Uncovering enzymatic tools promoting lignocellulose breakdown in the anaerobic bacterium Ruminiclostridium cellulolyticum

Understanding the anaerobic deconstruction of recalcitrant lignocellulose remains challenging. Combining substrate composition and transcriptomic analyses, we shortlisted Ruminiclostridium cellulolyticum enzymes that modify lignocelullose and distinguished two members of the large SGNH hydrolase superfamily potentially enhancing lignocellulosic biomass degradation by acting on decorations of lignin and hemicelluloses but also on cross-links implicating lignin. Using genetic modifications, bioinformatics and biochemistry, we show they promote the plant cell wall ester-linked hydroxycinnamic acid derivatives release, a role never described for these proteins mainly synthesized by the restricted group of cellulolytic and cellulosome-producing bacteria. In addition to the recent observation of fungal limited lignin alterations in oxygen absence, this discovery is to the best of our knowledge, the first evidence of such anaerobic bacterial process that provides a better comprehension of the biogeochemical Earth's carbon cycle. Furthermore, a better knowledge of the anaerobic plant biomass degradation could help to design non-fossil resources based biotechnological applications, a cornerstone of bioeconomy development.

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Journal
Communications Biology
Published
2025-12-04
DOI
https://doi.org/10.1038/s42003-025-09287-y
Primary Topic
Enzyme-mediated dye degradation
Type
article
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0.00

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article

Uncovering enzymatic tools promoting lignocellulose breakdown in the anaerobic bacterium Ruminiclostridium cellulolyticum

Caroline Monteil, Yann Denis, Sébastien Santini, David Crônier et al.
Communications Biology
Enzyme-mediated dye degradation
article

Uncovering enzymatic tools promoting lignocellulose breakdown in the anaerobic bacterium Ruminiclostridium cellulolyticum

Caroline Monteil, Yann Denis, Sébastien Santini, David Crônier, Véronique Aguié‐Béghin, Paul‐Henri Ducrot, Felipe Mejia-Otalvaro, Craig B. Faulds, Anouck Habrant, Giuliano Sciara, Séverine Gagnot, Henri‐Pierre Fierobe, Gaël Panis, Brigitte Chabbert, Éric Record, Stéphanie Perret, Nicolas Vita, Florian Pion, Marion Holmière, Lison Degeilh, Fabian Debard
article en

Abstract

Understanding the anaerobic deconstruction of recalcitrant lignocellulose remains challenging. Combining substrate composition and transcriptomic analyses, we shortlisted Ruminiclostridium cellulolyticum enzymes that modify lignocelullose and distinguished two members of the large SGNH hydrolase superfamily potentially enhancing lignocellulosic biomass degradation by acting on decorations of lignin and hemicelluloses but also on cross-links implicating lignin. Using genetic modifications, bioinformatics and biochemistry, we show they promote the plant cell wall ester-linked hydroxycinnamic acid derivatives release, a role never described for these proteins mainly synthesized by the restricted group of cellulolytic and cellulosome-producing bacteria. In addition to the recent observation of fungal limited lignin alterations in oxygen absence, this discovery is to the best of our knowledge, the first evidence of such anaerobic bacterial process that provides a better comprehension of the biogeochemical Earth's carbon cycle. Furthermore, a better knowledge of the anaerobic plant biomass degradation could help to design non-fossil resources based biotechnological applications, a cornerstone of bioeconomy development.

Communications BiologyVol. 9(1)
University of Geneva (CH), Centre National de la Recherche Scientifique (FR), Aix-Marseille Université (FR), Commissariat à l'Énergie Atomique et aux Énergies Alternatives (FR), Université Paris-Saclay (FR), Novo Nordisk Foundation (DK), Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement (FR), Institut Jean-Pierre Bourgin (FR), Biodiversité et Biotechnologie Fongiques (FR), Institut de Biosciences et Biotechnologies (FR), Université de Reims Champagne-Ardenne (FR)
Aix-Marseille Université, Agence Nationale de la Recherche, Université de Reims Champagne-Ardenne
Openalex Percentile: Top 72%
Enzyme-mediated dye degradation
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