Evidence map›Paper›PMID 34310858›Full record

ArticleMicrobial biotechnology2021

Depolymerization of biorefinery lignin by improved laccases of the white-rot fungus Obba rivulosa.

Janne Wallenius, Jussi Kontro, Christina Lyra, Jaana Kuuskeri, Xing Wan, Mika A Kähkönen, Irshad Baig, Paul C J Kamer, Jussi Sipilä, Miia R Mäkelä and 2 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Microbial biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

5 citing papers in PubMed, 13 citations in OpenAlex.

  1. Interfacial Properties of Surface-Modified Lignin Nanoparticles.Langmuir : the ACS journal of surfaces and colloids · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Production of Recombinant Laccase FromFrontiers in bioengineering and biotechnology · 2021
    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

12 authors at 2 institutions in 2 countries.

Janne WalleniusFungal Genetics and Biotechnology, Department of Microbiology, University of Helsinki, University of Helsinki, Biocenter 1 PO Box 56 Viikinkaari 9, Helsinki, FI-00014, Finland.
Jussi KontroDepartment of Chemistry, University of Helsinki, P.O. Box 55 A. I. Virtasen Aukio 1, Helsinki, FI-00014, Finland.
Christina LyraFungal Genetics and Biotechnology, Department of Microbiology, University of Helsinki, University of Helsinki, Biocenter 1 PO Box 56 Viikinkaari 9, Helsinki, FI-00014, Finland.
Jaana KuuskeriFungal Genetics and Biotechnology, Department of Microbiology, University of Helsinki, University of Helsinki, Biocenter 1 PO Box 56 Viikinkaari 9, Helsinki, FI-00014, Finland.
Xing WanFungal Genetics and Biotechnology, Department of Microbiology, University of Helsinki, University of Helsinki, Biocenter 1 PO Box 56 Viikinkaari 9, Helsinki, FI-00014, Finland.
Mika A KähkönenFungal Genetics and Biotechnology, Department of Microbiology, University of Helsinki, University of Helsinki, Biocenter 1 PO Box 56 Viikinkaari 9, Helsinki, FI-00014, Finland.
Irshad BaigEaStCHEM, School of Chemistry, University of St Andrews, Fife, UK.
Paul C J KamerEaStCHEM, School of Chemistry, University of St Andrews, Fife, UK.
Jussi SipiläDepartment of Chemistry, University of Helsinki, P.O. Box 55 A. I. Virtasen Aukio 1, Helsinki, FI-00014, Finland.
Miia R MäkeläFungal Genetics and Biotechnology, Department of Microbiology, University of Helsinki, University of Helsinki, Biocenter 1 PO Box 56 Viikinkaari 9, Helsinki, FI-00014, Finland.ORCID 0000-0003-0771-2329
Paula NousiainenDepartment of Chemistry, University of Helsinki, P.O. Box 55 A. I. Virtasen Aukio 1, Helsinki, FI-00014, Finland.
Kristiina HildénFungal Genetics and Biotechnology, Department of Microbiology, University of Helsinki, University of Helsinki, Biocenter 1 PO Box 56 Viikinkaari 9, Helsinki, FI-00014, Finland.ORCID 0000-0002-0126-8186
University of Helsinki · FIUniversity of St Andrews · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fungal laccases are attracting enzymes for sustainable valorization of biorefinery lignins. To improve the lignin oxidation capacity of two previously characterized laccase isoenzymes from the white-rot fungus Obba rivulosa, we mutated their substrate-binding site at T1. As a result, the pH optimum of the recombinantly produced laccase variant rOrLcc2-D206N shifted by three units towards neutral pH. O. rivulosa laccase variants with redox mediators oxidized both the dimeric lignin model compound and biorefinery poplar lignin. Significant structural changes, such as selective benzylic α-oxidation, were detected by nuclear magnetic resonance analysis, although no polymerization of lignin was observed by gel permeation chromatography. This suggests that especially rOrLcc2-D206N is a promising candidate for lignin-related applications.

Indexed as

LaccasePolyporalesFungiLigninOxidation-ReductionLaccaseLignin

Identifiers

PMID34310858
PMCPMC8449659
OpenAlexW3184655681

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.