Purification and characterization of a novel lignin peroxidase from white-rot fungus Phanerochaete sordida YK-624.
Identifieur interne : 001820 ( Main/Exploration ); précédent : 001819; suivant : 001821Purification and characterization of a novel lignin peroxidase from white-rot fungus Phanerochaete sordida YK-624.
Auteurs : Mutsumi Sugiura [Japon] ; Hirofumi Hirai ; Tomoaki NishidaSource :
- FEMS microbiology letters [ 0378-1097 ] ; 2003.
Descripteurs français
- KwdFr :
- Acroléine (analogues et dérivés), Acroléine (métabolisme), Alcools (métabolisme), Catalyse (MeSH), Cinétique (MeSH), Dimérisation (MeSH), Masse moléculaire (MeSH), Oxydoréduction (MeSH), Peroxidases (composition chimique), Peroxidases (isolement et purification), Peroxidases (métabolisme), Phanerochaete (enzymologie), Protéines fongiques (composition chimique), Protéines fongiques (isolement et purification), Protéines fongiques (métabolisme).
- MESH :
- analogues et dérivés : Acroléine.
- composition chimique : Peroxidases, Protéines fongiques.
- enzymologie : Phanerochaete.
- isolement et purification : Peroxidases, Protéines fongiques.
- métabolisme : Acroléine, Alcools, Peroxidases, Protéines fongiques.
- Catalyse, Cinétique, Dimérisation, Masse moléculaire, Oxydoréduction.
English descriptors
- KwdEn :
- Acrolein (analogs & derivatives), Acrolein (metabolism), Alcohols (metabolism), Catalysis (MeSH), Dimerization (MeSH), Fungal Proteins (chemistry), Fungal Proteins (isolation & purification), Fungal Proteins (metabolism), Kinetics (MeSH), Molecular Weight (MeSH), Oxidation-Reduction (MeSH), Peroxidases (chemistry), Peroxidases (isolation & purification), Peroxidases (metabolism), Phanerochaete (enzymology).
- MESH :
- chemical , analogs & derivatives : Acrolein.
- chemical , chemistry : Fungal Proteins, Peroxidases.
- chemical , isolation & purification : Fungal Proteins, Peroxidases.
- chemical , metabolism : Acrolein, Alcohols, Fungal Proteins, Peroxidases.
- enzymology : Phanerochaete.
- Catalysis, Dimerization, Kinetics, Molecular Weight, Oxidation-Reduction.
Abstract
We characterized kinetics and substrate oxidation of a novel lignin peroxidase (YK-LiP) isolated from white-rot fungus Phanerochaete sordida YK-624. YK-LiP enzyme was identified and purified to homogeneity by anion-exchange chromatography and gel permeation chromatography. The molecular mass of YK-LiP was approximately 50 kDa, and the absorption spectrum of YK-LiP was almost the same as that of the LiP (Pc-LiP) from Phanerochaete chrysosporium. Steady-state kinetics of veratryl alcohol oxidation by YK-LiP (unlike that by Pc-LiP) revealed a bi-reactant sequential mechanism, although reactivity of YK-LiP to various monomeric substituted aromatic compounds was similar to that of Pc-LiP. Degradation of dimeric lignin model compounds was more effective by YK-LiP than by Pc-LiP, and the oxidation rate of sinapyl alcohol oligomer by YK-LiP was much faster than that by Pc-LiP.
DOI: 10.1016/S0378-1097(03)00447-6
PubMed: 12892894
Affiliations:
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type="abstract" xml:lang="en">We characterized kinetics and substrate oxidation of a novel lignin peroxidase (YK-LiP) isolated from white-rot fungus Phanerochaete sordida YK-624. YK-LiP enzyme was identified and purified to homogeneity by anion-exchange chromatography and gel permeation chromatography. The molecular mass of YK-LiP was approximately 50 kDa, and the absorption spectrum of YK-LiP was almost the same as that of the LiP (Pc-LiP) from Phanerochaete chrysosporium. Steady-state kinetics of veratryl alcohol oxidation by YK-LiP (unlike that by Pc-LiP) revealed a bi-reactant sequential mechanism, although reactivity of YK-LiP to various monomeric substituted aromatic compounds was similar to that of Pc-LiP. Degradation of dimeric lignin model compounds was more effective by YK-LiP than by Pc-LiP, and the oxidation rate of sinapyl alcohol oligomer by YK-LiP was much faster than that by Pc-LiP.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12892894</PMID><DateCompleted><Year>2003</Year><Month>10</Month><Day>03</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>30</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0378-1097</ISSN><JournalIssue CitedMedium="Print"><Volume>224</Volume><Issue>2</Issue><PubDate><Year>2003</Year><Month>Jul</Month><Day>29</Day></PubDate></JournalIssue><Title>FEMS microbiology letters</Title><ISOAbbreviation>FEMS Microbiol Lett</ISOAbbreviation></Journal><ArticleTitle>Purification and characterization of a novel lignin peroxidase from white-rot fungus Phanerochaete sordida YK-624.</ArticleTitle><Pagination><MedlinePgn>285-90</MedlinePgn></Pagination><Abstract><AbstractText>We characterized kinetics and substrate oxidation of a novel lignin peroxidase (YK-LiP) isolated from white-rot fungus Phanerochaete sordida YK-624. YK-LiP enzyme was identified and purified to homogeneity by anion-exchange chromatography and gel permeation chromatography. The molecular mass of YK-LiP was approximately 50 kDa, and the absorption spectrum of YK-LiP was almost the same as that of the LiP (Pc-LiP) from Phanerochaete chrysosporium. Steady-state kinetics of veratryl alcohol oxidation by YK-LiP (unlike that by Pc-LiP) revealed a bi-reactant sequential mechanism, although reactivity of YK-LiP to various monomeric substituted aromatic compounds was similar to that of Pc-LiP. 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