A weak chemical signal might result in a large response when biochemically amplified. Enzymatic recycling of the analyte is one of the biochemical ways of providing an effective increase in biosensor sensitivity by several orders of magnitude. The enhancement of sensitivity is provided by consecutive consumption and generation of the analyte on the sensor surface. The principle of enzymatic substrate regeneration using bioelectrocatalysis and coupled enzymes is shortly reviewed and illustrated with some recent developments of biosensors for catecholamines, and its potential for electrochemical immunoassays is outlined.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1007/978-3-0348-9045-8_4 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Uncovering the substrate of olefin synthase loading domains in cyanobacteria sp. strain PCC 7002.
RSC Chem Biol
January 2025
Department of Chemical and Biological Engineering, University of Wisconsin - Madison Madison Wisconsin 53706 USA
Cyanobacteria are widespread, photosynthetic, gram-negative bacteria that generate numerous bioactive secondary metabolites complex biosynthetic enzymatic machinery. The model cyanobacterium sp. strain PCC 7002, hereafter referred to as PCC 7002, contains a type I polyketide synthase (PKS), termed olefin synthase (OlsWT), that synthesizes 1-nonadecene and 1,14-nonadecadiene: α-olefins that are important for growth at low temperatures.
View Article and Find Full Text PDFMicelle-enabled bromination of α-oxo ketene dithioacetals: mild and scalable approach enzymatic catalysis.
Org Biomol Chem
January 2025
Nanotec-CU Center of Excellence on Food and Agriculture, Department of Chemistry, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand.
The bromination of α-oxo ketene dithioacetals using KBr/HO, catalyzed by vanadium chloroperoxidase (VCPO), has been successfully demonstrated. A comparative study of enzymatic processes "on water" "in water", using 2 wt% of the surfactant TPGS-750-M revealed that the in-water protocol not only provides higher yields but also accommodates a broader substrate scope. This bromination method in an aqueous micellar medium enabled the preparation of brominated α-oxo ketene dithioacetals in fair to excellent yields (23 examples).
View Article and Find Full Text PDFStudy of the interaction between alkaline phosphatase and biomacromolecule substrates.
Anal Bioanal Chem
January 2025
Gene Engineering and Biotechnology of Beijing Key Laboratory, College of Life Sciences, Beijing Normal University, Beijing, 100875, China.
Alkaline phosphatase (ALP) is a nonspecific phosphatase, and its interaction with substrates mainly depends on the recognition of phosphate groups on the substrate. Previous enzymatic research has focused mainly on the enzymatic reaction kinetics of the inorganic small molecule p-nitrophenol phosphate (pNPP) as a substrate, but its interaction with biomacromolecule substrates has not been reported. In current scientific research, ALP is often used for molecular cloning, such as removing the 5' termini of nucleic acids.
View Article and Find Full Text PDFDiscovery and mechanistic exploration of promiscuous xylosyltransferase based on protein engineering.
Int J Biol Macromol
January 2025
National Resource Center for Chinese Meteria Medica, China Academy of Chinese Medical Sciences, Beijing 100700, China; State Key Laboratory for Quality Ensurance and Sustainable Use of Dao-di Herbs, Beijing 100700, China.
Glycosylation is an effective means to alter the structure and properties of plant compounds, influencing the pharmacological activity of natural products (NPs) to obtain highly active NPs. In nature, glucosides are the most widely distributed, while other glycosides such as xylosides are less common and present in lower quantities. This is due to the scarcity of xylosyltransferases with substrate promiscuity in nature, and the modification of their catalytic function is also quite challenging.
View Article and Find Full Text PDFThe Stenotrophomonas maltophilia L2 cephalosporinase is one of two beta-lactamases which afford S. maltophilia beta-lactam resistance. With the overuse of beta-lactams, selective pressures have contributed to the evolution of these proteins, generating proteins with an extended spectrum of activity.
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!