensors in the array, the number of different enzymes used, if the determination is aimed to substrates or inhibitors, etc. Significant applications in real problem-solving, mainly in the food and clinical or environmental fields, are commented.

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A disposable Laccase–Tyrosinase based biosensor for amperometric detection of phenolic compounds in must and wine

Cited by 106 publications

References 23 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

Bioelectroanalytical Determination of Rutin Based on bi‐Enzymatic Sensor Containing Iridium Nanoparticles in Ionic Liquid Phase Supported in Clay

Bioelectronic Tongues Employing Electrochemical Biosensors

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