Natalie Wichmann, Josephine Meibom, Tamar Kohn, Michael Zumstein
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Conserved specificity of extracellular wastewater peptidases revealed by multiplex substrate profiling by mass spectrometry
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.
期刊介绍：
Environmental Chemistry Letters explores the intersections of geology, chemistry, physics, and biology. Published articles are of paramount importance to the examination of both natural and engineered environments. The journal features original and review articles of exceptional significance, encompassing topics such as the characterization of natural and impacted environments, the behavior, prevention, treatment, and control of mineral, organic, and radioactive pollutants. It also delves into interfacial studies involving diverse media like soil, sediment, water, air, organisms, and food. Additionally, the journal covers green chemistry, environmentally friendly synthetic pathways, alternative fuels, ecotoxicology, risk assessment, environmental processes and modeling, environmental technologies, remediation and control, and environmental analytical chemistry using biomolecular tools and tracers.
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