Evidence map›Paper›PMID 30353103›Full record

ArticleScientific reports2018

A highly stable laccase obtained by swapping the second cupredoxin domain.

Isabel Pardo, David Rodríguez-Escribano, Pablo Aza, Felipe de Salas, Angel T Martínez, Susana Camarero

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
7.4field-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

18 citing papers in PubMed, 44 citations in OpenAlex.

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  15. Protein Engineering Approaches to Enhance Fungal Laccase Production inInternational journal of molecular sciences · 2021
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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

6 authors at 2 institutions in 2 countries.

Isabel PardoCentro de Investigaciones Biológicas, CSIC, Madrid, Spain.ORCID http://orcid.org/0000-0002-8568-1559
David Rodríguez-EscribanoCentro de Investigaciones Biológicas, CSIC, Madrid, Spain.
Pablo AzaCentro de Investigaciones Biológicas, CSIC, Madrid, Spain.
Felipe de SalasCentro de Investigaciones Biológicas, CSIC, Madrid, Spain.
Angel T MartínezCentro de Investigaciones Biológicas, CSIC, Madrid, Spain.ORCID http://orcid.org/0000-0002-1584-2863
Susana CamareroCentro de Investigaciones Biológicas, CSIC, Madrid, Spain. susanacam@cib.csic.es.ORCID http://orcid.org/0000-0002-2812-895X
Centro de Investigaciones Biológicas Margarita Salas · ESNational Laboratory of the Rockies · US

Funding

Ministerio de Economía y Competitividad (Ministry of Economy and Competitiveness) BIO2014-56388-RMinisterio de Economía y Competitividad (Ministry of Economy and Competitiveness) BIO2017- 86559-R
6 · The paper itself

Abstract

The robustness of a high-redox potential laccase has been enhanced by swapping its second cupredoxin domain with that from another fungal laccase, which introduced a pool of neutral mutations in the protein sequence without affecting enzyme functionality. The new laccase showed outstanding stability to temperature, pH (2-9) and to organic solvents, while maintaining the ability to oxidize high-redox potential substrates. By engineering the signal peptide, enzyme secretion levels in Saccharomyces cerevisiae were increased, which allowed to purify the engineered enzyme for further characterization. The purified domain-swap laccase presented higher activity in the presence of ethanol or methanol, superior half-lives at 50-70 °C, improved stability at acidic pH, and similar catalytic efficiency for DMP albeit a lower one for ABTS (due to a shift in optimum pH). A new N-glycosylation site and a putative new surface salt-bridge were evaluated as possible determinants for the improved stability by site-directed mutagenesis. Although neither seemed to be strictly responsible for the improved thermostability, the new salt bridge was found to notably contribute to the high stability of the swapped enzyme in a broad pH range. Finally, the application potential of the new laccase was demonstrated with the enzymatic treatment of kraft lignin, an industrially relevant lignin stream, at high temperature, neutral pH and short incubation times.

Indexed as

AzurinBasidiomycotaEnzyme StabilityFungal ProteinsHydrogen-Ion ConcentrationLaccaseLigninModels, MolecularMutagenesis, Site-DirectedOxidation-ReductionProtein DomainsProtein EngineeringSaccharomycesSubstrate SpecificityTemperatureAzurincupredoxinFungal ProteinsKraft ligninLaccaseLignin

Identifiers

PMID30353103
PMCPMC6199291
OpenAlexW2896935192

What OpenQuestion holds

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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.