Biomimetic CO<sub>2</sub> Capture Unlocked through Enzyme Mining: Discovery of a Highly Thermo- and Alkali-Stable Carbonic Anhydrase

Taking immediate action to combat the urgent threat of CO<sub>2</sub>-driven global warming is crucial for ensuring a habitable planet. Decarbonizing the industrial sector requires implementing sustainable carbon-capture technologies, such as biomimetic hot potassium carbonate capture (BioHPC). BioHPC is superior to traditional amine-based strategies due to its eco-friendly nature. This innovative technology relies on robust carbonic anhydrases (CAs), enzymes that accelerate CO<sub>2</sub> hydration and endure harsh industrial conditions like high temperature and alkalinity. Thus, the discovery of highly stable CAs is crucial for the BioHPC technology advancement. Through high-throughput bioinformatics analysis, we identified a highly thermo- and alkali-stable CA, termed CA-KR1, originating from a metagenomic sample collected at a hot spring in Kirishima, Japan. CA-KR1 demonstrates remarkable stability at high temperatures and pH, with a half-life of 24 h at 80 °C and retains activity and solubility even after 30 d in a 20% (w/v) K<sub>2</sub>CO<sub>3</sub>/pH 11.5 solution─a standard medium for HPC. In pressurized batch reactions, CA-KR1 enhanced CO<sub>2</sub> absorption by >90% at 90 °C, 20% K<sub>2</sub>CO<sub>3</sub>, and 7 bar. To our knowledge, CA-KR1 constitutes the most resilient CA biocatalyst for efficient CO<sub>2</sub> capture under HPC-relevant conditions, reported to date. CA-KR1 integration into industrial settings holds great promise in promoting efficient BioHPC, a potentially game-changing development for enhancing carbon-capture capacity toward industrial decarbonization.

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Publication Details

Journal
Environmental Science & Technology
Published
2024-09-23
DOI
https://doi.org/10.1021/acs.est.4c04291
Citations
21
Primary Topic
Enzyme function and inhibition
Type
article
Field-Weighted Citation Impact
4.91

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article

Biomimetic CO2 Capture Unlocked through Enzyme Mining: Discovery of a Highly Thermo- and Alkali-Stable Carbonic Anhydrase

Dimitra Zarafeta, Georgios Filis, Io Antonopoulou, Pavlos Saridis et al.
21 citations
Environmental Science & Technology
Enzyme function and inhibition
4.91
article

Biomimetic CO2 Capture Unlocked through Enzyme Mining: Discovery of a Highly Thermo- and Alkali-Stable Carbonic Anhydrase

Dimitra Zarafeta, Georgios Filis, Io Antonopoulou, Pavlos Saridis, Γεώργιος Σκρέτας, Ayanne de Oliveira Maciel, Konstantinos Rigkos
article en
21 citations

Abstract

Taking immediate action to combat the urgent threat of CO<sub>2</sub>-driven global warming is crucial for ensuring a habitable planet. Decarbonizing the industrial sector requires implementing sustainable carbon-capture technologies, such as biomimetic hot potassium carbonate capture (BioHPC). BioHPC is superior to traditional amine-based strategies due to its eco-friendly nature. This innovative technology relies on robust carbonic anhydrases (CAs), enzymes that accelerate CO<sub>2</sub> hydration and endure harsh industrial conditions like high temperature and alkalinity. Thus, the discovery of highly stable CAs is crucial for the BioHPC technology advancement. Through high-throughput bioinformatics analysis, we identified a highly thermo- and alkali-stable CA, termed CA-KR1, originating from a metagenomic sample collected at a hot spring in Kirishima, Japan. CA-KR1 demonstrates remarkable stability at high temperatures and pH, with a half-life of 24 h at 80 °C and retains activity and solubility even after 30 d in a 20% (w/v) K<sub>2</sub>CO<sub>3</sub>/pH 11.5 solution─a standard medium for HPC. In pressurized batch reactions, CA-KR1 enhanced CO<sub>2</sub> absorption by >90% at 90 °C, 20% K<sub>2</sub>CO<sub>3</sub>, and 7 bar. To our knowledge, CA-KR1 constitutes the most resilient CA biocatalyst for efficient CO<sub>2</sub> capture under HPC-relevant conditions, reported to date. CA-KR1 integration into industrial settings holds great promise in promoting efficient BioHPC, a potentially game-changing development for enhancing carbon-capture capacity toward industrial decarbonization.

Environmental Science & TechnologyVol. 58(40)
Luleå University of Technology (SE), University of Ioannina (GR), National and Kapodistrian University of Athens (GR), National Hellenic Research Foundation (GR), Alexander Fleming Biomedical Sciences Research Center (GR)
Hellenic Academic Libraries Link, European Commission, Horizon 2020 Framework Programme, HORIZON EUROPE Framework Programme
Openalex Percentile: Top 4%
Enzyme function and inhibition
4.91
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