A sonochemically fabricated alcohol oxidase enzyme micro-electrode array is reported. Sensors of this type were fabricated by first depositing an insulating polydiaminobenzene film on supporting gold electrodes. Sonication and subsequent ablation exposed discrete areas of the underlying conducting electrode, which collectively act as a microelectrode array. Electropolymerisation of aniline has been used to generate in situ polyaniline containing entrapped alcohol oxidase. The physical and electrochemical properties of these films were studied and reported within this paper. The final composites were shown to behave with microelectrode performance characteristics for the detection of aqueous ethanol concentrations.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.bios.2004.12.012 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Modeling and interaction study of alcohol oxidase and ProteaseA in methylotrophic yeast : insights from In-silico analysis.
J Biomol Struct Dyn
December 2024
Department of Bioinformatics, School of Life Sciences Pondicherry University, Puducherry, India.
Flavin adenine nucleotide (FAD)-dependent oxidoreductase enzyme Alcohol oxidase (AOX) facilitates the growth of methylotrophic yeast C. boidinii by catabolizing methanol, producing formaldehyde and hydrogen peroxide. Vacuolar Protease-A (PrA) from C.
View Article and Find Full Text PDFIntegrated Wearable Flexible Hydrogel Patch Sensing System for the Detection of Physiological Markers.
Anal Chem
January 2025
School of Agricultural Engineering, Jiangsu University, Zhenjiang 212013, PR China.
Conventional wearable flexible sensing systems typically comprise three components: a flexible substrate that contacts the skin, a signal processing module, and a signal output module. These components function relatively independently, resulting in a complex system that lacks sufficient integration. Therefore, developing an integrated wearable flexible sensing system by combining the flexible substrate, the signal processing module, and the signal output module not only enhances performance and comfort, but also reduces manufacturing costs and the risk of failure.
View Article and Find Full Text PDFHybrid Enzyme-Electrocatalyst Cascade Modified Gas-Diffusion Electrodes for Methanol Formation from Carbon Dioxide.
Angew Chem Int Ed Engl
December 2024
Analytical Chemistry - Center for Electrochemical Sciences (CES), Faculty of Chemistry and Biochemistry, Ruhr University Bochum, Universitätsstr. 150, D-44780, Bochum, Germany.
We propose a hybrid electrocatalytic-bioelectrocatalytic reaction cascade integrated on a gas diffusion electrode for CO reduction under selective formation of methanol. Ag-BiO selectively reduces gaseous CO to formate at neutral pH conditions. A subsequent enzymatic cascade comprising formaldehyde dehydrogenase and alcohol dehydrogenase, which are both nicotinamide adenine dinucleotide (NAD)-dependent, further reduce formate sequentially to formaldehyde and methanol.
View Article and Find Full Text PDFBiochemical and structural insights into pinoresinol hydroxylase from Pseudomonas sp.
Arch Biochem Biophys
November 2024
Department of Biology and Biotechnology "Lazzaro Spallanzani", University of Pavia, Pavia, Italy. Electronic address:
The vanillyl alcohol oxidase/p-cresol methylhydroxylase (VAO/PCMH) flavoprotein family comprises a broad spectrum of enzymes capable of catalyzing the oxidative bioconversions of various substrates. Among them, pinoresinol hydroxylase (PinH) from the 4-alkylphenol oxidizing subgroup initiates the oxidative degradation of (+)-pinoresinol, a lignan important for both lignin structure and plant defense. In this study, we present a detailed biochemical and structural characterization of PinH from Pseudomonas sp.
View Article and Find Full Text PDFNovel Basidiomycetous Alcohol Oxidase from -Characterisation, Kinetics, and Proteolytic Modifications.
Int J Mol Sci
November 2024
Department of Biochemistry and Biotechnology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Akademicka 19 St., 20-033 Lublin, Poland.
Intracellular alcohol oxidase (AOX) was isolated from the basidiomycetous white rot fungus FCL139. The enzyme was semi-purified (13-fold) using two-step chromatography with 30% activity recovery. The identity of the protein was confirmed by LC-MS/MS analysis, and its MW (72 kDa) and pI (6.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!