A sustainable amperometric biosensor for the analysis of ascorbic, benzoic, gallic and kojic acids through catechol detection. Innovation and signal processing

Casanova, Ana; Cuartero, María; Alacid, Yolanda; Almagro, Carmen M.; Garcı́a-Cánovas, Francisco; García, María I. Rodríguez; Ortuño, J

doi:10.1039/c9an02523e

Cited by 10 publications

(12 citation statements)

References 38 publications

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“…Indeed, by increasing the substrate concentration from 20 µM to 200 µM, the inhibition curve shifted to the right and the IC 50 increased from 30 µM to 58 µM, demonstrating that tyrosinase inhibition by kojic acid is a competitive inhibition. This was also confirmed by other previous work in the literature [ 10 , 45 ]. We previously reported [ 27 ] that the degree of inhibition is equal to [I]/([I] + [IC 50 ]), which means a hyperbolic relationship exists between the degree of inhibition and concentration of an inhibitor.…”

Section: Resultssupporting

confidence: 93%

“…As indicated in Figure 5, increasing the substrate concentration causes parallel lines with a high intercept and unvaried slope. These results confirm the competitive inhibition of tyrosinase by kojic acid and are in agreement with the previous literature [10,45] and with the above As well as the analytical aspects, the diagnosis of the inhibition type can be ascertained from the plot t' 1/2 versus inhibitor concentrations. The substrate concentration will be varied to determine its effect on the half-time reaction, and after this change, we can directly determine the type of inhibition.…”

Section: Kinetic Study and Analytical Aspects Of Free Tyrosinasesupporting

confidence: 92%

“…The enzymatic biosensors were widely used because of their ability to detect a target substance/analyte with a high specificity through enzyme-catalyzed reactions [5][6][7]. The detection of phenolic [8,9] and other compounds that can be used as a food preservative, and can be hazardous to human health at levels greater than authorized safety standards, such as benzoic acid, sodium azide and kojic acid [10], is of great interest for both quality assurance and consumer protection [11]. Tyrosinase-based amperometric biosensors have been extensively reported in the literature for the detection of various compounds (particularly mono-and di-phenols) due to their rapid response, low cost and low energy consumption [12][13][14].…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Resultssupporting

confidence: 93%

Section: Kinetic Study and Analytical Aspects Of Free Tyrosinasesupporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

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

Attaallah

Amine

2021

Biosensors

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“…Film fabrication Tyrosinase Catalysis of gelatin-chitosan conjugation for use as scaffold for tissue engineering. [155,178] Building materials…”

Section: Tyrosinasementioning

confidence: 99%

Enzyme‐catalysed polymer cross‐linking: Biocatalytic tools for chemical biology, materials science and beyond

et al. 2020

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Intermolecular cross-linking is one of the most important techniques that can be used to fundamentally alter the material properties of a polymer. The introduction of covalent bonds between individual polymer chains creates 3D macromolecular assemblies with enhanced mechanical properties and greater chemical or thermal tolerances. In contrast to many chemical cross-linking reactions, which are the basis of thermoset plastics, enzyme catalysed processes offer a complimentary paradigm for the assembly of cross-linked polymer networks through their predictability and high levels of control. Additionally, enzyme catalysed reactions offer an inherently 'greener' and more biocompatible approach to covalent bond formation, which could include the use of aqueous solvents, ambient temperatures, and heavy metal-free reagents. Here, we review recent progress in the development of biocatalytic methods for polymer cross-linking, with a specific focus on the most promising candidate enzyme classes and their underlying catalytic mechanisms. We also provide exemplars of the use of enzyme catalysed cross-linking reactions in industrially relevant applications, noting the limitations of these approaches and outlining strategies to mitigate reported deficiencies.

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“…Benzoic acid, which is commonly used as a preservative for food and pharmaceutical products has been reported to be a reversible tyrosinase inhibitor (Casanova et al, 2020;Kochana et al, 2012;Li et al, 2010;López et al, 2011;Shan et al, 2008). In this context, the analytical characteristics of the catechol capsule-based tyrosinase biosensor and its performance towards the detection of benzoic acid as an inhibitor are therefore described.…”

Section: Introductionmentioning

confidence: 99%

Microcapsule-based biosensor containing catechol for the reagent-free inhibitive detection of benzoic acid by tyrosinase

Nédellec

Gondran

Gorgy

et al. 2021

Biosensors and Bioelectronics

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A sustainable amperometric biosensor for the analysis of ascorbic, benzoic, gallic and kojic acids through catechol detection. Innovation and signal processing

Abstract: A sustainable catechol biosensor for the analysis of beverages and cosmetics.

Cited by 10 publications

References 38 publications

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

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

Enzyme‐catalysed polymer cross‐linking: Biocatalytic tools for chemical biology, materials science and beyond

Microcapsule-based biosensor containing catechol for the reagent-free inhibitive detection of benzoic acid by tyrosinase

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