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Lookup NU author(s): Dr Anastasia ResteuORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
Limonene is a natural monoterpene omnipresent in human environments. It enters wastewater and is also metabolised in methanogenic digesters. A stable limonene-degrading methanogenic enrichment culture was investigated by metagenomic, metatranscriptomic and metaproteomic data sets to characterise the microbial community and identify the limonene degradation pathway. Thirty-two metagenome-assembled genomes revealed a complex community of bacteria and methanogenic archaea dominated by Candidatus Velamenicoccus archaeovorus as the top predator, contributing two-thirds of the reads in the metagenome. The presence of several fermenting bacteria (Anaerolineaceae, Aminidesulfovibrio, Smithellaceae, Lentimicrobium) indicated the recycling of necromass in a microbial loop. Only one hydrocarbon-activating enzyme system was expressed, a member of the alkyl- and arylsuccinate synthase family which is a glycine radical enzyme that adds fumarate to hydrocarbons. The limonenylsuccinate synthase gene encodes a modified substrate binding pocket with two smaller amino acids, suggesting an adaptation for the larger structure of limonene. The limonenylsuccinate synthase operon and a ring cleavage operon, as well as genes for the final syntrophic fermentation to acetate, hydrogen and formate were encoded in a Syntrophobacteraceae genome. Almost all genes for this degradation pathway were highly transcribed and expressed, demonstrating a catalytic role for glycine radical enzymes in methanogenic systems degrading limonene
Author(s): Lonsing A, Martens GA, Resteu A, Kizina J, Wilkie I, Bahr A, Harder J
Publication type: Article
Publication status: Published
Journal: Environmental Microbiology
Year: 2025
Volume: 27
Issue: 11
Print publication date: 01/11/2025
Online publication date: 03/11/2025
Acceptance date: 27/11/2025
Date deposited: 29/01/2026
ISSN (print): 1462-2912
ISSN (electronic): 1462-2920
Publisher: Wiley
URL: https://doi.org/10.1111/1462-2920.70192
DOI: 10.1111/1462-2920.70192
Data Access Statement: Proteomic data are available at PRIDE (PXD025008). NGS sequences and MAGs are deposited at NCBI.
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