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Oxidation of a non-phenolic lignin model compound by two Irpex lacteus manganese peroxidases: evidence for implication of carboxylate and radicals.

Identifieur interne : 000534 ( Main/Exploration ); précédent : 000533; suivant : 000535

Oxidation of a non-phenolic lignin model compound by two Irpex lacteus manganese peroxidases: evidence for implication of carboxylate and radicals.

Auteurs : Xing Qin [République populaire de Chine] ; Xianhua Sun [République populaire de Chine] ; Huoqing Huang [République populaire de Chine] ; Yingguo Bai [République populaire de Chine] ; Yuan Wang [République populaire de Chine] ; Huiying Luo [République populaire de Chine] ; Bin Yao [République populaire de Chine] ; Xiaoyu Zhang [République populaire de Chine] ; Xiaoyun Su [République populaire de Chine]

Source :

RBID : pubmed:28439296

Abstract

BACKGROUND

Manganese peroxidase is one of the Class II fungal peroxidases that are able to oxidize the low redox potential phenolic lignin compounds. For high redox potential non-phenolic lignin degradation, mediators such as GSH and unsaturated fatty acids are required in the reaction. However, it is not known whether carboxylic acids are a mediator for non-phenolic lignin degradation.

RESULTS

The white rot fungus

CONCLUSIONS

We provide evidence that a carboxylic acid may mediate oxidation of non-phenolic lignin through the action of radicals. MnPs, but not LiP, VP, or DyP, are predominant peroxidases secreted by some white rot fungi such as


DOI: 10.1186/s13068-017-0787-z
PubMed: 28439296
PubMed Central: PMC5399396


Affiliations:


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Le document en format XML

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<name sortKey="Wang, Yuan" sort="Wang, Yuan" uniqKey="Wang Y" first="Yuan" last="Wang">Yuan Wang</name>
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<title level="j">Biotechnology for biofuels</title>
<idno type="ISSN">1754-6834</idno>
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<div type="abstract" xml:lang="en">
<p>
<b>BACKGROUND</b>
</p>
<p>Manganese peroxidase is one of the Class II fungal peroxidases that are able to oxidize the low redox potential phenolic lignin compounds. For high redox potential non-phenolic lignin degradation, mediators such as GSH and unsaturated fatty acids are required in the reaction. However, it is not known whether carboxylic acids are a mediator for non-phenolic lignin degradation.</p>
</div>
<div type="abstract" xml:lang="en">
<p>
<b>RESULTS</b>
</p>
<p>The white rot fungus </p>
</div>
<div type="abstract" xml:lang="en">
<p>
<b>CONCLUSIONS</b>
</p>
<p>We provide evidence that a carboxylic acid may mediate oxidation of non-phenolic lignin through the action of radicals. MnPs, but not LiP, VP, or DyP, are predominant peroxidases secreted by some white rot fungi such as </p>
</div>
</front>
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<PMID Version="1">28439296</PMID>
<DateRevised>
<Year>2020</Year>
<Month>10</Month>
<Day>01</Day>
</DateRevised>
<Article PubModel="Electronic-eCollection">
<Journal>
<ISSN IssnType="Print">1754-6834</ISSN>
<JournalIssue CitedMedium="Print">
<Volume>10</Volume>
<PubDate>
<Year>2017</Year>
</PubDate>
</JournalIssue>
<Title>Biotechnology for biofuels</Title>
<ISOAbbreviation>Biotechnol Biofuels</ISOAbbreviation>
</Journal>
<ArticleTitle>Oxidation of a non-phenolic lignin model compound by two
<i>Irpex lacteus</i>
manganese peroxidases: evidence for implication of carboxylate and radicals.</ArticleTitle>
<Pagination>
<MedlinePgn>103</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1186/s13068-017-0787-z</ELocationID>
<Abstract>
<AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">Manganese peroxidase is one of the Class II fungal peroxidases that are able to oxidize the low redox potential phenolic lignin compounds. For high redox potential non-phenolic lignin degradation, mediators such as GSH and unsaturated fatty acids are required in the reaction. However, it is not known whether carboxylic acids are a mediator for non-phenolic lignin degradation.</AbstractText>
<AbstractText Label="RESULTS" NlmCategory="RESULTS">The white rot fungus
<i>Irpex lacteus</i>
is one of the most potent fungi in degradation of lignocellulose and xenobiotics. Two manganese peroxidases (
<i>Il</i>
MnP1 and
<i>Il</i>
MnP2) from
<i>I. lacteus</i>
CD2 were over-expressed in
<i>Escherichia coli</i>
and successfully refolded from inclusion bodies. Both
<i>Il</i>
MnP1 and
<i>Il</i>
MnP2 oxidized the phenolic compounds efficiently. Surprisingly, they could degrade veratryl alcohol, a non-phenolic lignin compound, in a Mn
<sup>2+</sup>
-dependent fashion. Malonate or oxalate was found to be also essential in this degradation. The oxidation of non-phenolic lignin was further confirmed by analysis of the reaction products using LC-MS/MS. We proved that Mn
<sup>2+</sup>
and a certain carboxylate are indispensable in oxidation and that the radicals generated under this condition, specifically superoxide radical, are at least partially involved in lignin oxidative degradation.
<i>Il</i>
MnP1 and
<i>Il</i>
MnP2 can also efficiently decolorize dyes with different structures.</AbstractText>
<AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">We provide evidence that a carboxylic acid may mediate oxidation of non-phenolic lignin through the action of radicals. MnPs, but not LiP, VP, or DyP, are predominant peroxidases secreted by some white rot fungi such as
<i>I. lacteus</i>
and the selective lignocellulose degrader
<i>Ceriporiopsis subvermispora</i>
. Our finding will help understand how these fungi can utilize MnPs and an excreted organic acid, which is usually a normal metabolite, to efficiently degrade the non-phenolic lignin. The unique properties of
<i>Il</i>
MnP1 and
<i>Il</i>
MnP2 make them good candidates for exploring molecular mechanisms underlying non-phenolic lignin compounds oxidation by MnPs and for applications in lignocellulose degradation and environmental remediation.</AbstractText>
</Abstract>
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<Affiliation>Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, No. 12 South Zhongguancun Street, Beijing, 100081 People's Republic of China.</Affiliation>
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</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Wang</LastName>
<ForeName>Yuan</ForeName>
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<AffiliationInfo>
<Affiliation>Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, No. 12 South Zhongguancun Street, Beijing, 100081 People's Republic of China.</Affiliation>
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<LastName>Luo</LastName>
<ForeName>Huiying</ForeName>
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<AffiliationInfo>
<Affiliation>Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, No. 12 South Zhongguancun Street, Beijing, 100081 People's Republic of China.</Affiliation>
<Identifier Source="ISNI">0000 0001 0526 1937</Identifier>
<Identifier Source="GRID">grid.410727.7</Identifier>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Yao</LastName>
<ForeName>Bin</ForeName>
<Initials>B</Initials>
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<LastName>Zhang</LastName>
<ForeName>Xiaoyu</ForeName>
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<Affiliation>College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, 430074 People's Republic of China.</Affiliation>
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