Manganese regulation of manganese peroxidase expression and lignin degradation by the white rot fungus Dichomitus squalens.
Identifieur interne : 000F11 ( Main/Exploration ); précédent : 000F10; suivant : 000F12Manganese regulation of manganese peroxidase expression and lignin degradation by the white rot fungus Dichomitus squalens.
Auteurs : F H Périé ; M H GoldSource :
- Applied and environmental microbiology [ 0099-2240 ] ; 1991.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Polyporaceae.
- métabolisme : Lignine, Manganèse, Peroxidases, Polyporaceae.
- Cinétique.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Lignin, Manganese, Peroxidases.
- enzymology : Polyporaceae.
- metabolism : Polyporaceae.
- Kinetics.
Abstract
Extracellular manganese peroxidase and laccase activities were detected in cultures of Dichomitus squalens (Polyporus anceps) under conditions favoring lignin degradation. In contrast, neither extracellular lignin peroxidase nor aryl alcohol oxidase activity was detected in cultures grown under a wide variety of conditions. The mineralization of 14C-ring-, -side chain-, and -methoxy-labeled synthetic guaiacyl lignins by D. squalens and the expression of extracellular manganese peroxidase were dependent on the presence of Mn(II), suggesting that manganese peroxidase is an important component of this organism's lignin degradation system. The expression of laccase activity was independent of manganese. In contrast to previous findings with Phanerochaete chrysosporium, lignin degradation by D. squalens proceeded in the cultures containing excess carbon and nitrogen.
DOI: 10.1128/AEM.57.8.2240-2245.1991
PubMed: 1768094
PubMed Central: PMC183557
Affiliations:
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In contrast, neither extracellular lignin peroxidase nor aryl alcohol oxidase activity was detected in cultures grown under a wide variety of conditions. The mineralization of 14C-ring-, -side chain-, and -methoxy-labeled synthetic guaiacyl lignins by D. squalens and the expression of extracellular manganese peroxidase were dependent on the presence of Mn(II), suggesting that manganese peroxidase is an important component of this organism's lignin degradation system. The expression of laccase activity was independent of manganese. In contrast to previous findings with Phanerochaete chrysosporium, lignin degradation by D. squalens proceeded in the cultures containing excess carbon and nitrogen.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1768094</PMID><DateCompleted><Year>1992</Year><Month>02</Month><Day>20</Day></DateCompleted><DateRevised><Year>2020</Year><Month>07</Month><Day>24</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0099-2240</ISSN><JournalIssue CitedMedium="Print"><Volume>57</Volume><Issue>8</Issue><PubDate><Year>1991</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Applied and environmental microbiology</Title><ISOAbbreviation>Appl Environ Microbiol</ISOAbbreviation></Journal><ArticleTitle>Manganese regulation of manganese peroxidase expression and lignin degradation by the white rot fungus Dichomitus squalens.</ArticleTitle><Pagination><MedlinePgn>2240-5</MedlinePgn></Pagination><Abstract><AbstractText>Extracellular manganese peroxidase and laccase activities were detected in cultures of Dichomitus squalens (Polyporus anceps) under conditions favoring lignin degradation. In contrast, neither extracellular lignin peroxidase nor aryl alcohol oxidase activity was detected in cultures grown under a wide variety of conditions. The mineralization of 14C-ring-, -side chain-, and -methoxy-labeled synthetic guaiacyl lignins by D. squalens and the expression of extracellular manganese peroxidase were dependent on the presence of Mn(II), suggesting that manganese peroxidase is an important component of this organism's lignin degradation system. The expression of laccase activity was independent of manganese. In contrast to previous findings with Phanerochaete chrysosporium, lignin degradation by D. squalens proceeded in the cultures containing excess carbon and nitrogen.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Périé</LastName><ForeName>F H</ForeName><Initials>FH</Initials><AffiliationInfo><Affiliation>Department of Chemical and Biological Sciences, Oregon Graduate Institute of Science and Technology, Beaverton 97006-1999.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gold</LastName><ForeName>M H</ForeName><Initials>MH</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Appl 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