Evidence map›Paper›PMID 26475626›Full record

ArticleExtremophiles : life under extreme conditions2016

Cloning, expression and characterization of a novel cold‑adapted GDSL family esterase from Photobacterium sp. strain J15.

Mehrnoush Hadaddzadeh Shakiba, Mohd Shukuri Mohamad Ali, Raja Noor Zaliha Raja Abd Rahman, Abu Bakar Salleh, Thean Chor Leow

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Article in Extremophiles : life under extreme conditions, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

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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

18 citing papers in PubMed, 38 citations in OpenAlex.

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  10. Green Synthesis of the Flavor Esters with a MarineIndian journal of microbiology · 2020
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  11. Article
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  13. Characterization and Immobilization of a Novel SGNH Family Esterase (International journal of molecular sciences · 2019
    Article
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  18. Review
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

5 authors at 1 institution in 1 country.

Mehrnoush Hadaddzadeh ShakibaEnzyme and Microbial Technology Research Centre, Universiti Putra Malaysia, 43400 Serdang, Selangor, Malaysia. mehr_sh_2008@yahoo.com
Mohd Shukuri Mohamad Ali
Raja Noor Zaliha Raja Abd Rahman
Abu Bakar Salleh
Thean Chor Leow
Universiti Putra Malaysia · MY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The gene encoding for a novel cold-adapted enzyme from family II of bacterial classification (GDSL family) was cloned from the genomic DNA of Photobacterium sp. strain J15 in an Escherichia coli system, yielding a recombinant 36 kDa J15 GDSL esterase which was purified in two steps with a final yield and purification of 38.6 and 15.3 respectively. Characterization of the biochemical properties showed the J15 GDSL esterase had maximum activity at 20 °C and pH 8.0, was stable at 10 °C for 3 h and retained 50 % of its activity after a 6 h incubation at 10 °C. The enzyme was activated by Tween-20, -60 and Triton-X100 and inhibited by 1 mM Sodium dodecyl sulphate (SDS), while β-mercaptoethanol and Dithiothreitol (DTT) enhanced activity by 4.3 and 5.4 fold respectively. These results showed the J15 GDSL esterase was a novel cold-adapted enzyme from family II of lipolytic enzymes. A structural model constructed using autotransporter EstA from Pseudomonas aeruginosa as a template revealed the presence of a typical catalytic triad consisting of a serine, aspartate, and histidine which was verified with site directed mutagenesis on active serine.

Indexed as

AcclimatizationCold TemperatureAmino Acid SequenceBacterial ProteinsCarboxylic Ester HydrolasesEnzyme StabilityMolecular Sequence DataPhotobacteriumPhylogenyBacterial ProteinsCarboxylic Ester Hydrolases

Identifiers

PMID26475626
OpenAlexW2111470314

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Registered trials

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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.