Catalase Biosensor Research Articles

Fabrication and characterization of a Layered Double Hydroxide based catalase biosensor and a catalytic sensor for hydrogen peroxide determination

An enzyme catalase biosensor was fabricated to determine hydrogen peroxide. The enzyme was cross-linked with [ZnIIAlIII (OH)2]+ NO3– Layered Double Hydroxide (LDH), which was glued on a glassy carbon (GC) electrode. The amperometric response to hydrogen peroxide was studied. A limit of detection (LOD) of about 0.20 mM and a good lifetime as high as 75 days were observed. A sensor with the same configuration, without the immobilized catalase enzyme and with LDH glued on (GC), was also realized. This non-enzymatic sensor also showed catalytic activity towards H2O2, exhibiting an amperometric response obviously much lower than that of the enzyme biosensor, with a LOD of about 1.0 mM. However, also the lifetime of this catalytic sensor was longer than 2 months after preparation.

Catalase biosensor based on the PAni/cMWCNT support for peroxide sensing

Abstract Polymeric-based composites can contribute to enhancing the detection, stability, and performance of enzymatic biosensors, due to their high structural stability, conductivity, and biocompatibility. This work presents the fabrication of a nanocomposite of polyaniline (PAni)/gold nanoparticles (AuNP)/carboxylated multiwalled carbon nanotubes (cMWCNT) as functional support for covalently linked catalase (CAT) enzyme. PAni was electropolymerized on a screen-printed carbon electrode (SPCE) and decorated with AuNP to improve charge transfer properties. CAT was bonded through amide formation using the carboxylic groups of cMWCNT, resulting in PAni/AuNP/cMWCNT/CAT biosensor. The structural and electroactive characteristics of the nanocomposite were studied by SEM, FT-IR, and cyclic voltammetry. The optimal performance was achieved after CAT immobilization over PAni/AuNP/cMWCNT/nanocomposite, showing improved analytical features such as a fast amperometric response of 1.28 s, a wide detection range from 0.01 to 6.8 mM, a correlation coefficient (R 2) of 0.9921, a low detection limit of 2.34 µM, and an average recovery rate of 99.6% when evaluated in milk samples. Additionally, the bioelectrode showed excellent selectivity and retained bioactivity after 30 days of storage. Such remarkable performance proved the synergistic effects of both the high surface area of the cMWCNT and AuNP and the inherent PAni electroactivity, yielding direct electron transfer from CAT.

Direct Methanol Catalytic Fuel Cell, for Measuring Ethanol Contents in Pharmaceutical Tinctures

Background: In order to test real direct applicability for analytical purposes, a small and simple direct methanol (or ethanol) catalytic, enzymatic or non-enzymatic fuel cell (DMFC) was used for the analysis of ethanol-based pharmaceutical tinctures; a detailed experimental study was conducted on five different pharmaceutical tinctures available at drugstores. Results: The results obtained using both enzymatic and non-enzymatic devices were compared with those obtained by analyzing the same pharmaceutical samples with a conventional catalase biosensor. Finally, the results were compared with the nominal values provided by manufacturing firms. Conclusion: The correlations between the different experimental and nominal values considered were good in general or satisfactory and the applied statistical tests (f-test and t-test) were also very comforting. At the end of the study, the use of enzymatic DMFC proved to be better than non- enzymatic DMFC devices, because it requires shorter analysis times.

Hidrogen peroksidinin analizi üçün sensorlar

The physico-chemical properties of new type catalase sensors, the so-called biomimetic sensors modulating some of catalase biosensor functions were investigated. These sensors have technological advantages ever their biological analogs due to the properties usually attributed to chemical sensors. The development electrochemical system stands in between bio- and chemical sensors.

Inhibition of 2,4-Dichlorophenoxyacetic Acid to Catalase Immobilized on Hierarchical Porous Calcium Phosphate: Kinetic Aspect and Electrochemical Biosensor Construction

The inhibition mechanism of 2,4-dichlorophenoxyacetic acid (2,4-D) to catalase was studied by a catalase biosensor in a flow-injection analysis (FIA) system. This system provides an ideal sensing platform to electrochemically evaluate the chemical mechanism of enzyme inhibition. Hierarchical porous calcium phosphate (hp-CaP), as a biocompatible nanomaterial, was used to immobilize catalase for repeat use. 2,4-D together with H2O2 was injected into the bioreactor of the immobilized catalase-FIA system during the experimental procedure. The activity of the immobilized catalase was inhibited, which caused a decrease of the catalase-catalyzed H2O2 reduction current. Lineweaver–Burk, Dixon, and Cornish–Bowden plots confirmed that the inhibition of catalase by 2,4-D followed an competitive mechanism with a inhibition constant of 4.78 × 10–7 M. Based on this inhibition characters, a biosensor for 2,4-D detection was constructed. This biosensor showed a linear range from 0.03 to 3.00 μM with a detection limit of ...

Forchlorfenuron detection based on its inhibitory effect towards catalase immobilized on boron nitride substrate

An enzymatic procedure based on a catalase biosensor for the detection of forchlorfenuron (CPPU) has been reported in this work. Catalase was immobilized on boron nitride (BN) sheets dispersed in chitosan by adsorption. The immobilized catalase exhibited direct electron transfer character and excellent electrocatalytic activity towards H2O2 reduction. After introducing CPPU into the H2O2 containing phosphate buffer solution, the catalase-catalyzed H2O2 reduction current decreased. By measuring the current decrease, CPPU can be determined in the range of 0.5–10.0µM with the detection limit of 0.07μM. The non-competitive inhibition behavior of CPPU towards catalase was verified by the Lineweaver–Burk plots. Long stability character has been ascribed to this biosensor. Possible use of this biosensor in flow systems is illustrated. The proposed biosensor has been successfully applied to CPPU determination in fruits samples with satisfactory results.

Polyaniline based catalase biosensor for the detection of hydrogen peroxide and azide

The CAT/PANi/ITO bioelectrode has been prepared as a catalase biosensor and shows response for monitoring not only of H2O2 but also azide. The sensor exhibited an excellent response to the H2O2 and azide. The linear range of H2O2 was 0.064∼1 mM and for azide 0.125∼4 mM, respectively. Catalase biosensor was based on the principle of the measurements as the decrease in the differentiation of oxygen level, which has been caused by the inhibition of catalase in the bioactive layer of the biosensor by azide. The repeatability experiments were done in triplicate. The logarithm response of the biosensor to H2O2 (r2 = 0.99), as well as, for azide (r2 = 0.90) were reported, respectively. The bioelectrode was characterized by CV and AFM. The proposed biosensor would be applied for the determination of H2O2 and azide in various biological samples.

Activation‐Based Catalase Enzyme Electrode and its Usage for Glucose Determination

In this study, a novel type amperometric biosensor, which is based on the activation of catalase enzyme by glucose, was developed and used for the sensitive determination of glucose. For the preparation of the biosensor catalase enzyme was immobilized in gelatin by using cross‐linking agent glutaraldehyde and fixed on a pretreated teflon membrane of a dissolved oxygen probe. Glucose was used as an activator for the catalase enzyme and determination of glucose is based on the assay of the differences on the catalase activity of the biosensor on the oxygenmeter in the absence and the presence of glucose in the reaction medium. The responses of the activation based catalase biosensor have a linear relation to glucose concentrations and good measurement correlation between 0.5 and 5.0 µM with 2 min response time. In the optimization studies of the biosensor the most suitable catalase amount were found as 1324 U cm−2 and also phosphate buffer (pH: 7.0; 50 mM) and 35°C were obtained as the optimum working conditions. For the characterization studies of the biosensor some parameters such as activator and interference effects of some substances on the biosensor response, reproducibility and operational stability were performed.

Catalase Immobilization in Cellulose Acetate Beads and Determination of its Hydrogen Peroxide Decomposition Level by using a Catalase Biosensor

Catalase enzyme (EC 1.11.1.6) was immobilized by entrapping in cellulose acetate beads. This organic matrix is highly resistant to mechanical stability and can be used under various conditions. Initial studies were conducted to examine the immobilization ability of catalase on the matrix previously activated with a series of reagent normally and the best results were obtained with the beads activated with Ce(SO4)2. In the optimization studies of the immobilized enzyme optimum pH and temperature were found as pH:7.0 (Tris-HCl, 50 mM) and 35 degrees C. In the characterization studies of the immobilized enzyme some parameters such as storage and thermal stability were investigated. Finally, the immobilized enzyme was used for the decomposition of hydrogen peroxide in milk samples and also by using a catalase biosensor prepared the decomposition level of hydrogen peroxide was detected.

Catalase Immobilization in Cellulose Acetate Beads and Determination of its Hydrogen Peroxide Decomposition Level by using a Catalase Biosensor

Catalase enzyme (EC 1.11.1.6) was immobilized by entrapping in cellulose acetate beads. This organic matrix is highly resistant to mechanical stability and can be used under various conditions. Initial studies were conducted to examine the immobilization ability of catalase on the matrix previously activated with a series of reagent normally and the best results were obtained with the beads activated with Ce(SO4)2. In the optimization studies of the immobilized enzyme optimum pH and temperature were found as pH:7.0 (Tris–HCl, 50 mM) and 35°C. In the characterization studies of the immobilized enzyme some parameters such as storage and thermal stability were investigated. Finally, the immobilized enzyme was used for the decomposition of hydrogen peroxide in milk samples and also by using a catalase biosensor prepared the decomposition level of hydrogen peroxide was detected.

Immobilization of Catalase by Entrapping in Alginate Beads and Catalase Biosensor Preparation for the Determination of Hydrogen Peroxide Decomposition

In this study, catalase enzyme was immobilized by entrapping in alginate beads in the presence of gelatin. In the optimization studies of the bioactive layer immobilized some parameters such as enzyme amount, alginate, gelatin, and crosslinking agent glutaraldehyde amount were determined as 700 U/mL, 2.0%, 18 mg/mL, and 5.0%, respectively. Effects of pH and temperature on the immobilization were also investigated. In the characterization studies of the immobilized enzyme storage and thermal stability experiments were done. The immobilized enzyme was used for the decomposition of hydrogen peroxide in milk samples and also by using a catalase biosensor prepared by the decomposition level of hydrogen peroxide was detected.

Immobilization of Catalase by Entrapping in Alginate Beads and Catalase Biosensor Preparation for the Determination of Hydrogen Peroxide Decomposition

Immobilization of Catalase by Entrapping in Alginate Beads and Catalase Biosensor Preparation for the Determination of Hydrogen Peroxide Decomposition

Hydroperoxide determination by a catalase OPEE: application to the study of extra virgin olive oil rancidification process

A new application to authentic matrices of a catalase organic phase enzyme electrode (OPEE) recently developed by the present authors is described in this communication. This biosensor was obtained by coupling an amperometric gas diffusion electrode for the oxygen, made of teflon, and the catalase enzyme immobilised in kappa-carrageenan gel. The response of the catalase biosensor to cumene hydroperoxide and to terbutylhydroperoxide, working directly in n-decane or toluene, was studied. The hydroperoxide content of the extra virgin olive oil was monitored during an artificial rancidification process. One interesting result obtained is the qualitative correlation observed between the above trend of the hydroperoxide content pool and that of the peroxide number; moreover, a qualitative inverse correlation trend was found between both the last two indicators and the content of polyphenols in the olive oil which are known to be the most important natural antioxidant agents contained in olive oil.

An Attempt to Create Stable Biomimetic Sensors for Express Analysis of Hydrogen Peroxide in Water Solutions

The physico-chemical properties of a new type catalase sensor, the so-called biomimetic sensors, modulating some of the catalase biosensor functions were investigated. These sensors have technological advantages over their biological analogs because of properties usually attributed to chemical sensors. The developed electrochemical system lies between bio- and chemical sensors.

Hydrogen peroxide determination in pharmaceutical formulations and cosmetics using a new catalase biosensor

The possibility of evaluating the content of hydrogen peroxide in several authentic matrices, such as cosmetic and pharmaceutical formulations, was studied. A new catalase biosensor fabricated using an amperometric gas-diffusion oxygen sensor as electrochemical transducer and the catalase enzyme immobilized in kappa-carrageenan gel and capable of operating in both aqueous and non aqueous solvents was developed and tested for this purpose. Creams, emulsions and disinfectant solutions were analysed. To this end, a preliminary check was needed to establish the best conditions to analyse these matrices; the choice of solvent was one of the most important points studied. The solvents considered included dioxane, water-dioxane mixtures, water saturated chloroform and aqueous solutions. The different solubility properties of the matrices analysed were taken into account.

Catalase biosensor for the determination of hydrogen peroxide, fluoride and cyanide

The enzyme catalase, which catalyses the decomposition of hydrogen peroxide to oxygen and water, was immobilized in a membrane by entrapping it in polyacryl amide and contacted to a Clark-type oxygen electrode. With the resulting catalase biosensor it was possible to detect the substrate hydrogen peroxide and the inhibitors fluoride and cyanide in phosphate buffer.

Microelectrochemical cell containing chloroplast membranes as a fast bioassay for catalase determination

A three-electrode photoelectrochemical cell has been found to be an excellent catalase biosensor. The cell contains a sample of easily prepared photosynthetic membranes and produces via the electrochemical degradation of hydrogen peroxide at its working electrode. The cell is shown in this report to be very sensitive to the enzymatic action of catalase, even in small quantities, and is capable of providing a rough estimate of the amount of contaminating catalase present in a sample. Furthermore, individual assays are fast (≈ 5 min), allowing a large number of replicates to be performed quickly.