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
Links to Exploration step
pubmed:15869957Le document en format XML
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<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>
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<author><name sortKey="Sugiura, Mutsumi" sort="Sugiura, Mutsumi" uniqKey="Sugiura M" first="Mutsumi" last="Sugiura">Mutsumi Sugiura</name>
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<author><name sortKey="Kawai, Shingo" sort="Kawai, Shingo" uniqKey="Kawai S" first="Shingo" last="Kawai">Shingo Kawai</name>
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<author><name sortKey="Nishida, Tomoaki" sort="Nishida, Tomoaki" uniqKey="Nishida T" first="Tomoaki" last="Nishida">Tomoaki Nishida</name>
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<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>
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<keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Lignin</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Fungal Proteins</term>
<term>Peroxidases</term>
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<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Fungal Proteins</term>
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<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>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term>
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<keywords scheme="MESH" xml:lang="en"><term>Chromatography, Gel</term>
<term>Chromatography, Ion Exchange</term>
<term>Kinetics</term>
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<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>
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<ArticleTitle>Characteristics of novel lignin peroxidases produced by white-rot fungus Phanerochaete sordida YK-624.</ArticleTitle>
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<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>
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