Evidence map›Paper›PMID 34884966›Full record

ArticleInternational journal of molecular sciences2021

Oxidation of Various Kraft Lignins with a Bacterial Laccase Enzyme.

Sebastian A Mayr, Raditya Subagia, Renate Weiss, Nikolaus Schwaiger, Hedda K Weber, Johannes Leitner, Doris Ribitsch, Gibson S Nyanhongo, Georg M Guebitz

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

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  14. Laccases and Tyrosinases in Organic Synthesis.International journal of molecular sciences · 2022
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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 at 2 institutions in 1 country.

Sebastian A MayrInstitute of Environmental Biotechnology, University of Natural Resources and Life Sciences (BOKU), Konrad Lorenz Strasse 20, 3430 Tulln, Austria.ORCID 0000-0001-6319-9908
Raditya SubagiaAustrian Centre for Industrial Biotechnology (ACIB), Konrad Lorenz Strasse 20, 3430 Tulln, Austria.
Renate WeissInstitute of Environmental Biotechnology, University of Natural Resources and Life Sciences (BOKU), Konrad Lorenz Strasse 20, 3430 Tulln, Austria.ORCID 0000-0001-7680-9832
Nikolaus SchwaigerSappi Paper Holding GmbH, Brucker Strasse 21, 8101 Gratkorn, Austria.ORCID 0000-0003-4720-2518
Hedda K WeberSappi Paper Holding GmbH, Brucker Strasse 21, 8101 Gratkorn, Austria.
Johannes LeitnerMondi Aktiengesellschaft, Marxergasse 4A, 1030 Vienna, Austria.
Doris RibitschInstitute of Environmental Biotechnology, University of Natural Resources and Life Sciences (BOKU), Konrad Lorenz Strasse 20, 3430 Tulln, Austria.
Gibson S NyanhongoInstitute of Environmental Biotechnology, University of Natural Resources and Life Sciences (BOKU), Konrad Lorenz Strasse 20, 3430 Tulln, Austria.
Georg M GuebitzInstitute of Environmental Biotechnology, University of Natural Resources and Life Sciences (BOKU), Konrad Lorenz Strasse 20, 3430 Tulln, Austria.ORCID 0000-0003-2262-487X
Austrian Centre of Industrial Biotechnology (Austria) · ATBOKU University · AT

Funding

Bio-based Industries Joint Untertaking 792021EuropeanUnion Horizon 2020 792021FFG COMET Flippr2 follows
6 · The paper itself

Abstract

Modification of kraft lignin (KL), traditionally uses harsh and energy-demanding physical and chemical processes. In this study, the potential of the bacterial laccase CotA (spore coating protein A) for oxidation of KL under mild conditions was assessed. Thereby, the efficiency of CotA to oxidize both softwood and hardwood KL of varying purity at alkaline conditions was examined. For the respective type of wood, the highest oxidation activity by CotA was determined for the medium ash content softwood KL (MA_S) and the medium ash content hardwood KL (MA_H), respectively. By an up to 95% decrease in fluorescence and up to 65% in phenol content coupling of the structural lignin units was indicated. These results correlated with an increase in viscosity and molecular weight, which increased nearly 2 and 20-fold for MA_H and about 1.3 and 6.0-fold for MA_S, respectively. Thus, this study confirms that the CotA laccase can oxidize a variety of KL at alkaline conditions, while the origin and purity of KL were found to have a major impact on the efficiency of oxidation. Under the herein tested conditions, it was observed that the MA_H KL showed the highest susceptibility to CotA oxidation when compared to the other hardwood KLs and the softwood KLs. Therefore, this could be a viable method to produce sustainable resins and adhesives.

Indexed as

BacteriaBacterial ProteinsLaccaseLigninMolecular WeightOxidation-ReductionBacterial ProteinsKraft ligninLaccaseLigninCotAisolationkraft ligninlaccaselignosulfonateoxidationprecipitationpurity

Identifiers

PMID34884966
PMCPMC8658217
OpenAlexW4200616493

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.