Characteristics of novel lignin peroxidases produced by white-rot fungus Phanerochaete sordida YK-624.
Identifieur interne : 000844 ( Main/Corpus ); précédent : 000843; suivant : 000845Characteristics of novel lignin peroxidases produced by white-rot fungus Phanerochaete sordida YK-624.
Auteurs : Hirofumi Hirai ; Mutsumi Sugiura ; Shingo Kawai ; Tomoaki NishidaSource :
- FEMS microbiology letters [ 0378-1097 ] ; 2005.
English descriptors
- KwdEn :
- Benzyl Alcohols (metabolism), Chromatography, Gel (MeSH), Chromatography, Ion Exchange (MeSH), Fungal Proteins (chemistry), Fungal Proteins (isolation & purification), Fungal Proteins (metabolism), Hydrogen Peroxide (metabolism), Kinetics (MeSH), Lignin (analogs & derivatives), Lignin (metabolism), Molecular Weight (MeSH), Oxidation-Reduction (MeSH), Peroxidases (chemistry), Peroxidases (isolation & purification), Peroxidases (metabolism), Phanerochaete (enzymology), Spectrum Analysis (MeSH).
- MESH :
- chemical , analogs & derivatives : Lignin.
- chemical , chemistry : Fungal Proteins, Peroxidases.
- chemical , isolation & purification : Fungal Proteins, Peroxidases.
- chemical , metabolism : Benzyl Alcohols, Fungal Proteins, Hydrogen Peroxide, Lignin, Peroxidases.
- enzymology : Phanerochaete.
- Chromatography, Gel, Chromatography, Ion Exchange, Kinetics, Molecular Weight, Oxidation-Reduction, Spectrum Analysis.
Abstract
We characterized a lignin peroxidase (YK-LiP2) isolated from shaking culture inoculated with the white-rot fungus Phanerochaete sordida YK-624. The YK-LiP2 enzyme was identified and purified to homogeneity by anion-exchange chromatography and gel permeation chromatography. The molecular weight of YK-LiP2 was approximately 45 kDa, and its absorption spectrum was almost the same as that of the LiP (Pc-LiP) from P. chrysosporium. Steady-state kinetics of veratryl alcohol (VA) oxidation by YK-LiP2 revealed an ordered bi-bi ping-pong mechanism, although the Pc-LiP oxidation of ferrocytochrome c obeys peroxidase ping-pong kinetics rather than ordered bi-bi ping-pong kinetics. Degradation of dimeric lignin model compounds by YK-LiP2 was more effective than that by Pc-LiP. Moreover, YK-LiP2 and YK-LiP1, which was previously isolated from static culture inoculated with P. sordida YK-624, oxidized VA under a higher concentration of hydrogen peroxide (>2.5 mM) although Pc-LiP could not oxidize VA in the presence of 2.5 mM hydrogen peroxide.
DOI: 10.1016/j.femsle.2005.03.032
PubMed: 15869957
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pubmed:15869957Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Characteristics of novel lignin peroxidases produced by white-rot fungus Phanerochaete sordida YK-624.</title><author><name sortKey="Hirai, Hirofumi" sort="Hirai, Hirofumi" uniqKey="Hirai H" first="Hirofumi" last="Hirai">Hirofumi Hirai</name><affiliation><nlm:affiliation>Department of Forest Resources Science, Faculty of Agriculture, Shizuoka University, Shizuoka 422-8529, Japan. afhhirai@agr.shizuoka.ac.jp</nlm:affiliation></affiliation></author><author><name sortKey="Sugiura, Mutsumi" sort="Sugiura, Mutsumi" uniqKey="Sugiura M" first="Mutsumi" last="Sugiura">Mutsumi Sugiura</name></author><author><name sortKey="Kawai, Shingo" sort="Kawai, Shingo" uniqKey="Kawai S" first="Shingo" last="Kawai">Shingo Kawai</name></author><author><name sortKey="Nishida, Tomoaki" sort="Nishida, Tomoaki" uniqKey="Nishida T" first="Tomoaki" last="Nishida">Tomoaki Nishida</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2005">2005</date><idno type="RBID">pubmed:15869957</idno><idno type="pmid">15869957</idno><idno type="doi">10.1016/j.femsle.2005.03.032</idno><idno type="wicri:Area/Main/Corpus">000844</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000844</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Characteristics of novel lignin peroxidases produced by white-rot fungus Phanerochaete sordida YK-624.</title><author><name sortKey="Hirai, Hirofumi" sort="Hirai, Hirofumi" uniqKey="Hirai H" first="Hirofumi" last="Hirai">Hirofumi Hirai</name><affiliation><nlm:affiliation>Department of Forest Resources Science, Faculty of Agriculture, Shizuoka University, Shizuoka 422-8529, Japan. afhhirai@agr.shizuoka.ac.jp</nlm:affiliation></affiliation></author><author><name sortKey="Sugiura, Mutsumi" sort="Sugiura, Mutsumi" uniqKey="Sugiura M" first="Mutsumi" last="Sugiura">Mutsumi Sugiura</name></author><author><name sortKey="Kawai, Shingo" sort="Kawai, Shingo" uniqKey="Kawai S" first="Shingo" last="Kawai">Shingo Kawai</name></author><author><name sortKey="Nishida, Tomoaki" sort="Nishida, Tomoaki" uniqKey="Nishida T" first="Tomoaki" last="Nishida">Tomoaki Nishida</name></author></analytic><series><title level="j">FEMS microbiology letters</title><idno type="ISSN">0378-1097</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Benzyl Alcohols (metabolism)</term><term>Chromatography, Gel (MeSH)</term><term>Chromatography, Ion Exchange (MeSH)</term><term>Fungal Proteins (chemistry)</term><term>Fungal Proteins (isolation & purification)</term><term>Fungal Proteins (metabolism)</term><term>Hydrogen Peroxide (metabolism)</term><term>Kinetics (MeSH)</term><term>Lignin (analogs & derivatives)</term><term>Lignin (metabolism)</term><term>Molecular Weight (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (chemistry)</term><term>Peroxidases (isolation & purification)</term><term>Peroxidases (metabolism)</term><term>Phanerochaete (enzymology)</term><term>Spectrum Analysis (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Lignin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Fungal Proteins</term><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Fungal Proteins</term><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Benzyl Alcohols</term><term>Fungal Proteins</term><term>Hydrogen Peroxide</term><term>Lignin</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Chromatography, Gel</term><term>Chromatography, Ion Exchange</term><term>Kinetics</term><term>Molecular Weight</term><term>Oxidation-Reduction</term><term>Spectrum Analysis</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We characterized a lignin peroxidase (YK-LiP2) isolated from shaking culture inoculated with the white-rot fungus Phanerochaete sordida YK-624. The YK-LiP2 enzyme was identified and purified to homogeneity by anion-exchange chromatography and gel permeation chromatography. The molecular weight of YK-LiP2 was approximately 45 kDa, and its absorption spectrum was almost the same as that of the LiP (Pc-LiP) from P. chrysosporium. Steady-state kinetics of veratryl alcohol (VA) oxidation by YK-LiP2 revealed an ordered bi-bi ping-pong mechanism, although the Pc-LiP oxidation of ferrocytochrome c obeys peroxidase ping-pong kinetics rather than ordered bi-bi ping-pong kinetics. Degradation of dimeric lignin model compounds by YK-LiP2 was more effective than that by Pc-LiP. Moreover, YK-LiP2 and YK-LiP1, which was previously isolated from static culture inoculated with P. sordida YK-624, oxidized VA under a higher concentration of hydrogen peroxide (>2.5 mM) although Pc-LiP could not oxidize VA in the presence of 2.5 mM hydrogen peroxide.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15869957</PMID><DateCompleted><Year>2005</Year><Month>09</Month><Day>29</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0378-1097</ISSN><JournalIssue CitedMedium="Print"><Volume>246</Volume><Issue>1</Issue><PubDate><Year>2005</Year><Month>May</Month><Day>01</Day></PubDate></JournalIssue><Title>FEMS microbiology letters</Title><ISOAbbreviation>FEMS Microbiol Lett</ISOAbbreviation></Journal><ArticleTitle>Characteristics of novel lignin peroxidases produced by white-rot fungus Phanerochaete sordida YK-624.</ArticleTitle><Pagination><MedlinePgn>19-24</MedlinePgn></Pagination><Abstract><AbstractText>We characterized a lignin peroxidase (YK-LiP2) isolated from shaking culture inoculated with the white-rot fungus Phanerochaete sordida YK-624. The YK-LiP2 enzyme was identified and purified to homogeneity by anion-exchange chromatography and gel permeation chromatography. The molecular weight of YK-LiP2 was approximately 45 kDa, and its absorption spectrum was almost the same as that of the LiP (Pc-LiP) from P. chrysosporium. Steady-state kinetics of veratryl alcohol (VA) oxidation by YK-LiP2 revealed an ordered bi-bi ping-pong mechanism, although the Pc-LiP oxidation of ferrocytochrome c obeys peroxidase ping-pong kinetics rather than ordered bi-bi ping-pong kinetics. Degradation of dimeric lignin model compounds by YK-LiP2 was more effective than that by Pc-LiP. Moreover, YK-LiP2 and YK-LiP1, which was previously isolated from static culture inoculated with P. sordida YK-624, oxidized VA under a higher concentration of hydrogen peroxide (>2.5 mM) although Pc-LiP could not oxidize VA in the presence of 2.5 mM hydrogen peroxide.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hirai</LastName><ForeName>Hirofumi</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Forest Resources Science, Faculty of Agriculture, Shizuoka University, Shizuoka 422-8529, Japan. afhhirai@agr.shizuoka.ac.jp</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sugiura</LastName><ForeName>Mutsumi</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Kawai</LastName><ForeName>Shingo</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Nishida</LastName><ForeName>Tomoaki</ForeName><Initials>T</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEMS Microbiol Lett</MedlineTA><NlmUniqueID>7705721</NlmUniqueID><ISSNLinking>0378-1097</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001592">Benzyl Alcohols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="C042858">lignin peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>MB4T4A711H</RegistryNumber><NameOfSubstance UI="C042197">veratryl alcohol</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001592" MajorTopicYN="N">Benzyl Alcohols</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002850" MajorTopicYN="N">Chromatography, Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002852" MajorTopicYN="N">Chromatography, Ion Exchange</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013057" MajorTopicYN="N">Spectrum Analysis</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2004</Year><Month>12</Month><Day>24</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2005</Year><Month>03</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2005</Year><Month>03</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>5</Month><Day>5</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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