Evidence map›Paper›PMID 32298310›Full record

ArticlePloS one2020

Laccase activity of the ascomycete fungus Nectriella pironii and innovative strategies for its production on leaf litter of an urban park.

Aleksandra Góralczyk-Bińkowska, Anna Jasińska, Andrzej Długoński, Przemysław Płociński, Jerzy Długoński

Erratum issuedOpen access · goldAbstract read
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. An erratum has been issued. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
7.9field-weighted citation impact, top 3% 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

16 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Laccase Production Optimization from RecombinantMolecules (Basel, Switzerland) · 2024
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  6. Article
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  9. Review
  10. Review
  11. Article
  12. Article
  13. Bisphenol A Removal by the FungusInternational journal of molecular sciences · 2021
    Article
  14. Article
  15. Biodegradation of Chloroxylenol byInternational journal of molecular sciences · 2021
    Article
  16. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Aleksandra Góralczyk-BińkowskaDepartment of Industrial Microbiology and Biotechnology, Faculty of Biology and Environmental Protection, University of Lodz, Lodz, Poland.
Anna JasińskaDepartment of Industrial Microbiology and Biotechnology, Faculty of Biology and Environmental Protection, University of Lodz, Lodz, Poland.
Andrzej DługońskiDepartment of Environmental Engineering, Faculty of Biology and Environmental Sciences, Cardinal Stefan Wyszynski University in Warsaw, Warsaw, Poland.
Przemysław PłocińskiInstitute of Medical Biology of Polish Academy of Sciences, Lodz, Poland.
Jerzy DługońskiDepartment of Industrial Microbiology and Biotechnology, Faculty of Biology and Environmental Protection, University of Lodz, Lodz, Poland.ORCID 0000-0002-2075-5967
University of Łódź · PLCardinal Stefan Wyszynski University in Warsaw · PLInstitute for Medical Biology · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A laccase-producing ascomycete fungus was isolated from soil collected around the premises of a textile dye factory and identified as Nectriella pironii. Efficient laccase production was achieved via the synergistic action of 1 mM copper sulfate and ferulic acid. Extracts of rapeseed oil cake, grass hay, and leaf litter collected in a pocket urban park were used for enzyme production. The highest laccase activity (3,330 U/L) was observed in the culture grown on the leaf litter extract. This is the first report on biosynthesis of laccase by N. pironii. This is also the first study on utilization of naturally fallen park leaves as a substrate for fungal laccase production. The extracellular enzyme possessing laccase activity was purified to homogeneity by ion-exchange and gel filtration chromatographic techniques. The amino acid sequence of the protein revealed highest similarity to the laccase enzyme produced by Stachybotrys chartarum-and considerable homology to those produced by other fungal species. The purified laccase possessed a molecular mass of 50 kDa. The enzyme had an optimum pH of 2.0 or 6.0 and retained more than 50% of residual activity after 3 hours of incubation at pH 3.0-10.6 or 4.0-9.0 when 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid or 2,6-dimethoxyphenol, respectively, were used. Dithiothreitol, β-mercaptoethanol, and sodium azide at 1 mM concentration strongly inhibited the laccase activity, while in the presence of 50 mM urea, the enzyme was found to retain 25% of its activity. The laccase was able to decolorize more than 80% of Indigo Carmine, Remazol Brilliant Blue R, Reactive Orange 16, and Acid Red 27 dyes within 1 h. The possibility of leaf litter use for the production of the laccase enzyme from N. pironii (IM 6443), exhibiting high pH stability and degradative potential, makes it a promising tool for use in different environmental and industrial operations.

Indexed as

Parks, RecreationalAscomycotaLaccasePlant LeavesSoil MicrobiologyLaccase

Identifiers

PMID32298310
PMCPMC7162450
OpenAlexW3016661042

What OpenQuestion holds

Textmetadata
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.