Electropolymerized Carbonic Anhydrase Immobilization for Carbon Dioxide Capture
Biomimetic carbonation carried out with carbonic anhydrase (CA) in CO2-absorbing solutions, such as methyldiethanolamine (MDEA), is one approach that has been developed to accelerate the capture of CO2. However, there are several practical issues, such as high cost and limited enzyme stability, that...
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Veröffentlicht in: | Langmuir 2014-06, Vol.30 (23), p.6915-6919 |
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description | Biomimetic carbonation carried out with carbonic anhydrase (CA) in CO2-absorbing solutions, such as methyldiethanolamine (MDEA), is one approach that has been developed to accelerate the capture of CO2. However, there are several practical issues, such as high cost and limited enzyme stability, that need to be overcome. In this study, the capacity of CA immobilization on a porous solid support was studied to improve the instability in the tertiary amine solvent. We have shown that a 63% porosity macroporous carbon foam support makes separation and reuse facile and allows for an efficient supply and presentation of CO2 to an aqueous solvent and the enzyme catalytic center. These enzymatic supports conserved 40% of their initial activity after 42 days at 70 °C in an amine solvent, whereas the free enzyme shows no activity after 1 h in the same conditions. In this work, we have overcome the technical barrier associated with the recovery of the biocatalyst after operation, and most of all, these electropolymerized enzymatic supports have shown a remarkable increase of thermal stability in an amine-based CO2 sequestration solvent. |
doi_str_mv | 10.1021/la501333s |
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However, there are several practical issues, such as high cost and limited enzyme stability, that need to be overcome. In this study, the capacity of CA immobilization on a porous solid support was studied to improve the instability in the tertiary amine solvent. We have shown that a 63% porosity macroporous carbon foam support makes separation and reuse facile and allows for an efficient supply and presentation of CO2 to an aqueous solvent and the enzyme catalytic center. These enzymatic supports conserved 40% of their initial activity after 42 days at 70 °C in an amine solvent, whereas the free enzyme shows no activity after 1 h in the same conditions. 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However, there are several practical issues, such as high cost and limited enzyme stability, that need to be overcome. In this study, the capacity of CA immobilization on a porous solid support was studied to improve the instability in the tertiary amine solvent. We have shown that a 63% porosity macroporous carbon foam support makes separation and reuse facile and allows for an efficient supply and presentation of CO2 to an aqueous solvent and the enzyme catalytic center. These enzymatic supports conserved 40% of their initial activity after 42 days at 70 °C in an amine solvent, whereas the free enzyme shows no activity after 1 h in the same conditions. In this work, we have overcome the technical barrier associated with the recovery of the biocatalyst after operation, and most of all, these electropolymerized enzymatic supports have shown a remarkable increase of thermal stability in an amine-based CO2 sequestration solvent.</description><subject>Carbon Dioxide - chemistry</subject><subject>Carbonic Anhydrases - chemistry</subject><subject>Carbonic Anhydrases - metabolism</subject><subject>Enzymes, Immobilized - chemistry</subject><subject>Ethanolamines - chemistry</subject><issn>0743-7463</issn><issn>1520-5827</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0E9LwzAYBvAgipvTg19AehH0UM2fpkmPY04dDHbRc0jTt5iRNjVpwe3TW9n05OnlhR8PPA9C1wQ_EEzJo9McE8ZYPEFTwilOuaTiFE2xyFgqspxN0EWMW4xxwbLiHE1oJnkuJJ6izdKB6YPvvNs1EOweqmShQ-lba5J5-7Grgo6QrJrGl9bZve6tb5Pah6NKnqz_shWMb9cPAS7RWa1dhKvjnaH35-Xb4jVdb15Wi_k61UySPuWClzWnBqjgoIk0JeeVpkVd5lTWBZFEZ0LnktLKkAI0lMwYgLEWM0JKymbo7pDbBf85QOxVY6MB53QLfoiKcCaIEJkoRnp_oCb4GAPUqgu20WGnCFY_-6m__UZ7c4wdygaqP_k72AhuD0CbqLZ-CO3Y8p-gb0lcd5M</recordid><startdate>20140617</startdate><enddate>20140617</enddate><creator>Merle, Geraldine</creator><creator>Fradette, Sylvie</creator><creator>Madore, Eric</creator><creator>Barralet, Jake E</creator><general>American Chemical Society</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20140617</creationdate><title>Electropolymerized Carbonic Anhydrase Immobilization for Carbon Dioxide Capture</title><author>Merle, Geraldine ; Fradette, Sylvie ; Madore, Eric ; Barralet, Jake E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a381t-575bf52ce275ea18cb55da29fb628f9181a47a6822dc19eaeb3ccee8273c78823</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Carbon Dioxide - chemistry</topic><topic>Carbonic Anhydrases - chemistry</topic><topic>Carbonic Anhydrases - metabolism</topic><topic>Enzymes, Immobilized - chemistry</topic><topic>Ethanolamines - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Merle, Geraldine</creatorcontrib><creatorcontrib>Fradette, Sylvie</creatorcontrib><creatorcontrib>Madore, Eric</creatorcontrib><creatorcontrib>Barralet, Jake E</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Langmuir</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Merle, Geraldine</au><au>Fradette, Sylvie</au><au>Madore, Eric</au><au>Barralet, Jake E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Electropolymerized Carbonic Anhydrase Immobilization for Carbon Dioxide Capture</atitle><jtitle>Langmuir</jtitle><addtitle>Langmuir</addtitle><date>2014-06-17</date><risdate>2014</risdate><volume>30</volume><issue>23</issue><spage>6915</spage><epage>6919</epage><pages>6915-6919</pages><issn>0743-7463</issn><eissn>1520-5827</eissn><abstract>Biomimetic carbonation carried out with carbonic anhydrase (CA) in CO2-absorbing solutions, such as methyldiethanolamine (MDEA), is one approach that has been developed to accelerate the capture of CO2. 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subjects | Carbon Dioxide - chemistry Carbonic Anhydrases - chemistry Carbonic Anhydrases - metabolism Enzymes, Immobilized - chemistry Ethanolamines - chemistry |
title | Electropolymerized Carbonic Anhydrase Immobilization for Carbon Dioxide Capture |
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