Evidence map›Paper›PMID 32497077›Full record

ArticlePloS one2020

Tree bark scrape fungus: A potential source of laccase for application in bioremediation of non-textile dyes.

R Z Sayyed, H M Bhamare, Sapna, Najat Marraiki, Abdallah M Elgorban, Asad Syed, Hesham Ali El-Enshasy, Daniel J Dailin

RetractedErratum issuedOpen access · goldAbstract readRetracted Publication
In one paragraph

Article in PloS one, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
4.2field-weighted citation impact, top 7% 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

7 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Purification and characterisation of new laccase fromBiotechnology reports (Amsterdam, Netherlands) · 2020
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 5 institutions in 4 countries.

R Z SayyedDepartment of Microbiology, PSGVP Mandal's Arts, Science and Commerce College, Shahada, India.ORCID 0000-0002-1553-1213
H M BhamareDepartment of Biotechnology, SSVP Sansth's Late Karmveer Dr. P. R. Ghogrey Science College, Dhule, India.
SapnaICAR-National Bureau of Plant Genetic Resources, New Delhi, India.
Najat MarraikiDepartment of Botany and Microbiology, College of Science, King Saud University, Riyadh, Saudi Arabia.
Abdallah M ElgorbanDepartment of Botany and Microbiology, College of Science, King Saud University, Riyadh, Saudi Arabia.
Asad SyedDepartment of Botany and Microbiology, College of Science, King Saud University, Riyadh, Saudi Arabia.
Hesham Ali El-EnshasyInstitute of Bioproduct Development, Universiti Teknologi Malaysia (UTM), Skudai, Johor Bahru, Malaysia.
Daniel J DailinInstitute of Bioproduct Development, Universiti Teknologi Malaysia (UTM), Skudai, Johor Bahru, Malaysia.
King Saud University · SACity of Scientific Research and Technological Applications · EGG.S. Science, Arts And Commerce College · INNational Bureau of Plant Genetic Resources · INUniversity of Technology Malaysia · MY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although laccase has been recognized as a wonder molecule and green enzyme, the use of low yielding fungal strains, poor production, purification, and low enzyme kinetics have hampered its large-scale application. Thus,this study aims to select high yielding fungal strains and optimize the production, purification, and kinetics of laccase of Aspergillus sp. HB_RZ4. The results obtained indicated that Aspergillus sp. HB_RZ4 produced a significantly large amount of laccase under meso-acidophilic shaking conditions in a medium containing glucose and yeast extract. A 25 μM CuSO4 was observed to enhance the enzyme yield. The enzyme was best purified on a Sephadex G-100 column. The purified enzyme resembled laccase of A. flavus. The kinetics of the purified enzyme revealed high substrate specificity and good velocity of reaction,using ABTS as a substrate. The enzyme was observed to be stable over various pH values and temperatures. The peptide structure of the purified enzyme was found to resemble laccase of A. kawachii IFO 4308. The fungus was observed to decolorize various dyes independent of the requirement of a laccase mediator system.Aspergillus sp. HB_RZ4 was observed to be a potent natural producer of laccase, and it decolorized the dyes even in the absence of a laccase mediator system. Thus, it can be used for bioremediation of effluent that contains non-textile dyes.

Indexed as

AspergillusBiodegradation, EnvironmentalBiotechnologyColoring AgentsEnzyme ActivationEnzyme InhibitorsEnzymes, ImmobilizedEnzyme StabilityHydrogen-Ion ConcentrationLaccasePlant BarkColoring AgentsEnzyme InhibitorsEnzymes, ImmobilizedLaccase

Identifiers

PMID32497077
PMCPMC7272029
OpenAlexW3033515501

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.