Title
Conserved specificity of extracellular wastewater peptidases revealed by multiplex substrate profiling by mass spectrometry
Author
Josephine Meibom
Laboratory of Environmental Virology, School of Architecture, Civil and Environmental Engineering, École Polytechnique Fédérale de Lausanne (EPFL)
Tamar Kohn
Laboratory of Environmental Virology, School of Architecture, Civil and Environmental Engineering, École Polytechnique Fédérale de Lausanne (EPFL)
... show all
Abstract
Peptide-based chemicals are promising for numerous applications including home and personal care and medical treatments. To better understand and control the environmental fate of peptide-based chemicals, in-depth knowledge on the specificity of wastewater peptidases is needed. Here, we employed multiplex substrate profiling by mass spectrometry to obtain specificity profiles of extracellular peptidases derived from influent and aeration tanks of three full-scale wastewater treatment plants. Specificities were confirmed by fluorogenic peptidase substrates. Our results revealed highly similar specificity profiles across wastewater treatment plants. We found that hydrolysis by extracellular wastewater peptidases is favored when positively charged amino acid residues surround the cleavage site and disfavored when negatively charged amino acid residues surround the cleavage site.
Keywords
Peptidase specificityWastewater systemsMultiplex substrate profiling by mass spectrometryPeptide-based chemicalsEnvironmental fateBenign-by-design
Object type
Language
English [eng]
Persistent identifier
Appeared in
Title
Environmental Chemistry Letters
Volume
23
Issue
4
ISSN
1610-3653
Issued
2025
From page
953
To page
959
Publication
Springer Science and Business Media LLC
Version type
Date issued
2025
Access rights
Rights
Rights statement
© The Author(s) 2025
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