Evidence map›Paper›PMID 24308857›Full record

ArticleBMC biochemistry2013

Soybean peroxidase-mediated degradation of an azo dye- a detailed mechanistic study.

Liaquat Ali, Rowdha Algaithi, Hosam M Habib, Usama Souka, Muhammad A Rauf, S Salman Ashraf

Open access · hybridAbstract read
In one paragraph

Article in BMC biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
4.6field-weighted citation impact, top 6% 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

11 citing papers in PubMed, 77 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

6 authors at 1 institution in 1 country.

Liaquat Ali
Rowdha Algaithi
Hosam M Habib
Usama Souka
Muhammad A Rauf
S Salman AshrafDepartment of Chemistry, College of Science, UAE University, P,O, Box 15551, Al-Ain, United Arab Emirates. salman.ashraf@uaeu.ac.ae.
United Arab Emirates University · AE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundPeroxidases are emerging as an important class of enzymes that can be used for the efficient degradation of organic pollutants. However, detailed studies identifying the various intermediates produced and the mechanisms involved in the enzyme-mediated pollutant degradation are not widely published.

resultsIn the present study, the enzymatic degradation of an azo dye (Crystal Ponceau 6R, CP6R) was studied using commercially available soybean peroxidase (SBP) enzyme. Several operational parameters affecting the enzymatic degradation of dye were evaluated and optimized, such as initial dye concentration, H2O2 dosage, mediator amount and pH of the solution. Under optimized conditions, 40 ppm dye solution could be completely degraded in under one minute by SBP in the presence of H2O2 and a redox mediator. Dye degradation was also confirmed using HPLC and TOC analyses, which showed that most of the dye was being mineralized to CO2 in the process.

conclusionsDetailed analysis of metabolites, based on LC/MS results, showed that the enzyme-based degradation of the CP6R dye proceeded in two different reaction pathways- via symmetric azo bond cleavage as well as asymmetric azo bond breakage in the dye molecule. In addition, various critical transformative and oxidative steps such as deamination, desulfonation, keto-oxidation are explained on an electronic level. Furthermore, LC/MS/MS analyses confirmed that the end products in both pathways were small chain aliphatic carboxylic acids.

Indexed as

Azo CompoundsCarbon DioxideChromatography, High Pressure LiquidColoring AgentsGlycine maxHydrogen-Ion ConcentrationHydrogen PeroxideMass SpectrometryOxidation-ReductionPeroxidaseAzo CompoundsCarbon DioxideColoring AgentsHydrogen PeroxidePeroxidaseponceau 6R

Identifiers

PMID24308857
PMCPMC4028748
OpenAlexW2133500248

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.