Isozymes of lignin peroxidase and manganese(II) peroxidase from the white-rot basidiomycete Trametes versicolor. I. Isolation of enzyme forms and characterization of physical and catalytic properties.
Identifieur interne : 000E32 ( Main/Corpus ); précédent : 000E31; suivant : 000E33Isozymes of lignin peroxidase and manganese(II) peroxidase from the white-rot basidiomycete Trametes versicolor. I. Isolation of enzyme forms and characterization of physical and catalytic properties.
Auteurs : T. Johansson ; P O NymanSource :
- Archives of biochemistry and biophysics [ 0003-9861 ] ; 1993.
English descriptors
- KwdEn :
- Basidiomycota (enzymology), Basidiomycota (growth & development), Chromatography, Affinity (MeSH), Chromatography, Gel (MeSH), Chromatography, Ion Exchange (MeSH), Electrophoresis, Polyacrylamide Gel (MeSH), Isoenzymes (isolation & purification), Isoenzymes (metabolism), Kinetics (MeSH), Molecular Weight (MeSH), Peroxidases (isolation & purification), Peroxidases (metabolism), Spectrophotometry (MeSH).
- MESH :
- chemical , isolation & purification : Isoenzymes, Peroxidases.
- enzymology : Basidiomycota.
- growth & development : Basidiomycota.
- chemical , metabolism : Isoenzymes, Peroxidases.
- Chromatography, Affinity, Chromatography, Gel, Chromatography, Ion Exchange, Electrophoresis, Polyacrylamide Gel, Kinetics, Molecular Weight, Spectrophotometry.
Abstract
The basidiomycete Trametes versicolor is a white-rot fungus and a potent degrader of lignin. The development of extracellular enzyme activities in the fungal culture under physiological conditions of secondary metabolism was investigated. Using the culture medium as starting material a large number of peroxidase forms were purified by the use of chromatographic techniques. Sixteen forms of lignin peroxidase and five forms of manganese(II) peroxidase were separated and the majority of these enzymes was characterized with respect to isoelectric point, molecular mass, and specific enzyme activity. The manganese(II) peroxidases showed a lower isoelectric point (pI 3.2-2.9) and a slightly higher molecular mass (44-45 kDa) than the lignin peroxidases (pI 3.7-3.1, and 41-43 kDa). Specific enzyme activities for the forms of lignin peroxidase, using veratryl alcohol as the substrate, were found to differ considerably. Certain differences in the specific enzyme activity were also observed among the forms of manganese(II) peroxidase. A multitude of peroxidase forms has previously been encountered in another white-rot fungus, Phanerochaete chrysosporium. The discovery that it also occurs in T. versicolor would suggest that this multiplicity could be a common feature among white-rot fungi and may be essential for the biodegradation of lignin.
DOI: 10.1006/abbi.1993.1007
PubMed: 8424685
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pubmed:8424685Le document en format XML
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Johansson</name><affiliation><nlm:affiliation>Department of Biochemistry, University of Lund, Sweden.</nlm:affiliation></affiliation></author><author><name sortKey="Nyman, P O" sort="Nyman, P O" uniqKey="Nyman P" first="P O" last="Nyman">P O Nyman</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1993">1993</date><idno type="RBID">pubmed:8424685</idno><idno type="pmid">8424685</idno><idno type="doi">10.1006/abbi.1993.1007</idno><idno type="wicri:Area/Main/Corpus">000E32</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000E32</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Isozymes of lignin peroxidase and manganese(II) peroxidase from the white-rot basidiomycete Trametes versicolor. I. Isolation of enzyme forms and characterization of physical and catalytic properties.</title><author><name sortKey="Johansson, T" sort="Johansson, T" uniqKey="Johansson T" first="T" last="Johansson">T. Johansson</name><affiliation><nlm:affiliation>Department of Biochemistry, University of Lund, Sweden.</nlm:affiliation></affiliation></author><author><name sortKey="Nyman, P O" sort="Nyman, P O" uniqKey="Nyman P" first="P O" last="Nyman">P O Nyman</name></author></analytic><series><title level="j">Archives of biochemistry and biophysics</title><idno type="ISSN">0003-9861</idno><imprint><date when="1993" type="published">1993</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (enzymology)</term><term>Basidiomycota (growth & development)</term><term>Chromatography, Affinity (MeSH)</term><term>Chromatography, Gel (MeSH)</term><term>Chromatography, Ion Exchange (MeSH)</term><term>Electrophoresis, Polyacrylamide Gel (MeSH)</term><term>Isoenzymes (isolation & purification)</term><term>Isoenzymes (metabolism)</term><term>Kinetics (MeSH)</term><term>Molecular Weight (MeSH)</term><term>Peroxidases (isolation & purification)</term><term>Peroxidases (metabolism)</term><term>Spectrophotometry (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Isoenzymes</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Basidiomycota</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Isoenzymes</term><term>Peroxidases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Chromatography, Affinity</term><term>Chromatography, Gel</term><term>Chromatography, Ion Exchange</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Kinetics</term><term>Molecular Weight</term><term>Spectrophotometry</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The basidiomycete Trametes versicolor is a white-rot fungus and a potent degrader of lignin. The development of extracellular enzyme activities in the fungal culture under physiological conditions of secondary metabolism was investigated. Using the culture medium as starting material a large number of peroxidase forms were purified by the use of chromatographic techniques. Sixteen forms of lignin peroxidase and five forms of manganese(II) peroxidase were separated and the majority of these enzymes was characterized with respect to isoelectric point, molecular mass, and specific enzyme activity. The manganese(II) peroxidases showed a lower isoelectric point (pI 3.2-2.9) and a slightly higher molecular mass (44-45 kDa) than the lignin peroxidases (pI 3.7-3.1, and 41-43 kDa). Specific enzyme activities for the forms of lignin peroxidase, using veratryl alcohol as the substrate, were found to differ considerably. Certain differences in the specific enzyme activity were also observed among the forms of manganese(II) peroxidase. A multitude of peroxidase forms has previously been encountered in another white-rot fungus, Phanerochaete chrysosporium. The discovery that it also occurs in T. versicolor would suggest that this multiplicity could be a common feature among white-rot fungi and may be essential for the biodegradation of lignin.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8424685</PMID><DateCompleted><Year>1993</Year><Month>02</Month><Day>23</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0003-9861</ISSN><JournalIssue CitedMedium="Print"><Volume>300</Volume><Issue>1</Issue><PubDate><Year>1993</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Archives of biochemistry and biophysics</Title><ISOAbbreviation>Arch Biochem Biophys</ISOAbbreviation></Journal><ArticleTitle>Isozymes of lignin peroxidase and manganese(II) peroxidase from the white-rot basidiomycete Trametes versicolor. I. Isolation of enzyme forms and characterization of physical and catalytic properties.</ArticleTitle><Pagination><MedlinePgn>49-56</MedlinePgn></Pagination><Abstract><AbstractText>The basidiomycete Trametes versicolor is a white-rot fungus and a potent degrader of lignin. The development of extracellular enzyme activities in the fungal culture under physiological conditions of secondary metabolism was investigated. Using the culture medium as starting material a large number of peroxidase forms were purified by the use of chromatographic techniques. Sixteen forms of lignin peroxidase and five forms of manganese(II) peroxidase were separated and the majority of these enzymes was characterized with respect to isoelectric point, molecular mass, and specific enzyme activity. The manganese(II) peroxidases showed a lower isoelectric point (pI 3.2-2.9) and a slightly higher molecular mass (44-45 kDa) than the lignin peroxidases (pI 3.7-3.1, and 41-43 kDa). Specific enzyme activities for the forms of lignin peroxidase, using veratryl alcohol as the substrate, were found to differ considerably. Certain differences in the specific enzyme activity were also observed among the forms of manganese(II) peroxidase. A multitude of peroxidase forms has previously been encountered in another white-rot fungus, Phanerochaete chrysosporium. 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