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具有独特热稳定性和重金属耐受性的红海亚特兰蒂斯二号盐水池腈水解酶。

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

作者信息

Sonbol Sarah A, Ferreira Ari J S, Siam Rania

机构信息

Biology Department and YJ-Science and Technology Research Center, American University in Cairo, New Cairo, 11835, Egypt.

出版信息

BMC Biotechnol. 2016 Feb 11;16:14. doi: 10.1186/s12896-016-0244-2.

DOI:10.1186/s12896-016-0244-2
PMID:26868129
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4751646/
Abstract

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.

摘要

背景

腈水解酶可将腈类化合物一步水解为羧酸和氨，由于自然界中腈类化合物丰富，且其在精细化学品和制药领域有应用，因此受到越来越多关注。极端环境是分离和鉴定包括具有独特抗性的腈水解酶在内的极端酶的潜在栖息地。红海盐水池具有多种极端条件。红海亚特兰蒂斯二号深盐水池的下部对流层（LCL）具有温度升高（68°C）、高盐浓度（250‰）、缺氧条件和高重金属浓度的特点。

结果

我们从红海LCL的亚特兰蒂斯二号深盐水池中鉴定并分离出一种腈水解酶。分离得到的338个氨基酸的腈水解酶（NitraS-ATII）是不同细菌门类中一个高度保守操纵子的一部分，功能不明。该酶被克隆、表达并纯化。对纯化后的NitraS-ATII的表征揭示了其对二腈的选择性，这表明其在氰基羧酸合成中可能具有工业应用价值。此外，与一种密切相关的腈水解酶相比，NitraS-ATII表现出更高的热稳定性，同时还观察到它对高浓度选定重金属具有耐受性。

结论

这种酶揭示了亚特兰蒂斯二号深LCL中微生物为适应多样极端环境而发生的进化，并且在生物修复过程中可能具有重要价值。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75eb/4751646/748641158718/12896_2016_244_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75eb/4751646/ffdf6c781eb3/12896_2016_244_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75eb/4751646/f59c82be7ad0/12896_2016_244_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75eb/4751646/a895cd173350/12896_2016_244_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75eb/4751646/f57742b2c11e/12896_2016_244_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75eb/4751646/1c9584f23605/12896_2016_244_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75eb/4751646/77afbc317168/12896_2016_244_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75eb/4751646/748641158718/12896_2016_244_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75eb/4751646/ffdf6c781eb3/12896_2016_244_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75eb/4751646/f59c82be7ad0/12896_2016_244_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75eb/4751646/a895cd173350/12896_2016_244_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75eb/4751646/f57742b2c11e/12896_2016_244_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75eb/4751646/1c9584f23605/12896_2016_244_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75eb/4751646/77afbc317168/12896_2016_244_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75eb/4751646/748641158718/12896_2016_244_Fig7_HTML.jpg

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