Evidence map›Paper›PMID 35507234›Full record

ArticleMarine biotechnology (New York, N.Y.)2022

Production of a Novel Marine Pseudomonas aeruginosa Recombinant L-Asparaginase: Insight on the Structure and Biochemical Characterization.

Fatemeh Izadpanah Qeshmi, Ahmad Homaei, Khosro Khajeh, Ehsan Kamrani, Pedro Fernandes

Abstract read
PubMed Publisher
In one paragraph

Article in Marine biotechnology (New York, N.Y.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
10.6field-weighted citation impact, top 1% 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

15 citing papers in PubMed, 55 citations in OpenAlex.

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  12. Characterization of a Novel FeInternational journal of molecular sciences · 2022
    Article
  13. Enhancing the Catalytic Activity of Type II L-Asparaginase fromInternational journal of molecular sciences · 2022
    Article
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  15. Article
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 3 institutions in 2 countries.

Fatemeh Izadpanah QeshmiDepartment of Marine Biology, Faculty of Marine Science and Technology, University of Hormozgan, P.O. Box 3995, Bandar Abbas, Iran.
Ahmad HomaeiDepartment of Marine Biology, Faculty of Marine Science and Technology, University of Hormozgan, P.O. Box 3995, Bandar Abbas, Iran. a.homaei@hormozgan.ac.ir.ORCID https://orcid.org/0000-0003-4310-0637
Khosro KhajehDepartment of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran.
Ehsan KamraniFisheries Department, Faculty of Marine Science and Technology, University of Hormozgan, Bandar Abbas, Iran.
Pedro FernandesDepartment of Bioengineering and IBB-Institute for Bioengineering and Biosciences, Instituto Superior Técnico, Universidade de Lisboa, Av. Rovisco Pais, 1049-001, Lisbon, Portugal.
University of Hormozgan · IRTarbiat Modares University · IRUniversity of Lisbon · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The present study focused on the cloning, expression, and characterization of L-asparaginase of marine Pseudomonas aeruginosa HR03 isolated from fish intestine. Thus, a gene fragment containing the L-asparaginase sequence of Pseudomonas aeruginosa HR03 isolated from the fish intestine was cloned in the pET21a vector and then expressed in Escherichia coli BL21 (DE3) cells. Thereafter, the recombinant L-asparaginase (HR03Asnase) was purified by nickel affinity chromatography, and the enzymatic properties of HR03Asnase, including the effects of pH and temperature on HR03Asnase activity and its kinetic parameters, were determined. The recombinant enzyme HR03Asnase showed the highest similarity to type I L-asparaginase from Pseudomonas aeruginosa. The three-dimensional (3D) modeling results indicate that HR03Asnase exists as a homotetramer. Its molecular weight was 35 kDa, and the maximum activity of the purified enzyme was observed at pH8 and at 40 °C. The k

Indexed as

AsparaginasePseudomonas aeruginosaAnimalsAsparagineEnzyme StabilityEscherichia coliHydrogen-Ion ConcentrationKineticsRecombinant ProteinsAsparaginaseAsparagineRecombinant ProteinsAcrylamideCloningE. coliEnzyme activityPurification

Identifiers

PMID35507234
OpenAlexW4229062908

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.