Evidence map›Paper›PMID 33134747›Full record

ReviewAIMS microbiology2020

Breakthroughs in the discovery and use of different peroxidase isoforms of microbial origin.

Pontsho Patricia Twala, Alfred Mitema, Cindy Baburam, Naser Aliye Feto

Open access · goldAbstract readReview
In one paragraph

Review in AIMS microbiology, 2020. 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
5.1field-weighted citation impact, top 5% 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, 60 citations in OpenAlex.

  1. Article
  2. Article
  3. Asphaltene biotransformation by a novel enzyme thiol peroxidase fromApplied and environmental microbiology · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. 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

4 authors at 1 institution in 1 country.

Pontsho Patricia TwalaOMICS Research Group, Department of Biotechnology, Vaal University of Technology, Vanderbijlpark, South Africa.
Alfred MitemaOMICS Research Group, Department of Biotechnology, Vaal University of Technology, Vanderbijlpark, South Africa.
Cindy BaburamOMICS Research Group, Department of Biotechnology, Vaal University of Technology, Vanderbijlpark, South Africa.
Naser Aliye FetoOMICS Research Group, Department of Biotechnology, Vaal University of Technology, Vanderbijlpark, South Africa.
Vaal University of Technology · ZA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peroxidases are classified as oxidoreductases and are the second largest class of enzymes applied in biotechnological processes. These enzymes are used to catalyze various oxidative reactions using hydrogen peroxide and other substrates as electron donors. They are isolated from various sources such as plants, animals and microbes. Peroxidase enzymes have versatile applications in bioenergy, bioremediation, dye decolorization, humic acid degradation, paper and pulp, and textile industries. Besides, peroxidases from different sources have unique abilities to degrade a broad range of environmental pollutants such as petroleum hydrocarbons, dioxins, industrial dye effluents, herbicides and pesticides. Ironically, unlike most biological catalysts, the function of peroxidases varies according to their source. For instance, manganese peroxidase (MnP) of fungal origin is widely used for depolymerization and demethylation of lignin and bleaching of pulp. While, horseradish peroxidase of plant origin is used for removal of phenols and aromatic amines from waste waters. Microbial enzymes are believed to be more stable than enzymes of plant or animal origin. Thus, making microbially-derived peroxidases a well-sought-after biocatalysts for versatile industrial and environmental applications. Therefore, the current review article highlights on the recent breakthroughs in the discovery and use of peroxidase isoforms of microbial origin at a possible depth.

Indexed as

degradationenzymesmicrobial peroxidasesperoxidase isoformsperoxidasespollutants

Identifiers

PMID33134747
PMCPMC7595840
OpenAlexW3088276253

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.