Abstract:Abstract-Gold screen-printed electrodes coated with thin films of layered double hydroxides containing cobalt and aluminium (Co 1.57 Al(OH) x SO 4 , shortened as CoAl) have been investigated for the design of an electrochemical tyrosinasebased biosensor used for the detection of a complex mixture of polyphenols extracted from green tea. Physicochemical analyses show that the resulted biosensor exhibits very attractive characteristics: a high sensitivity, a large dynamic range (up to 1000 ng.mL −1 ), and very l… Show more
“…As an extension, the biosensor was used in the detection of polyphenols in tea and wine samples and was compared with the conventional technique (HPLC). In 2017, Soussou et al., reported the determination of tea polyphenols, using Ty enzyme, immobilized over the layered double hydroxide (LDH) hybrid of cobalt and aluminum (designated as CoAl) modified gold SPE (AuSPE) [49]. The CME was designated as AuSPE/CoAl/Ty.…”
Section: Classification Of Different Techniques For the Detection Of mentioning
Tea, contains an abundant amount of polyphenols, has many health benefits, and acts as a remedy for many diseases, including cardiovascular and neurological disorders. In this article, we have reviewed the reported electrochemical techniques for the detection of tea polyphenols under the sub‐headings, separation coupled with electrochemical detection, direct electrochemical detection, bioelectrochemical sensing, simultaneous electrochemical detection and flow injection analysis.
“…As an extension, the biosensor was used in the detection of polyphenols in tea and wine samples and was compared with the conventional technique (HPLC). In 2017, Soussou et al., reported the determination of tea polyphenols, using Ty enzyme, immobilized over the layered double hydroxide (LDH) hybrid of cobalt and aluminum (designated as CoAl) modified gold SPE (AuSPE) [49]. The CME was designated as AuSPE/CoAl/Ty.…”
Section: Classification Of Different Techniques For the Detection Of mentioning
Tea, contains an abundant amount of polyphenols, has many health benefits, and acts as a remedy for many diseases, including cardiovascular and neurological disorders. In this article, we have reviewed the reported electrochemical techniques for the detection of tea polyphenols under the sub‐headings, separation coupled with electrochemical detection, direct electrochemical detection, bioelectrochemical sensing, simultaneous electrochemical detection and flow injection analysis.
“…Layered Double Hydroxide in (bio) Sensing: Layered double hydroxides are nanomaterials with high stability, low toxicity, variable morphological properties and significant adsorption capacity. Due to these characteristics, LDHs were perfect candidates for the immobilization of different molecules and biomolecules as DNA, drugs and enzymes [42]. Furthermore, they can be considerate as promising materials for electrochemical sensors and biosensor design.…”
Section: Layered Double Hydroxides In Biomedicinementioning
confidence: 99%
“…The enzymes are biomolecules with catalytic activity which can be used in different processes due to their high specificity and efficiency [43]. LDHs nanocomposites have proven to be suitable supports for enzyme immobilization, without notable modification of enzyme activity [42]. One of the most important directions of enzyme immobilization on LDHs nanocomposites is their utilization in biosensing.…”
Section: Enzyme-ldhs As Biohybrid In Biosensors Designmentioning
confidence: 99%
“…A robust polyphenols biosensor was designed by covering gold electrodes with LDH, followed by tyrosinase binding to the modified electrodes. The biosensor was used many times with good performances, and it is appropriate to be used in fields where traces need to be detected (medicine, environment) [42]. Horseradish peroxidase (HRP) is an oxidoreductase used in biosensig for H2O2 detection.…”
Section: Enzyme-ldhs As Biohybrid In Biosensors Designmentioning
Layered double hydroxides are known for over 150 years. The first discovered natural mineral with this structure was hydrotalcite [5], reported by Hochstetter in 1842, synthesized 100 years later by Feitknecht [6]. The structure of this compound is related to that of brucite in which part of Mg 2+ cations are replaced by Al3+. Carbonate anions are intercalated between the layers to maintain the electroneutrality of material. The presence of hydrotalcite in nature is reduced. For this reason, the synthesis of LDHs was
“…vn by co-precipitation in the presence of Fe3O4 produces magnetic and porous support for enzyme immobilization. Several enzymes were immobilized on HT and used for biosensor application such as dextranase (Ding et al, 2018), peroxidase Baccar & Hafaiedh, 2011;Hidouri et al, 2021), superoxide−dismutase (Szilágyi et al, 2018), laccase (Camacho Córdova et al, 2009), lactate−dehydrogenase (Djebbi et al, 2016), tyrosinase (Soussou et al, 2017). Starch hydrolytic enzymes such as amylase (Bruna et al, 2015;Sahutoglu & Akgul, 2015), lipase (Dias et al, 2019), glucosidase, and cellulase (Zhang et al, 2020) are attracted by research groups.…”
mHT(Zn) and mHT(Mg) hydrotalcites were fabricated by coprecipitation of Zn 2+ /Al 3+ and Mg 2+ /Al 3+ salt mixtures in the presence of Fe3O4 and used as supports for immobilizing cellulase to form cell@mHT(Zn) and cell@mHT(Mg). The structure and properties of mHT(Zn), mHT(Mg), cell@mHT(Zn), and cell@mHT(Mg) were characterized by Fourier−transform infrared spectroscopy, X-ray diffraction, filtering electron microscopy. The effect of pH, cellulase concentration, and the number of supports on the immobilization of cellulase onto supports were carefully investigated. The enzyme activity of free cellulase, immobilized cellulase, and immobilization efficiency was analyzed by determining reduced glucose using DNS as a color indicator. The highest immobilization efficiency obtained was 94.9 % when carried out on mHT(Zn) at pH 6.5 and 95.3 % on mHT(Mg) and the concentration of cellulase in 0.1mg/mL at the pH of 5.5, using 0.2 g of supports. Cell@mHT(Zn) and cell@mHT(Mg) show high enzyme activity when reacting with 1 % CMC solution at 50 o C with relative enzyme activity of 78.0% and 70.4 %, respectively.
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