Evidence map›Paper›PMID 26868129›Full record

ArticleBMC biotechnology2016

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

Sarah A Sonbol, Ari J S Ferreira, Rania Siam

Open access · goldAbstract read
In one paragraph

Article in BMC biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
3.4field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 23 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Sarah A SonbolBiology Department and YJ-Science and Technology Research Center, American University in Cairo, New Cairo, 11835, Egypt. sasonbol@aucegypt.edu.
Ari J S FerreiraBiology Department and YJ-Science and Technology Research Center, American University in Cairo, New Cairo, 11835, Egypt. ariferreira@aucegypt.edu.
Rania SiamBiology Department and YJ-Science and Technology Research Center, American University in Cairo, New Cairo, 11835, Egypt. rsiam@aucegypt.edu.
American University in Cairo · EG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundNitrilases, 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.

resultsWe 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.

conclusionThis 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.

Indexed as

Amino Acid SequenceAminohydrolasesBacteriaBacterial ProteinsEnzyme StabilityHot TemperatureHydrogen-Ion ConcentrationIndian OceanMetagenomeMetagenomicsMetals, HeavyModels, MolecularWater MicrobiologyAminohydrolasesBacterial ProteinsMetals, Heavynitrilase

Identifiers

PMID26868129
PMCPMC4751646
OpenAlexW2264411329

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.