Evidence map›Paper›PMID 39753629›Full record

ArticleScientific reports2025

Characterization and evaluation of the immobilized laccase enzyme potential in dye degradation via one factor and response surface methodology approaches.

Abdelmageed M Othman, Angelina G Flaifil

Abstract read
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Immobilized CuClPhotochemistry and photobiology
    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

2 authors.

Abdelmageed M OthmanMicrobial Chemistry Department, Biotechnology Research Institute, National Research Centre, Dokki, Giza, 12622, Egypt. othmanam_nrc@yahoo.com.
Angelina G FlaifilFaculty of Biotechnology, German International University, Regional Ring Road, East Cairo, New Administrative Capital, Cairo, Egypt.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the current study, calcium alginate was used as a carrier for Agaricus bisporus CU13 laccase immobilization, with an immobilization yield of the entrapped laccase of 91.95%. Free and immobilized enzymes showed their best enzyme activity at 60 °C as an optimum temperature. Free laccase was nearly completely inactivated at high temperatures (70 and 80 °C C) after 30 min, whereas the immobilized form retained around 60 and 40% of its activity after 30 min at the same temperatures. The metal ion of MgSO

Indexed as

Coloring AgentsEnzymes, ImmobilizedLaccaseAgaricusAlginatesEnzyme StabilityHydrogen-Ion ConcentrationTemperatureAlginatesColoring AgentsEnzymes, ImmobilizedLaccaseDegradationEnvironmental biotechnologyImmobilizationLaccasePollutants

Identifiers

PMID39753629
PMCPMC11699123

What OpenQuestion holds

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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.