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Thermostable Carbonic Anhydrases in Biotechnological Applications

Carbonic anhydrases are ubiquitous metallo-enzymes which catalyze the reversible hydration of carbon dioxide in bicarbonate ions and protons. Recent years have seen an increasing interest in the utilization of these enzymes in CO(2) capture and storage processes. However, since this use is greatly l...

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Autores principales: Di Fiore, Anna, Alterio, Vincenzo, Monti, Simona M., De Simone, Giuseppina, D’Ambrosio, Katia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4519908/
https://www.ncbi.nlm.nih.gov/pubmed/26184158
http://dx.doi.org/10.3390/ijms160715456
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author Di Fiore, Anna
Alterio, Vincenzo
Monti, Simona M.
De Simone, Giuseppina
D’Ambrosio, Katia
author_facet Di Fiore, Anna
Alterio, Vincenzo
Monti, Simona M.
De Simone, Giuseppina
D’Ambrosio, Katia
author_sort Di Fiore, Anna
collection PubMed
description Carbonic anhydrases are ubiquitous metallo-enzymes which catalyze the reversible hydration of carbon dioxide in bicarbonate ions and protons. Recent years have seen an increasing interest in the utilization of these enzymes in CO(2) capture and storage processes. However, since this use is greatly limited by the harsh conditions required in these processes, the employment of thermostable enzymes, both those isolated by thermophilic organisms and those obtained by protein engineering techniques, represents an interesting possibility. In this review we will provide an extensive description of the thermostable carbonic anhydrases so far reported and the main processes in which these enzymes have found an application.
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spelling pubmed-45199082015-08-03 Thermostable Carbonic Anhydrases in Biotechnological Applications Di Fiore, Anna Alterio, Vincenzo Monti, Simona M. De Simone, Giuseppina D’Ambrosio, Katia Int J Mol Sci Review Carbonic anhydrases are ubiquitous metallo-enzymes which catalyze the reversible hydration of carbon dioxide in bicarbonate ions and protons. Recent years have seen an increasing interest in the utilization of these enzymes in CO(2) capture and storage processes. However, since this use is greatly limited by the harsh conditions required in these processes, the employment of thermostable enzymes, both those isolated by thermophilic organisms and those obtained by protein engineering techniques, represents an interesting possibility. In this review we will provide an extensive description of the thermostable carbonic anhydrases so far reported and the main processes in which these enzymes have found an application. MDPI 2015-07-08 /pmc/articles/PMC4519908/ /pubmed/26184158 http://dx.doi.org/10.3390/ijms160715456 Text en © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Di Fiore, Anna
Alterio, Vincenzo
Monti, Simona M.
De Simone, Giuseppina
D’Ambrosio, Katia
Thermostable Carbonic Anhydrases in Biotechnological Applications
title Thermostable Carbonic Anhydrases in Biotechnological Applications
title_full Thermostable Carbonic Anhydrases in Biotechnological Applications
title_fullStr Thermostable Carbonic Anhydrases in Biotechnological Applications
title_full_unstemmed Thermostable Carbonic Anhydrases in Biotechnological Applications
title_short Thermostable Carbonic Anhydrases in Biotechnological Applications
title_sort thermostable carbonic anhydrases in biotechnological applications
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4519908/
https://www.ncbi.nlm.nih.gov/pubmed/26184158
http://dx.doi.org/10.3390/ijms160715456
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