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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...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2015
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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. |
format | Online Article Text |
id | pubmed-4519908 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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