1- and 2-thionaphthylacetates were tested as cholinesterase substrates. It was shown that the butyrilcholinesterase from horse serum can hydrolize these compounds. The hydrolysis velocity of 1-thionaphthylacetate was comparable with hydrolysis velocity of acetylthiocholine (the well known cholinesterase substrate), but 2-thionaphthylacetate was hydrolysed more slowly. The values of the kinetic parameters V and K(m) for butyrylcholinesterase hydrolysis of 1- and 2-thionaphthylacetates were determined. It was offered to use 1-thionaphthylacetates as the substrate for cholinesterases.
Download full-text PDF |
Source |
---|
Environ Sci Technol
December 2024
Beijing Key Laboratory for Green Catalysis and Separation, Key Laboratory of Beijing on Regional Air Pollution Control, Key Laboratory of Advanced Functional Materials, Education Ministry of China, Laboratory of Catalysis Chemistry and Nanoscience, Department of Chemical Engineering and Technology, College of Materials Science and Engineering, Beijing University of Technology, Beijing 100124, China.
Chlorinated and oxygenated volatile organic compounds (CVOCs and OVOCs) pose a significant threat to human health. Catalytic oxidation effectively removes these pollutants, but catalyst deactivation is a challenge. Our study focused on the hydrolysis oxidation of chlorobenzene (CB) and ethyl acetate (EA) over Ru/MO/HZSM-5 (M = W, Mo).
View Article and Find Full Text PDFBiotechnol Biofuels Bioprod
December 2024
Department of Chemical and Biomolecular Engineering, Vanderbilt University, Nashville, TN, 37235, USA.
Background: Cellulose, an abundant biopolymer, has great potential to be utilized as a renewable fuel feedstock through its enzymatic degradation into soluble sugars followed by sugar fermentation into liquid biofuels. However, crystalline cellulose is highly resistant to hydrolysis, thus industrial-scale production of cellulosic biofuels has been cost-prohibitive to date. Mechanistic studies of enzymes that break down cellulose, called cellulases, are necessary to improve and adapt such biocatalysts for implementation in biofuel production processes.
View Article and Find Full Text PDFBiophys J
November 2024
Department of Bionanoscience, Kavli Institute of Nanoscience, Faculty of Applied Sciences, Delft University of Technology, Delft, the Netherlands. Electronic address:
Int J Biol Macromol
December 2024
School of Biological Science and Technology, University of Jinan, Jinan, Shandong 250022, China. Electronic address:
Enzyme therapy for cocaine detoxification should break down both cocaine and its primary toxic metabolite, benzoylecgonine (BZE), which is also the main form of cocaine contaminant in the environment. An ideal BZE-metabolizing enzyme (BZEase) is expected to be highly efficient and selective in BZE hydrolysis. Here, BZEase4 was engineered from bacterial cocaine esterase (CocE) by our reactant state-based enzyme design theories (RED), which has a 34,977-fold improved substrate discrimination between BZE and the neurotransmitter acetylcholine (ACh), compared with wild-type CocE.
View Article and Find Full Text PDFJ Sci Food Agric
January 2025
Department of Chemistry and Technology of Drugs, Food Chemistry Laboratory, Sapienza University of Rome, Rome, Italy.
Background: Cauliflower (Brassica oleracea L.) and globe artichoke (Cynara scolymus L.) are vegetables with a high waste index mainly related to stems and leaves.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!