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Phenol-driven cometabolic degradation of cis-1,2-dichloroethene (cDCE): insights from Acinetobacter pittii and Ectopseudomonas alcaliphila

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F27283933%3A_____%2F25%3AN0000026" target="_blank" >RIV/27283933:_____/25:N0000026 - isvavai.cz</a>

  • Result on the web

    <a href="https://link.springer.com/article/10.1186/s12302-025-01237-z" target="_blank" >https://link.springer.com/article/10.1186/s12302-025-01237-z</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1186/s12302-025-01237-z" target="_blank" >10.1186/s12302-025-01237-z</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Phenol-driven cometabolic degradation of cis-1,2-dichloroethene (cDCE): insights from Acinetobacter pittii and Ectopseudomonas alcaliphila

  • Original language description

    Accumulation of xenobiotic chlorinated ethenes (CEs) at legacy industrial soil and groundwater sites around the world is a pressing environmental and public health issue. Understanding the biochemical pathways through which microorganisms degrade cDCE is key to developing cost-effective, sustainable bioremediation strategies for CE contamination. Two strains, Acinetobacter pittii CEP14 and Ectopseudomonas alcaliphila JAB1, isolated from contaminated industrial sites, have demonstrated the ability to cometabolically degrade cDCE in the presence of phenol. In this study, we integrate transcriptomics, using differential gene expression analysis to pinpoint genes induced during cDCE co‐metabolism, with proteomics to confirm protein‐level expression. We use heterologous expression experiments to demonstrate that phenol monooxygenase is responsible for oxidising cDCE in both strains. Furthermore, we show that CEP14 and JAB1 α-subunits share 71.4% identity with each other but only 14.6–26.5% identity with established monooxygenases with known cDCE-oxidising activity, highlighting the diversity of enzymes that may be capable of cometabolic cDCE degradation. Finally, we hypothesise on a two-branch phenol monooxygenase-mediated cDCE degradation pathway in which the chemical degradative intermediates 2,2-dichloroacetaldehyde and cDCE epoxides are formed. This study sheds light on the biochemical mechanisms by which monoaromatic compounds can enhance the biodegradation of cDCE and demonstrates the potential utilisation of strains CEP14 and JAB1 for the biodegradation of cDCE.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>ost</sub> - Miscellaneous article in a specialist periodical

  • CEP classification

  • OECD FORD branch

    30304 - Public and environmental health

Result continuities

  • Project

  • Continuities

    N - Vyzkumna aktivita podporovana z neverejnych zdroju

Others

  • Publication year

    2025

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Environmental Sciences Europe

  • ISSN

  • e-ISSN

    2190-4715

  • Volume of the periodical

    37

  • Issue of the periodical within the volume

    196

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    15

  • Pages from-to

  • UT code for WoS article

    001609529600004

  • EID of the result in the Scopus database

    2-s2.0-105021089092