Amperometric Tyrosinase Biosensor Based on Carbon Black Paste Electrode for Sensitive Detection of Catechol in Environmental Samples

Wong, Ademar; Santos, Anderson M.; Fatibello‐Filho, Orlando; Sotomayor, Marı́a Del Pilar Taboada

doi:10.1002/elan.202060084

Cited by 13 publications

(4 citation statements)

References 23 publications

(20 reference statements)

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“…Tyrosinase can also be immobilized by various methods on several types of support electrodes (glassy carbon electrode, carbon paste electrode, screen-printed electrode, etc.) [ 76 , 79 , 80 , 81 , 82 , 83 , 84 ], each having advantages and limitations in preparation. For example, in the case of a carbon paste electrode, the enzyme can be incorporated into the paste (which contains a mineral oil) [ 85 ], or it can be immobilized beforehand in the preparation step of the graphite powder [ 45 ].…”

Section: Tyrosinase-based Electrochemical Biosensors—characteristicsmentioning

confidence: 99%

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Tyrosinase Immobilization Strategies for the Development of Electrochemical Biosensors—A Review

Bounegru

Apetrei

2023

Nanomaterials

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The development of enzyme biosensors has successfully overcome various challenges such as enzyme instability, loss of enzyme activity or long response time. In the electroanalytical field, tyrosinase is used to develop biosensors that exploit its ability to catalyze the oxidation of numerous types of phenolic compounds with antioxidant and neurotransmitter roles. This review critically examines the main tyrosinase immobilization techniques for the development of sensitive electrochemical biosensors. Immobilization strategies are mainly classified according to the degree of reversibility/irreversibility of enzyme binding to the support material. Each tyrosinase immobilization method has advantages and limitations, and its selection depends mainly on the type of support electrode, electrode-modifying nanomaterials, cross-linking agent or surfactants used. Tyrosinase immobilization by cross-linking is characterized by very frequent use with outstanding performance of the developed biosensors. Additionally, research in recent years has focused on new immobilization strategies involving cross-linking, such as cross-linked enzyme aggregates (CLEAs) and magnetic cross-linked enzyme aggregates (mCLEAs). Therefore, it can be considered that cross-linking immobilization is the most feasible and economical approach, also providing the possibility of selecting the reagents used and the order of the immobilization steps, which favor the enhancement of biosensor performance characteristics.

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Section: Tyrosinase-based Electrochemical Biosensors—characteristicsmentioning

confidence: 99%

“…However, the main problem with this type of electrode is its low stability. This limitation could be overcome if quasi-solid binders, such as paraffin wax, were used in the preparation of the paste, which could better protect the electrode material [ 83 , 84 , 85 ].…”

Section: Tyrosinase-based Electrochemical Biosensors—characteristicsmentioning

confidence: 99%

Tyrosinase Immobilization Strategies for the Development of Electrochemical Biosensors—A Review

Bounegru

Apetrei

2023

Nanomaterials

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“…Both enzymes are polyphenoloxydases capable of catalyzing the oxidation of the o-diphenol group to o-quinone and are often selected for the electrochemical determination of phenolic compounds [ 21 , 22 ] in different types of samples, food [ 23 , 24 , 25 ], drugs [ 26 , 27 , 28 ], environmental samples [ 29 , 30 , 31 ], etc.…”

Section: Introductionmentioning

confidence: 99%

Studies on the Detection of Oleuropein from Extra Virgin Olive Oils Using Enzymatic Biosensors

Bounegru

Apetrei

2022

IJMS

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Oleuropein (OLEU) is an important indicator of the quality and authenticity of extra virgin olive oils (EVOO). Electrochemical sensors and biosensors for the detection of oleuropein can be used to test the adulteration of extra virgin olive oils. The present study aimed at the qualitative and quantitative determination of oleuropein in commercial EVOO samples by applying electrochemical techniques, cyclic voltammetry (CV) and square wave voltammetry (SWV). The sensing devices used were two newly constructed enzyme biosensors, supported on single-layer carbon-nanotube-modified carbon screen-printed electrode (SPE/SWCNT) on whose surface tyrosinase (SPE/SWCNT/Tyr) and laccase (SPE/SWCNT/Lac) were immobilized, respectively. The active surfaces of the two biosensors were analyzed and characterized by different methods, cyclic voltammetry (CV), electrochemical impedance spectroscopy (EIS) and Fourier transform infrared spectroscopy (FTIR) and the results confirmed the efficient immobilization of the enzymes. SPE/SWCNT/Tyr was characterized by a low detection limit (LOD = 9.53 × 10−8 M) and a very good sensitivity (0.0718 μA·μM−1·cm−2) over a wide linearity range from 0.49 to 11.22 μM. The process occurring at the biosensor surface corresponds to kinetics (h = 0.90), and tyrosinase showed a high affinity towards OLEU. The tyrosinase-based biosensor was shown to have superior sensitive properties to the laccase-based one. Quantitative determination of OLEU in EVOOs was performed using SPE/SWCNT/Tyr and the results confirmed the presence of the compound in close amounts in the EVOOs analysed, proving that they have very good sensory properties.

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“…The immobilization and stability of tyrosinase is one of the most important aspects in the potential success of enzyme-based biosensors [ 16 , 17 ]. To date, the carbon black paste electrode has been positioned as an attractive candidate for enzyme immobilization due to the high surface area of carbon black (CB) and long-term stability of enzyme electrodes in various applications of an electrochemical biosensor [ 18 ].…”

Section: Introductionmentioning

confidence: 99%

The Kinetic and Analytical Aspects of Enzyme Competitive Inhibition: Sensing of Tyrosinase Inhibitors

Attaallah

Amine

2021

Biosensors

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An amperometric biosensor based on tyrosinase, immobilized onto a carbon black paste electrode using glutaraldehyde and BSA was constructed to detect competitive inhibitors. Three inhibitors were used in this study: benzoic acid, sodium azide, and kojic acid, and the obtained values for fifty percent of inhibition (IC50) were 119 µM, 1480 µM, and 30 µM, respectively. The type of inhibition can also be determined from the curve of the degree of inhibition by considering the shift of the inhibition curves. Amperometric experiments were performed with a biosensor polarized at the potential −0.15 V vs. Ag/AgCl and using 0.1 M phosphate buffer (pH 6.8) as an electrolyte. Under optimized conditions, the proposed biosensor showed a linear amperometric response toward catechol detection from 0.5 µM to 38 µM with a detection limit of 0.35 µM (S/N = 3), and its sensitivity was 66.5 mA M−1 cm−2. Moreover, the biosensor exhibited a good storage stability. Conversely, a novel graphical plot for the determination of reversible competitive inhibition was represented for free tyrosinase. The graph consisted of plotting the half-time reaction (t1/2) as a function of the inhibitor concentration at various substrate concentrations. This innovative method relevance was demonstrated in the case of kojic acid using a colorimetric bioassay relying on tyrosinase inhibition. The results showed that the t1/2 provides an extended linear range of tyrosinase inhibitors.

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Amperometric Tyrosinase Biosensor Based on Carbon Black Paste Electrode for Sensitive Detection of Catechol in Environmental Samples

Cited by 13 publications

References 23 publications

Tyrosinase Immobilization Strategies for the Development of Electrochemical Biosensors—A Review

Tyrosinase Immobilization Strategies for the Development of Electrochemical Biosensors—A Review

Studies on the Detection of Oleuropein from Extra Virgin Olive Oils Using Enzymatic Biosensors

The Kinetic and Analytical Aspects of Enzyme Competitive Inhibition: Sensing of Tyrosinase Inhibitors

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