Conserved specificity of extracellular wastewater peptidases revealed by multiplex substrate profiling by mass spectrometry

Natalie Wichmann, Josephine Meibom, Tamar Kohn, Michael Zumstein (Korresp. Autor*in)

Veröffentlichungen: Beitrag in FachzeitschriftArtikelPeer Reviewed

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.

OriginalspracheEnglisch
Aufsatznummer100210
Seiten (von - bis)953-959
Seitenumfang7
FachzeitschriftEnvironmental Chemistry Letters
Jahrgang23
Ausgabenummer4
DOIs
PublikationsstatusVeröffentlicht - Aug. 2025

Fördermittel

Open access funding provided by University of Vienna. Funding was provided by the Swiss National Science Foundation through the Ambizione Fellowship PZ00P2_193130 to MZ and project 310030_215226 to TK. This research was funded in part by the Austrian Science Fund (FWF) [Grant No. 10.55776/COE7]. For open access purposes, the author has applied a CC BY public copyright license to any author accepted manuscript version arising from this submission.

ÖFOS 2012

  • 104023 Umweltchemie

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