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Red Sea Atlantis II brine pool nitrilase with unique thermostability profile and heavy metal tolerance

BACKGROUND: Nitrilases, which hydrolyze nitriles in a one-step reaction into carboxylic acids and ammonia, gained increasing attention because of the abundance of nitrile compounds in nature and their use in fine chemicals and pharmaceutics. Extreme environments are potential habitats for the isolat...

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Autores principales: Sonbol, Sarah A., Ferreira, Ari J. S., Siam, Rania
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4751646/
https://www.ncbi.nlm.nih.gov/pubmed/26868129
http://dx.doi.org/10.1186/s12896-016-0244-2
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author Sonbol, Sarah A.
Ferreira, Ari J. S.
Siam, Rania
author_facet Sonbol, Sarah A.
Ferreira, Ari J. S.
Siam, Rania
author_sort Sonbol, Sarah A.
collection PubMed
description BACKGROUND: Nitrilases, which hydrolyze nitriles in a one-step reaction into carboxylic acids and ammonia, gained increasing attention because of the abundance of nitrile compounds in nature and their use in fine chemicals and pharmaceutics. Extreme environments are potential habitats for the isolation and characterization of extremozymes including nitrilases with unique resistant properties. The Red Sea brine pools are characterized by multitude of extreme conditions. The Lower Convective Layer (LCL) of the Atlantis II Deep Brine Pool in the Red Sea is characterized by elevated temperature (68 °C), high salt concentrations (250 ‰), anoxic conditions and high heavy metal concentrations. RESULTS: We identified and isolated a nitrilase from the Atlantis II Deep Brine Pool in the Red Sea LCL. The isolated 338 amino-acid nitrilase (NitraS-ATII) is part of a highly conserved operon in different bacterial phyla with indiscernible function. The enzyme was cloned, expressed and purified. Characterization of the purified NitraS-ATII revealed its selectivity towards dinitriles, which suggests a possible industrial application in the synthesis of cyanocarboxylic acids. Moreover, NitraS-ATII showed higher thermal stability compared to a closely related nitrilase, in addition to its observed tolerance towards high concentrations of selected heavy metals. CONCLUSION: This enzyme sheds light on evolution of microbes in the Atlantis II Deep LCL to adapt to the diverse extreme environment and can prove to be valuable in bioremediation processes. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12896-016-0244-2) contains supplementary material, which is available to authorized users.
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spelling pubmed-47516462016-02-13 Red Sea Atlantis II brine pool nitrilase with unique thermostability profile and heavy metal tolerance Sonbol, Sarah A. Ferreira, Ari J. S. Siam, Rania BMC Biotechnol Research Article BACKGROUND: Nitrilases, which hydrolyze nitriles in a one-step reaction into carboxylic acids and ammonia, gained increasing attention because of the abundance of nitrile compounds in nature and their use in fine chemicals and pharmaceutics. Extreme environments are potential habitats for the isolation and characterization of extremozymes including nitrilases with unique resistant properties. The Red Sea brine pools are characterized by multitude of extreme conditions. The Lower Convective Layer (LCL) of the Atlantis II Deep Brine Pool in the Red Sea is characterized by elevated temperature (68 °C), high salt concentrations (250 ‰), anoxic conditions and high heavy metal concentrations. RESULTS: We identified and isolated a nitrilase from the Atlantis II Deep Brine Pool in the Red Sea LCL. The isolated 338 amino-acid nitrilase (NitraS-ATII) is part of a highly conserved operon in different bacterial phyla with indiscernible function. The enzyme was cloned, expressed and purified. Characterization of the purified NitraS-ATII revealed its selectivity towards dinitriles, which suggests a possible industrial application in the synthesis of cyanocarboxylic acids. Moreover, NitraS-ATII showed higher thermal stability compared to a closely related nitrilase, in addition to its observed tolerance towards high concentrations of selected heavy metals. CONCLUSION: This enzyme sheds light on evolution of microbes in the Atlantis II Deep LCL to adapt to the diverse extreme environment and can prove to be valuable in bioremediation processes. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12896-016-0244-2) contains supplementary material, which is available to authorized users. BioMed Central 2016-02-11 /pmc/articles/PMC4751646/ /pubmed/26868129 http://dx.doi.org/10.1186/s12896-016-0244-2 Text en © Sonbol et al. 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research Article
Sonbol, Sarah A.
Ferreira, Ari J. S.
Siam, Rania
Red Sea Atlantis II brine pool nitrilase with unique thermostability profile and heavy metal tolerance
title Red Sea Atlantis II brine pool nitrilase with unique thermostability profile and heavy metal tolerance
title_full Red Sea Atlantis II brine pool nitrilase with unique thermostability profile and heavy metal tolerance
title_fullStr Red Sea Atlantis II brine pool nitrilase with unique thermostability profile and heavy metal tolerance
title_full_unstemmed Red Sea Atlantis II brine pool nitrilase with unique thermostability profile and heavy metal tolerance
title_short Red Sea Atlantis II brine pool nitrilase with unique thermostability profile and heavy metal tolerance
title_sort red sea atlantis ii brine pool nitrilase with unique thermostability profile and heavy metal tolerance
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4751646/
https://www.ncbi.nlm.nih.gov/pubmed/26868129
http://dx.doi.org/10.1186/s12896-016-0244-2
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