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Entrapment of glucose oxidase within gold converts it to a general monosaccharide-oxidase.

ABSTRACT: We report that entrapping glucose oxidase (GOx) within metallic gold, expands its activity to become an oxidase for monosaccharides that do not have a natural enzyme with that activity-fructose and xylose-and that this entrapment also removes the enantioselectivity, rendering this enzyme capable of oxidizing the "wrong" L-enantiomer of glucose. These observations suggest that in this biomaterial adsorptive interactions of the outer regions of the protein with the gold cage, pull apart and widen the tunnel between the two monomeric units of GOx, to a degree that its stereoselectivity is compromised; then, the active sites which are more versatile than currently attributed to, are free and capable of acting on the foreign sugars. To test this proposition, we entrapped in gold L-asparaginase, which is also a dimeric enzyme (a dimer of tight dimers), and found, again, that this metallic biomaterial widens the activity of that enzyme, to include the D-amino acid counter enantiomer as well. Detailed kinetic analyses for all substrates are provided for the gold bio-composites, including determination of the difference between the activation energies towards two opposite enantiomers.

SUBMITTER: Baruch-Shpigler Y

PROVIDER: S-EPMC8144553 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Glucose oxidase converted into a general sugar-oxidase.

Project description:Entrapment of glucose oxidase (GOx) within metallic gold converts this widely used enzyme into a general saccharide oxidase. The following sugar molecules were oxidized by the entrapped enzyme (in addition to D-glucose): fructose, xylose, L-glucose, glucose-6-phosphate, sucrose, lactose, methylglucoside, and the tri-saccharide raffinose. With the exception of raffinose, none of these sugars have a natural specific oxidase. The origin of this generalization of activity is attributed to the strong protein-gold 3D interactions and to the strong interactions of the co-entrapped CTAB with both the gold, and the protein. It is proposed that these interactions induce conformational changes in the channel leading to the active site, which is located at the interface between the two units of the dimeric GOx protein. The observations are compatible with affecting the specific conformation change of pulling apart and opening this gate-keeper, rendering the active site accessible to a variety of substrates. The entrapment methodology was also found to increase the thermal stability of GOx up to 100 °C and to allow its convenient reuse, two features of practical importance.

| S-EPMC9226012 | biostudies-literature

Thermal stabilization of glucose oxidase and glucoamylase by physical entrapment.

Project description:Physical entrapment was used as an approach to achieve thermal stabilization of enzymes. The t 1/2 values for the thermoinactivation of glucose oxidase and glucoamylase were increased several-fold by their entrapment in polyacrylamide gels. In polyacrylate gels the individual enzymes behaved differently, probably owing to microenvironmental effects arising by the polyelectrolyte nature of the carrier.

| S-EPMC1162617 | biostudies-other

The Impact of Glucose Oxidase Immobilization on Dendritic Gold Nanostructures on the Performance of Glucose Biosensors.

Project description:In recent years, many efforts have been made to develop rapid, sensitive and user-friendly glucose biosensors for monitoring blood glucose concentration in patients. In this study, the electrochemical glucose biosensors based on graphite rod (GR) electrode electrochemically modified with dendritic gold nanostructures (DGNs) and glucose oxidase (GOx) were developed. Phenazine methosulfate was used as a soluble redox mediator. Three GOx immobilization methods: adsorption on DGNs and cross-linking with glutaraldehyde (GA) vapour (GA-GOx/DGNs/GR), covalent immobilization on DGNs modified with 11-mercaptoundecanoic acid self-assembled monolayer (SAM) (GOx-SAM/DGNs/GR) and covalent immobilization on SAM with additional cross-linking with GA vapour (GA-GOx-SAM/DGNs/GR), were used. It was determined that GA significantly improved the stability of the enzyme layer. The difference of maximal current generated during the enzymatic reaction (ΔImax) equal to 272.06 ± 8.69 µA was obtained using a biosensor based on GA-GOx/DGNs/GR electrodes. However, the highest ΔImax equal to 384.20 ± 16.06 µA was obtained using GA-GOx-SAM/DGNs/GR electrode. ΔImax for biosensors based on the GA-GOx-SAM/DGNs/GR electrode was 1.41 times higher than for the GA-GOx/DGNs/GR, whereas the linear dynamic range from 0.1 to 10 mM was the same using all three GOx immobilization methods. The limit of detection using GA-GOx-SAM/DGNs/GR and GA-GOx/DGNs/GR electrodes was 0.019 and 0.022 mM, respectively. The ability to detect glucose in the serum by developed biosensors was evaluated.

| S-EPMC9139151 | biostudies-literature

The Development of Reagentless Amperometric Glucose Biosensor Based on Gold Nanostructures, Prussian Blue and Glucose Oxidase.

Project description:Precise blood glucose detection plays a crucial role in diagnosing and medicating diabetes, in addition to aiding diabetic patients in effectively managing their condition. In this research, a first-generation reagentless amperometric glucose biosensor was developed by combining the graphite rod (GR) electrode modification by gold nanostructures (AuNS) and Prussian blue (PB) with glucose oxidase (GOx)-an enzyme that can oxidize glucose and produce H2O2. Firstly, AuNS was electrochemically deposited on the GR electrode (AuNS/GR), and then PB was electrochemically synthesized on the AuNS/GR electrode (PB/AuNS/GR). Finally, GOx was immobilized over the PB/AuNS nanocomposite with the assistance of Nafion (Nf) (Nf-GOx/PB/AuNS/GR). An application of PB in the design of a glucose biosensor enables an easy electrochemical reduction and, thus, the determination of the H2O2 produced during the GOx-catalyzed oxidation of glucose in the sample at a low operation potential of -0.05 V vs. Ag/AgCl/KCl3 mol L-1. In addition, AuNS increased the electrochemically active surface area, improved the GOx immobilization and ensured a higher analytical signal. The developed glucose biosensor based on the Nf-GOx/PB/AuNS/GR electrode exhibited a wide linear range, from 0.025 to 1 mmol L-1 of glucose, with a 0.0088 mmol L-1 limit of detection, good repeatability and high selectivity over electroactive interfering substances. The developed biosensor is convenient for the determination of glucose in the physiological environment.

| S-EPMC10605372 | biostudies-literature

On-Chip Glucose Detection Based on Glucose Oxidase Immobilized on a Platinum-Modified, Gold Microband Electrode.

Project description:We report the microfabrication and characterization of gold microband electrodes on silicon using standard microfabrication methods, i.e., lithography and etching techniques. A two-step electrodeposition process was carried out using the on-chip platinum reference and gold counter electrodes, thus incorporating glucose oxidase onto a platinum-modified, gold microband electrode with an o-phenylenediamine and ß-cyclodextrin mixture. The as-fabricated electrodes were studied using optical microscopy, scanning electron microscopy, and atomic force microscopy. The two-step electrodeposition process was conducted in low sample volumes (50 µL) of both solutions required for biosensor construction. Cyclic voltammetry and electrochemical impedance spectroscopy were utilised for electrochemical characterization at each stage of the deposition process. The enzymatic-based microband biosensor demonstrated a linear response to glucose from 2.5-15 mM, using both linear sweep voltammetry and chronoamperometric measurements in buffer-based solutions. The biosensor performance was examined in 30 µL volumes of fetal bovine serum. Whilst a reduction in the sensor sensitivity was evident within 100% serum samples (compared to buffer media), the sensor demonstrated linear glucose detection with increasing glucose concentrations (5-17 mM).

| S-EPMC8392376 | biostudies-literature

Dispersed Conducting Polymer Nanocomposites with Glucose Oxidase and Gold Nanoparticles for the Design of Enzymatic Glucose Biosensors.

Project description:Biosensors for the determination of glucose concentration have a great significance in clinical diagnosis, and in the food and pharmaceutics industries. In this research, short-chain polyaniline (PANI) and polypyrrole (Ppy)-based nanocomposites with glucose oxidase (GOx) and 6 nm diameter AuNPs (AuNPs(6 nm)) were deposited on the graphite rod (GR) electrode followed by the immobilization of GOx. Optimal conditions for the modification of GR electrodes by conducting polymer-based nanocomposites and GOx were elaborated. The electrodes were investigated by cyclic voltammetry and constant potential amperometry in the presence of the redox mediator phenazine methosulfate (PMS). The improved enzymatic biosensors based on GR/PANI-AuNPs(6 nm)-GOx/GOx and GR/Ppy-AuNPs(6 nm)-GOx/GOx electrodes were characterized by high sensitivity (65.4 and 55.4 μA mM-1 cm-2), low limit of detection (0.070 and 0.071 mmol L-1), wide linear range (up to 16.5 mmol L-1), good repeatability (RSD 4.67 and 5.89%), and appropriate stability (half-life period (τ1/2) was 22 and 17 days, respectively). The excellent anti-interference ability to ascorbic and uric acids and successful practical application for glucose determination in serum samples was presented for GR/PANI-AuNPs(6 nm)-GOx/GOx electrode.

| S-EPMC8271668 | biostudies-literature

Glucose oxidase-catalyzed growth of gold nanoparticles enables quantitative detection of attomolar cancer biomarkers.

Project description:Ultrasensitive and quantitative detection of cancer biomarkers is an unmet challenge because of their ultralow concentrations in clinical samples. Although gold nanoparticle (AuNP)-based immunoassays offer high sensitivity, they were unable to quantitatively detect targets of interest most likely due to their very narrow linear ranges. This article describes a quantitative colorimetric immunoassay based on glucose oxidase (GOx)-catalyzed growth of 5 nm AuNPs that can detect cancer biomarkers from attomolar to picomolar levels. In addition, the limit of detection (LOD) of prostate-specific antigen (PSA) of this approach (93 aM) exceeds that of commercial enzyme-linked immunosorbent assay (ELISA) (6.3 pM) by more than 4 orders of magnitude. The emergence of red or purple color based on enzyme-catalyzed growth of 5 nm AuNPs in the presence of target antigen is particularly suitable for point-of-care (POC) diagnostics in both resource-rich and resource-limited settings.

| S-EPMC4066917 | biostudies-literature

Facile immobilization of glucose oxidase onto gold nanostars with enhanced binding affinity and optimal function.

Project description:Gold nanoparticles provide a user-friendly and efficient surface for immobilization of enzymes and proteins. In this paper, we present a novel approach for enzyme bioconjugation to gold nanostars (AuNSs). AuNSs were modified with l-cysteine (Cys) and covalently bound to N-hydroxysulfosuccinimide (sulfo-NHS) activated intermediate glucose oxidase (GOx) to fabricate a stable and sensitive AuNSs-Cys-GOx bioconjugate complex. Such a strategy has the potential for increased attachment affinity without protein adsorption onto the AuNSs surface. Good dispersity in buffer suspension was observed, as well as stability in high ionic environments. Using the AuNSs-Cys-GOx bioconjugates showed greater sensitivity in the measuring of low concentrations of glucose based on plasmonic and colorimetric detection. Such a novel approach for enzyme immobilization can lead to AuNSs-Cys-GOx bioconjugate complexes that can be used as catalytic nanodevices in nanobiosensors based on oxidases in biomedical applications.

| S-EPMC6549951 | biostudies-literature

Redox-Mediated Gold Nanoparticles with Glucose Oxidase and Egg White Proteins for Printed Biosensors and Biofuel Cells.

Project description:Glucose oxidase (GOx)-based electrodes are important for bioelectronics, such as glucose sensors. It is challenging to effectively link GOx with nanomaterial-modified electrodes while preserving enzyme activity in a biocompatible environment. To date, no reports have used biocompatible food-based materials, such as egg white proteins, combined with GOx, redox molecules, and nanoparticles to create the biorecognition layer for biosensors and biofuel cells. This article demonstrates the interface of GOx integrated with egg white proteins on a 5 nm gold nanoparticle (AuNP) functionalized with a 1,4-naphthoquinone (NQ) and conjugated with a screen-printed flexible conductive carbon nanotube (CNT)-modified electrode. Egg white proteins containing ovalbumin can form three-dimensional scaffolds to accommodate immobilized enzymes and adjust the analytical performance. The structure of this biointerface prevents the escape of enzymes and provides a suitable microenvironment for the effective reaction. The bioelectrode's performance and kinetics were evaluated. Using redox-mediated molecules with the AuNPs and the three-dimensional matrix made of egg white proteins improves the transfer of electrons between the electrode and the redox center. By engineering the layer of egg white proteins on the GOx-NQ-AuNPs-mediated CNT-functionalized electrodes, we can modulate analytical performances such as sensitivity and linear range. The bioelectrodes demonstrate high sensitivity and can prolong the stability by more than 85% after 6 h of continuous operation. The use of food-based proteins with redox molecule-modified AuNPs and printed electrodes demonstrates advantages for biosensors and energy devices due to their small size, large surface area, and ease of modification. This concept holds a promise for creating biocompatible electrodes for biosensors and self-sustaining energy devices.

| S-EPMC10002497 | biostudies-literature

Noninvasive continuous monitoring of physiological glucose using a monosaccharide-sensing contact lens.

Project description:We have tested the feasibility of tear glucose sensing using a daily, disposable contact lens embedded with boronic acid-containing fluorophores as a potential alternative to current invasive glucose-monitoring techniques. Our findings show that our approach may, indeed, be suitable for the continuous monitoring of tear glucose levels in the range 50-500 microM, which track blood glucose levels that are approximately 5-10-fold higher. We compare the response of the boronic acid probes in the contact lens to solution-based measurements and can conclude that both the pH and polarity within the contact lens need to be considered with respect to choosing/designing and optimizing glucose-sensing probes for contact lenses.

| S-EPMC6906081 | biostudies-literature

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