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Dye-decolorizing peroxidases in Irpex lacteus combining the catalytic properties of heme peroxidases and laccase play important roles in ligninolytic system.

Identifieur interne : 000446 ( Main/Exploration ); précédent : 000445; suivant : 000447

Dye-decolorizing peroxidases in Irpex lacteus combining the catalytic properties of heme peroxidases and laccase play important roles in ligninolytic system.

Auteurs : Xing Qin [République populaire de Chine] ; Huiying Luo [République populaire de Chine] ; Xiaoyu Zhang [République populaire de Chine] ; Bin Yao [République populaire de Chine] ; Fuying Ma [République populaire de Chine] ; Xiaoyun Su [République populaire de Chine]

Source :

RBID : pubmed:30455731

Abstract

Background

The white rot fungus

Results

Based on the extracellular enzyme activities and secretome analysis,

Conclusions

The results proved for the first time that DyPs depolymerized lignin individually, combining catalytic features of different peroxidases on the functional level. Therefore, DyPs may be considered an important part of ligninolytic system in wood-decaying fungi.


DOI: 10.1186/s13068-018-1303-9
PubMed: 30455731
PubMed Central: PMC6223037


Affiliations:


Links toward previous steps (curation, corpus...)


Le document en format XML

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<author>
<name sortKey="Qin, Xing" sort="Qin, Xing" uniqKey="Qin X" first="Xing" last="Qin">Xing Qin</name>
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<p>
<b>Background</b>
</p>
<p>The white rot fungus </p>
</div>
<div type="abstract" xml:lang="en">
<p>
<b>Results</b>
</p>
<p>Based on the extracellular enzyme activities and secretome analysis, </p>
</div>
<div type="abstract" xml:lang="en">
<p>
<b>Conclusions</b>
</p>
<p>The results proved for the first time that DyPs depolymerized lignin individually, combining catalytic features of different peroxidases on the functional level. Therefore, DyPs may be considered an important part of ligninolytic system in wood-decaying fungi.</p>
</div>
</front>
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<DateRevised>
<Year>2020</Year>
<Month>09</Month>
<Day>30</Day>
</DateRevised>
<Article PubModel="Electronic-eCollection">
<Journal>
<ISSN IssnType="Print">1754-6834</ISSN>
<JournalIssue CitedMedium="Print">
<Volume>11</Volume>
<PubDate>
<Year>2018</Year>
</PubDate>
</JournalIssue>
<Title>Biotechnology for biofuels</Title>
<ISOAbbreviation>Biotechnol Biofuels</ISOAbbreviation>
</Journal>
<ArticleTitle>Dye-decolorizing peroxidases in
<i>Irpex lacteus</i>
combining the catalytic properties of heme peroxidases and laccase play important roles in ligninolytic system.</ArticleTitle>
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<MedlinePgn>302</MedlinePgn>
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<Abstract>
<AbstractText Label="Background" NlmCategory="UNASSIGNED">The white rot fungus
<i>Irpex lacteus</i>
exhibits a great potential in biopretreatment of lignocellulose as well as in biodegradation of xenobiotic compounds by extracellular ligninolytic enzymes. Among these enzymes, the possible involvement of dye-decolorizing peroxidase (DyP) in lignin degradation is not clear yet.</AbstractText>
<AbstractText Label="Results" NlmCategory="UNASSIGNED">Based on the extracellular enzyme activities and secretome analysis,
<i>I. lacteus</i>
CD2 produced DyPs as the main ligninolytic enzymes when grown in Kirk's medium supplemented with lignin. Further transcriptome analysis revealed that induced transcription of genes encoding DyPs was accompanied by the increased expression of transcripts for H
<sub>2</sub>
O
<sub>2</sub>
-generating enzymes such as alcohol oxidase, pyranose 2-oxidase, and glyoxal oxidases. Meanwhile, accumulation of transcripts for glycoside hydrolase and protease was observed, in agreement with abundant proteins. Moreover, the biochemical analysis of
<i>Il</i>
DyP2 and
<i>Il</i>
DyP1 confirmed that DyPs were able to catalyze the oxidation of typical peroxidases substrates ABTS, phenolic lignin compounds DMP, and guaiacol as well as non-phenolic lignin compound, veratryl alcohol. More importantly,
<i>Il</i>
DyP1 enhanced catalytic activity for veratryl alcohol oxidation in the presence of mediator 1-hydroxybenzotriazole, which was similar to the laccase/1-hydroxybenzotriazole system.</AbstractText>
<AbstractText Label="Conclusions" NlmCategory="UNASSIGNED">The results proved for the first time that DyPs depolymerized lignin individually, combining catalytic features of different peroxidases on the functional level. Therefore, DyPs may be considered an important part of ligninolytic system in wood-decaying fungi.</AbstractText>
</Abstract>
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<Keyword MajorTopicYN="N">Irpex lacteus</Keyword>
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