Biochemical and molecular characterization of a manganese peroxidase isoenzyme from Pleurotus ostreatus.
Identifieur interne : 000C25 ( Main/Exploration ); précédent : 000C24; suivant : 000C26Biochemical and molecular characterization of a manganese peroxidase isoenzyme from Pleurotus ostreatus.
Auteurs : S. Sarkar [Espagne] ; A T Martínez ; M J MartínezSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 1997.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Polyporaceae.
- génétique : Isoenzymes, Peroxidases, Polyporaceae.
- isolement et purification : Isoenzymes, Peroxidases.
- Milieux de culture, Sondes moléculaires, Technique de Southern.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Isoenzymes, Peroxidases.
- chemical , isolation & purification : Isoenzymes, Peroxidases.
- chemical : Culture Media, Molecular Probes.
- enzymology : Polyporaceae.
- genetics : Polyporaceae.
- Blotting, Southern.
Abstract
In this study we purified and investigated the catalytic properties of a manganese peroxidase isoenzyme produced by the fungus Pleurotus ostreatus in liquid medium with peptone as nitrogen source. The isoenzyme was purified to homogeneity by chromatography on Bio-Rad Q-cartridge, Sephacryl S-200 and Mono-Q with activity yield of 59% and a purification factor of 36. The P. ostreatus MnP obtained had the same pI (3.75) and N-terminal sequence as MnP-1 of Pleurotus eryngii produced in the same medium (both exhibiting Mn-independent activities on phenolic and non-phenolic substrates). However, the N-terminal sequence of this P. ostreatus isoenzyme differed from a previous published sequence of MnP from this fungus. The results obtained show the importance of media composition in the production of different isoenzymes within the same fungal species. We have also demonstrated by Southern blots that the different isoenzymes are probably encoded by different genes, and that the MnP genes in both Pleurotus species are similar but different to those of Phanerochaete chrysosporium.
DOI: 10.1016/s0167-4838(96)00201-4
PubMed: 9165096
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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The isoenzyme was purified to homogeneity by chromatography on Bio-Rad Q-cartridge, Sephacryl S-200 and Mono-Q with activity yield of 59% and a purification factor of 36. The P. ostreatus MnP obtained had the same pI (3.75) and N-terminal sequence as MnP-1 of Pleurotus eryngii produced in the same medium (both exhibiting Mn-independent activities on phenolic and non-phenolic substrates). However, the N-terminal sequence of this P. ostreatus isoenzyme differed from a previous published sequence of MnP from this fungus. The results obtained show the importance of media composition in the production of different isoenzymes within the same fungal species. We have also demonstrated by Southern blots that the different isoenzymes are probably encoded by different genes, and that the MnP genes in both Pleurotus species are similar but different to those of Phanerochaete chrysosporium.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9165096</PMID><DateCompleted><Year>1997</Year><Month>06</Month><Day>12</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>10</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1339</Volume><Issue>1</Issue><PubDate><Year>1997</Year><Month>Apr</Month><Day>25</Day></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim Biophys Acta</ISOAbbreviation></Journal><ArticleTitle>Biochemical and molecular characterization of a manganese peroxidase isoenzyme from Pleurotus ostreatus.</ArticleTitle><Pagination><MedlinePgn>23-30</MedlinePgn></Pagination><Abstract><AbstractText>In this study we purified and investigated the catalytic properties of a manganese peroxidase isoenzyme produced by the fungus Pleurotus ostreatus in liquid medium with peptone as nitrogen source. The isoenzyme was purified to homogeneity by chromatography on Bio-Rad Q-cartridge, Sephacryl S-200 and Mono-Q with activity yield of 59% and a purification factor of 36. The P. ostreatus MnP obtained had the same pI (3.75) and N-terminal sequence as MnP-1 of Pleurotus eryngii produced in the same medium (both exhibiting Mn-independent activities on phenolic and non-phenolic substrates). However, the N-terminal sequence of this P. ostreatus isoenzyme differed from a previous published sequence of MnP from this fungus. The results obtained show the importance of media composition in the production of different isoenzymes within the same fungal species. We have also demonstrated by Southern blots that the different isoenzymes are probably encoded by different genes, and that the MnP genes in both Pleurotus species are similar but different to those of Phanerochaete chrysosporium.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sarkar</LastName><ForeName>S</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Centro de Investigaciones Biológicas, CSIC, Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Martínez</LastName><ForeName>A T</ForeName><Initials>AT</Initials></Author><Author ValidYN="Y"><LastName>Martínez</LastName><ForeName>M J</ForeName><Initials>MJ</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003470">Culture Media</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007527">Isoenzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015335">Molecular Probes</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.13</RegistryNumber><NameOfSubstance UI="C051129">manganese peroxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D015139" MajorTopicYN="N">Blotting, Southern</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003470" MajorTopicYN="N">Culture Media</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007527" MajorTopicYN="N">Isoenzymes</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015335" MajorTopicYN="N">Molecular Probes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011124" MajorTopicYN="N">Polyporaceae</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1997</Year><Month>4</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1997</Year><Month>4</Month><Day>25</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1997</Year><Month>4</Month><Day>25</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9165096</ArticleId><ArticleId IdType="pii">S0167-4838(96)00201-4</ArticleId><ArticleId IdType="doi">10.1016/s0167-4838(96)00201-4</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Espagne</li></country><region><li>Communauté de Madrid</li></region><settlement><li>Madrid</li></settlement></list><tree><noCountry><name sortKey="Martinez, A T" sort="Martinez, A T" uniqKey="Martinez A" first="A T" last="Martínez">A T Martínez</name><name sortKey="Martinez, M J" sort="Martinez, M J" uniqKey="Martinez M" first="M J" last="Martínez">M J Martínez</name></noCountry><country name="Espagne"><region name="Communauté de Madrid"><name sortKey="Sarkar, S" sort="Sarkar, S" uniqKey="Sarkar S" first="S" last="Sarkar">S. 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