Evidence map›Paper›PMID 39466517›Full record

ArticleBiotechnology letters2024

Biochemical characterization of a recombinant laccase from Halalkalibacterium halodurans C-125 and its application in the biotransformation of organic compounds.

Jihene Maati, Jolanta Polak, Monika Janczarek, Marcin Grąz, Issam Smaali, Anna Jarosz-Wilkołazka

Abstract read
In one paragraph

Article in Biotechnology letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
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.

Jihene MaatiLaboratory of Protein Engineering and Bioactive Molecules (LIP-MB-LR11ES24), National Institute of Applied Sciences and Technology INSAT-BP 676, University of Carthage, 1080, Tunis Cedex, Tunisia.
Jolanta PolakDepartment of Biochemistry and Biotechnology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Akademicka 19, 20-033, Lublin, Poland.
Monika JanczarekDepartment of Industrial and Environmental Microbiology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Akademicka 19, 20-033, Lublin, Poland.
Marcin GrązDepartment of Biochemistry and Biotechnology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Akademicka 19, 20-033, Lublin, Poland.
Issam SmaaliLaboratory of Protein Engineering and Bioactive Molecules (LIP-MB-LR11ES24), National Institute of Applied Sciences and Technology INSAT-BP 676, University of Carthage, 1080, Tunis Cedex, Tunisia.
Anna Jarosz-WilkołazkaDepartment of Biochemistry and Biotechnology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Akademicka 19, 20-033, Lublin, Poland. anna.jarosz-wilkolazka@mail.umcs.pl.ORCID http://orcid.org/0000-0002-8222-4379

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectivesThis study aimed to produce an engineered recombinant laccase from extremophilic Halalkalibacterium halodurans C-125 (Lac-HhC-125) with higher protein yield, into a more active conformation and with properties that meet the fundamental needs of biotechnological application.

resultsThe rLac-HhC125 was partially purified by size exclusion chromatography and concentrated by ultrafiltration (10 kDa) with a yield of 57.6%. Oxidation reactions showed that adding 2 mM CuSO

conclusionThe rLac-HhC125 was active at high temperatures and alkaline pH, exhibited tolerance to organic solvents, and efficiently transformed different hydroxy derivatives into coloured compounds, which indicates that it can be used in various biotechnological processes.

Indexed as

BiotransformationLaccaseRecombinant ProteinsBacterial ProteinsEnzyme StabilityHydrogen-Ion ConcentrationOrganic ChemicalsSolventsTemperatureBacterial ProteinsLaccaseOrganic ChemicalsRecombinant ProteinsSolventsBiotransformationGreen catalystHalalkalibacterium haloduransLaccase

Identifiers

PMID39466517
PMCPMC11550293

What Socratic 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 Socratic graph.