Evidence map›Paper›PMID 33794981›Full record

ArticleBiotechnology for biofuels2021

Discovery of two novel laccase-like multicopper oxidases from Pleurotus citrinopileatus and their application in phenolic oligomer synthesis.

A Zerva, C Pentari, A Termentzi, A H P America, D Zouraris, S K Bhattacharya, A Karantonis, G I Zervakis, E Topakas

Abstract read
In one paragraph

Article in Biotechnology for biofuels, 2021. 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. Genomic, Proteomic, and Biochemical Study ofJournal of agricultural and food chemistry · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Role and structure of the small subunit forming heterodimers with laccase-like enzymes.Protein science : a publication of the Protein Society · 2023
    Article
  8. Transcriptomic Analysis of Acetaminophen Biodegradation byJournal of fungi (Basel, Switzerland) · 2023
    Article
  9. 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

9 authors.

A ZervaIndustrial Biotechnology & Biocatalysis Group, Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens, 5 Iroon Polytechniou Str, Zografou Campus, Athens, Greece.
C PentariIndustrial Biotechnology & Biocatalysis Group, Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens, 5 Iroon Polytechniou Str, Zografou Campus, Athens, Greece.
A TermentziDepartment of Ophthalmology/Bascom Palmer Eye Institute, University of Miami, Miami, FL, 33136, USA.
A H P AmericaWageningen Plant Research, Wageningen University and Research, Wageningen, The Netherlands.
D ZourarisLaboratory of Physical Chemistry and Applied Electrochemistry, School of Chemical Engineering, National Technical University of Athens, Zografou, Athens, Greece.
S K BhattacharyaDepartment of Ophthalmology/Bascom Palmer Eye Institute, University of Miami, Miami, FL, 33136, USA.
A KarantonisLaboratory of Physical Chemistry and Applied Electrochemistry, School of Chemical Engineering, National Technical University of Athens, Zografou, Athens, Greece.
G I ZervakisLaboratory of General and Agricultural Microbiology, Agricultural University of Athens, Athens, Greece.
E TopakasIndustrial Biotechnology & Biocatalysis Group, Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens, 5 Iroon Polytechniou Str, Zografou Campus, Athens, Greece. vtopakas@chemeng.ntua.gr.ORCID http://orcid.org/0000-0003-0078-5904

Funding

European Regional Development Fund 5002550
6 · The paper itself

Abstract

backgroundLaccases and laccase-like multicopper oxidases (LMCOs) oxidize a vast array of phenolic compounds and amines, releasing water as a byproduct. Their low substrate specificity is responsible for their tremendous biotechnological interest, since they have been used for numerous applications. However, the laccases characterized so far correspond to only a small fraction of the laccase genes identified in fungal genomes. Therefore, the knowledge regarding the biochemistry and physiological role of minor laccase-like isoforms is still limited.

resultsIn the present work, we describe the isolation, purification and characterization of two novel LMCOs, PcLac1 and PcLac2, from Pleurotus citrinopileatus. Both LMCOs were purified with ion-exchange chromatographic methods. PcLac2 was found to oxidize a broader substrate range than PcLac1, but both LMCOs showed similar formal potentials, lower than those reported previously for laccases from white-rot fungi. Proteomic analysis of both proteins revealed their similarity with other well-characterized laccases from Pleurotus strains. Both LMCOs were applied to the oxidation of ferulic and sinapic acid, yielding oligomers with possible antioxidant activity.

conclusionsOverall, the findings of the present work can offer new insights regarding the biochemistry and variability of low-redox potential laccases of fungal origin. Low-redox potential biocatalysts could offer higher substrate selectivity than their high-redox counterparts, and thus, they could be of applied value in the field of biocatalysis.

Indexed as

BiocatalysisLaccase-like multicopper oxidasesPhenol oligomers

Identifiers

PMID33794981
PMCPMC8017616

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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.