Please use this identifier to cite or link to this item: http://hdl.handle.net/10773/27455
Title: Soluble esterases as biomarkers of neurotoxic compounds in the widespread serpulid Ficopomatus enigmaticus (Fauvel, 1923)
Author: Casu, Valentina
Tardelli, Federica
De Marchi, Lucia
Monni, Gianfranca
Cuccaro, Alessia
Oliva, Matteo
Freitas, Rosa
Pretti, Carlo
Keywords: Cholinesterase
Carboxylesterase
Serpulidae
Ficopomatus enigmaticus
Biomarkers
Issue Date: 16-Jul-2019
Publisher: Taylor & Francis
Abstract: The characterization of soluble cholinesterases (ChEs) together with carboxylesterases (CEs) in Ficopomatus enigmaticus as suitable biomarkers of neurotoxicity was the main aim of this study. ChEs of F. enigmaticus were characterized considering enzymatic activity, substrate affinity (acetyl-, butyryl-, propionylthiocholine), kinetic parameters (Km and Vmax) and in vitro response to model inhibitors (eserine hemisulfate, iso-OMPA, BW284C51), and carbamates (carbofuran, methomyl, aldicarb, and carbaryl). CEs were characterized based on enzymatic activity, kinetic parameters and in vitro response to carbamates (carbofuran, methomyl, aldicarb, and carbaryl). Results showed that cholinesterases from F. enigmaticus showed a substrate preference for acetylthiocholine followed by propionylthiocholine; butyrylthioline was not hydrolyzed differently from other Annelida species. CE activity was in the same range of cholinesterase activity with acetylthiocholine as substrate; the enzyme activity showed high affinity for the substrate p-nytrophenyl butyrate. Carbamates inhibited ChE activity with propionylthiocholine as substrate to a higher extent than with acetylthiocoline. Also CE activity was inhibited by all tested carbamates except carbaryl. In vitro data highlighted the presence of active forms of ChEs and CEs in F. enigmaticus that could potentially be inhibited by pesticides at environmentally relevant concentration.
Peer review: yes
URI: http://hdl.handle.net/10773/27455
DOI: 10.1080/03601234.2019.1640028
ISSN: 0360-1234
Appears in Collections:CESAM - Artigos
DBio - Artigos

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