Hyperthermophilic methanogenic archaea act as high-pressure CH4 cell factories
Bioprocesses converting carbon dioxide with molecular hydrogen to methane (CH 4 ) are currently being developed to enable a transition to a renewable energy production system. In this study, we present a comprehensive physiological and biotechnological examination of 80 methanogenic archaea (methano...
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Published in: | Communications biology Vol. 4; no. 1; p. 289 |
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Main Authors: | , , , , , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
London
Nature Publishing Group UK
05-03-2021
Nature Publishing Group Nature Portfolio |
Subjects: | |
Online Access: | Get full text |
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Summary: | Bioprocesses converting carbon dioxide with molecular hydrogen to methane (CH
4
) are currently being developed to enable a transition to a renewable energy production system. In this study, we present a comprehensive physiological and biotechnological examination of 80 methanogenic archaea (methanogens) quantifying growth and CH
4
production kinetics at hyperbaric pressures up to 50 bar with regard to media, macro-, and micro-nutrient supply, specific genomic features, and cell envelope architecture. Our analysis aimed to systematically prioritize high-pressure and high-performance methanogens. We found that the hyperthermophilic methanococci
Methanotorris igneus
and
Methanocaldococcoccus jannaschii
are high-pressure CH
4
cell factories. Furthermore, our analysis revealed that high-performance methanogens are covered with an S-layer, and that they harbour the amino acid motif Tyr
α444
Gly
α445
Tyr
α446
in the alpha subunit of the methyl-coenzyme M reductase. Thus, high-pressure biological CH
4
production in pure culture could provide a purposeful route for the transition to a carbon-neutral bioenergy sector.
Mauerhofer et al. examine 80 species of methanogenic archaea at high pressures and evaluate growth and methane production, identifying
Methanotorris igneus
and
Methanocaldococcoccus jannaschii
as high-pressure methane cell factories. They find that high-performance methanogens are covered with an S-layer and harbour the amino acid motif Tyrα444 Glyα445 Tyrα446 in the alpha subunit of the methyl-coenzyme M reductase. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 2399-3642 2399-3642 |
DOI: | 10.1038/s42003-021-01828-5 |