Evidence map›Paper›PMID 39153119›Full record

ArticleWorld journal of microbiology & biotechnology2024

Heterologous expression and characterization of a dye-decolorizing peroxidase from Ganoderma lucidum, and its application in decolorization and detoxifization of different types of dyes.

Dongmei Liu, Wentong Diao, Hong Chen, Xiwu Qi, Hailing Fang, Xu Yu, Li Li, Yang Bai, Chengyuan Liang

Abstract read
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In one paragraph

Article in World journal of microbiology & biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Ganodermataceae-current status, research, and development in Lower Mekong Basin.Frontiers in cellular and infection microbiology · 2025
    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

9 authors.

Dongmei Liu *Jiangsu Key Laboratory for the Research and Utilization of Plant Resources, Institute of Botany, Jiangsu Province and Chinese Academy of Sciences, Nanjing, 210014, China.
Wentong Diao *Nanjing University of Chinese Medicine, Nanjing, 210023, China.
Hong ChenNanjing University of Chinese Medicine, Nanjing, 210023, China.
Xiwu QiJiangsu Key Laboratory for the Research and Utilization of Plant Resources, Institute of Botany, Jiangsu Province and Chinese Academy of Sciences, Nanjing, 210014, China.
Hailing FangJiangsu Key Laboratory for the Research and Utilization of Plant Resources, Institute of Botany, Jiangsu Province and Chinese Academy of Sciences, Nanjing, 210014, China.
Xu YuJiangsu Key Laboratory for the Research and Utilization of Plant Resources, Institute of Botany, Jiangsu Province and Chinese Academy of Sciences, Nanjing, 210014, China.
Li LiJiangsu Key Laboratory for the Research and Utilization of Plant Resources, Institute of Botany, Jiangsu Province and Chinese Academy of Sciences, Nanjing, 210014, China.
Yang BaiJiangsu Key Laboratory for the Research and Utilization of Plant Resources, Institute of Botany, Jiangsu Province and Chinese Academy of Sciences, Nanjing, 210014, China.
Chengyuan LiangJiangsu Key Laboratory for the Research and Utilization of Plant Resources, Institute of Botany, Jiangsu Province and Chinese Academy of Sciences, Nanjing, 210014, China. liangcy618@cnbg.net.

Funding

National Natural Science Foundation of China 32102457
6 · The paper itself

Abstract

Dye-decolorizing peroxidases (DyPs) belong to a novel superfamily of heme peroxidases that can oxidize recalcitrant compounds. In the current study, the GlDyP2 gene from Ganoderma lucidum was heterologously expressed in Escherichia coli, and the enzymatic properties of the recombinant GlDyP2 protein were investigated. The GlDyP2 protein could oxidize not only the typical peroxidase substrate ABTS but also two lignin substrates, namely guaiacol and 2,6-dimethoxy phenol (DMP). For the ABTS substrate, the optimum pH and temperature of GlDyP2 were 4.0 and 35 °C, respectively. The pH stability and thermal stability of GlDyP2 were also measured; the results showed that GlDyP2 could function normally in the acidic environment, with a T

Indexed as

Coloring AgentsEnzyme StabilityEscherichia coliGuaiacolRecombinant ProteinsReishiTemperatureAnthraquinonesAzo CompoundsBenzothiazolesBiodegradation, EnvironmentalFungal ProteinsHydrogen-Ion ConcentrationKineticsLigninOxidation-Reduction2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acidAnthraquinonesAzo CompoundsBenzothiazolesColoring AgentsFungal ProteinsGuaiacolLigninmalachite greenPeroxidasePeroxidasesRecombinant ProteinsRemazol Brilliant Blue RRosaniline DyesSulfonic AcidsWastewaterWater Pollutants, ChemicalDecolorizationDetoxificationDye-decolorizing peroxidaseGanoderma lucidumHeterologous expression

Identifiers

PMID39153119

What OpenQuestion holds

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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.