Evidence map›Paper›PMID 36798915›Full record

ArticleAdvanced biomedical research2022

Expression Optimizing of Recombinant Oxalyl-CoA Decarboxylase in

Fatemeh Abarghooi Kahaki, Seyed Mohsen Dehnavi

Open access · goldAbstract read
In one paragraph

Article in Advanced biomedical research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.3field-weighted citation impact, top 39% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

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

2 authors at 2 institutions in 1 country.

Fatemeh Abarghooi KahakiDepartment of Biotechnology, School of Advanced Technologies in Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran.
Seyed Mohsen DehnaviDepartment of Cell and Molecular Biology, Faculty of Life Sciences and Biotechnology, Shahid Beheshti University, Tehran, Iran.
Shahid Beheshti University · IRShahid Beheshti University of Medical Sciences · IR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Background: One of the most common diseases of the urinary tract is stones of this system, including kidney stones. About 70%-80% of kidney stones are calcium oxalate. Oxalyl-CoA decarboxylase is a single polypeptide included of 568 amino acids which play a key role in oxalate degradation. Materials and Methods: The aim of current study is high-level expression of oxalyl-CoA decarboxylase in Results: The obtained data showed that the highest expression was related to the terrific broth culture medium and temperature of 32°C with an inducer concentration of 1 mM. Under this situation the ultimate cells dry weight and the final oxalyl-CoA decarboxylase expression were 2.46 g/l and 36% of total protein, respectively. Then induction time was optimized in a bench bioreactor and productivity of oxalyl-CoA decarboxylase was calculated. Under optimized condition the cell density, biomass productivity and oxalyl-CoA decarboxylase concentration reached 4.02 g/l, 0.22 g/l/h, and 0.7 g/l which are one of the highest reported rates. Conclusion: This study demonstrated that high levels of oxalyl-CoA decarboxylase can be achieved by optimizing the expression conditions.

Indexed as

Escherichia colioverexpressionoxalateoxalobacter formigenesoxalyl-CoA decarboxylase

Identifiers

PMID36798915
PMCPMC9926027
OpenAlexW4312492228

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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.