Evidence map›Paper›PMID 42557301›Full record

ArticleScientific reports2026

Recombinant DyP peroxidases for green synthesis and characterization of poly(pyrogallol).

Marina Refaat, Khaled O Sebakhy, Menna-T-Allah M Saad, Marwa ElRakaiby, Mohamed H Habib, Maha M Ismail

Abstract read
In one paragraph

Article in Scientific reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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

6 authors.

Marina Refaat *Department of Microbiology and Immunology, Faculty of Pharmacy, Cairo University, Kasr El-Aini, Cairo, 11562, Egypt.
Khaled O Sebakhy *Chemical and Industrial Processes Engineering, Faculty of Engineering, Bahrain Polytechnic, Isa Town, Kingdom of Bahrain.
Menna-T-Allah M SaadDepartment of Microbiology and Immunology, Faculty of Pharmacy, Cairo University, Kasr El-Aini, Cairo, 11562, Egypt.
Marwa ElRakaibyDepartment of Microbiology and Immunology, Faculty of Pharmacy, Cairo University, Kasr El-Aini, Cairo, 11562, Egypt.
Mohamed H HabibDepartment of Microbiology and Immunology, Faculty of Pharmacy, Cairo University, Kasr El-Aini, Cairo, 11562, Egypt. mohamed.habib@pharma.cu.edu.eg.ORCID 0000-0002-3732-5963
Maha M IsmailDepartment of Microbiology and Immunology, Faculty of Pharmacy, Cairo University, Kasr El-Aini, Cairo, 11562, Egypt.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phenolic compounds pose a major threat to water pollution due to their high toxicity. Enzymes have emerged over recent years to act as a green alternative for cleaning up and utilizing phenolic compounds in nature. DyP peroxidases, a member of the oxidoreductase family, have shown promising ability to convert dyes into harmless compounds and have been found indispensable tools for green polymerization. In this study, three recombinant DyP peroxidases were used to convert pyrogallol (PG) into a polymer which upon characterization using Fourier-transform infrared spectroscopy (FT-IR), Raman spectroscopy, powder X-ray diffraction (XRD) and scanning electron microscopy (SEM) have revealed intricate details characteristic of poly(pyrogallol) (PPG). The synthesized polymer showed a rigid structure, with potential use in material science applications such as coatings or binding agents, as well as broader aspects in environmental and biomedical research.

Indexed as

Green Chemistry TechnologyPeroxidasesPolymersPyrogallolMicroscopy, Electron, ScanningPolymerizationRecombinant ProteinsSpectroscopy, Fourier Transform InfraredX-Ray DiffractionPeroxidasesPolymersPyrogallolRecombinant ProteinsConjugated polymersDyP-peroxidasesGreen polymerizationPolymer characterizationPyrogallol

Identifiers

PMID42557301
PMCPMC13443537

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