Catalytic CO<sub>2</sub> Hydration and Sequestration by Carbonic Anhydrase-Mimetic Nanotubes

Promotion of the conversion of CO2 into HCO3– is necessary for the efficient sequestration of CO2 into metal carbonate minerals, a promising CO2 utilization strategy. Carbonic anhydrase (CA), a ubiquitous enzyme, exhibits high activity in CO2 hydration and suffers from inherent instability as a biological disadvantage. Consequently, there is a demand for a CA-mimetic catalyst that is stable at high temperatures and can be easily prepared. In this study, we have developed a new CA-mimetic nanotube (CMNT) catalyst, demonstrating remarkable catalytic activity in CO2 hydration. The CMNT catalyst is easily prepared by the layer-by-layer (LbL) method, which involves the sequential infusion of polyelectrolyte and polypeptide solutions into a track-etched polymeric membrane. Multiple catalytic Zn-histidyl imidazole complexes were built on the inner channel of nanotubes, on which CO2 hydration takes place. CMNT follows Michaelis–Menten kinetics with a catalytic activity (kcat/KM) of 8.2 M–1 s–1 at pH 7.5, comparable to those of other CA-mimetic catalysts. Remarkably, CMNT maintains its catalytic activity at 70 °C, a temperature that destabilizes CA. Sequestration of CO2 into calcites was demonstrated with extensive characterization of CMNT and catalytic activity. Moreover, the CMNT-integrated membranes could be applied to continuous CO2 hydration. This work underlines the straightforward preparation of a CA-mimetic catalyst using an established technique, offering the potential for future modification or incorporation of additional catalytic functions.

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Publication Details

Journal
ACS Sustainable Chemistry & Engineering
Published
2024-08-23
DOI
https://doi.org/10.1021/acssuschemeng.4c00659
Citations
7
Primary Topic
Enzyme function and inhibition
Type
article
Field-Weighted Citation Impact
1.64

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article

Catalytic CO2 Hydration and Sequestration by Carbonic Anhydrase-Mimetic Nanotubes

Ye Won Kim, Sang‐Yup Lee, Min‐Chul Kim, Hyesung Lee et al.
7 citations
ACS Sustainable Chemistry & Engineering
Enzyme function and inhibition
1.64
article

Catalytic CO2 Hydration and Sequestration by Carbonic Anhydrase-Mimetic Nanotubes

Ye Won Kim, Sang‐Yup Lee, Min‐Chul Kim, Hyesung Lee, Minji Kim
article en
7 citations

Abstract

Promotion of the conversion of CO2 into HCO3– is necessary for the efficient sequestration of CO2 into metal carbonate minerals, a promising CO2 utilization strategy. Carbonic anhydrase (CA), a ubiquitous enzyme, exhibits high activity in CO2 hydration and suffers from inherent instability as a biological disadvantage. Consequently, there is a demand for a CA-mimetic catalyst that is stable at high temperatures and can be easily prepared. In this study, we have developed a new CA-mimetic nanotube (CMNT) catalyst, demonstrating remarkable catalytic activity in CO2 hydration. The CMNT catalyst is easily prepared by the layer-by-layer (LbL) method, which involves the sequential infusion of polyelectrolyte and polypeptide solutions into a track-etched polymeric membrane. Multiple catalytic Zn-histidyl imidazole complexes were built on the inner channel of nanotubes, on which CO2 hydration takes place. CMNT follows Michaelis–Menten kinetics with a catalytic activity (kcat/KM) of 8.2 M–1 s–1 at pH 7.5, comparable to those of other CA-mimetic catalysts. Remarkably, CMNT maintains its catalytic activity at 70 °C, a temperature that destabilizes CA. Sequestration of CO2 into calcites was demonstrated with extensive characterization of CMNT and catalytic activity. Moreover, the CMNT-integrated membranes could be applied to continuous CO2 hydration. This work underlines the straightforward preparation of a CA-mimetic catalyst using an established technique, offering the potential for future modification or incorporation of additional catalytic functions.

ACS Sustainable Chemistry & EngineeringVol. 12(36)
Yonsei University (KR), Korea Research Institute of Chemical Technology (KR)
National Research Foundation of Korea
Openalex Percentile: Top 16%
Enzyme function and inhibition
1.64
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