Novel thermotolerant laccases produced by the white-rot fungus Physisporinus rivulosus.
Identifieur interne : 001434 ( Main/Exploration ); précédent : 001433; suivant : 001435Novel thermotolerant laccases produced by the white-rot fungus Physisporinus rivulosus.
Auteurs : Kristiina Hildén [Finlande] ; Terhi K. Hakala ; Pekka Maijala ; Taina K. Lundell ; Annele HatakkaSource :
- Applied microbiology and biotechnology [ 0175-7598 ] ; 2007.
Descripteurs français
- KwdFr :
- Bois (métabolisme), Cinétique (MeSH), Isoenzymes (biosynthèse), Laccase (biosynthèse), Lignine (métabolisme), Microbiologie industrielle (méthodes), Milieux de culture (MeSH), Picea (métabolisme), Polyporaceae (croissance et développement), Polyporaceae (enzymologie), Polyporaceae (génétique), Stabilité enzymatique (MeSH), Température élevée (MeSH).
- MESH :
- biosynthèse : Isoenzymes, Laccase.
- croissance et développement : Polyporaceae.
- enzymologie : Polyporaceae.
- génétique : Polyporaceae.
- métabolisme : Bois, Lignine, Picea.
- méthodes : Microbiologie industrielle.
- Cinétique, Milieux de culture, Stabilité enzymatique, Température élevée.
English descriptors
- KwdEn :
- Culture Media (MeSH), Enzyme Stability (MeSH), Hot Temperature (MeSH), Industrial Microbiology (methods), Isoenzymes (biosynthesis), Kinetics (MeSH), Laccase (biosynthesis), Lignin (metabolism), Picea (metabolism), Polyporaceae (enzymology), Polyporaceae (genetics), Polyporaceae (growth & development), Wood (metabolism).
- MESH :
- chemical , biosynthesis : Isoenzymes, Laccase.
- chemical , metabolism : Lignin.
- chemical : Culture Media.
- enzymology : Polyporaceae.
- genetics : Polyporaceae.
- growth & development : Polyporaceae.
- metabolism : Picea, Wood.
- methods : Industrial Microbiology.
- Enzyme Stability, Hot Temperature, Kinetics.
Abstract
The white-rot basidiomycete Physisporinus rivulosus strain T241i is highly selective for degradation of softwood lignin, which makes this fungus suitable for biopulping. In order to promote laccase production, P. rivulosus was cultivated in nutrient-nitrogen sufficient liquid media containing either charcoal or spruce sawdust as supplements. Two laccases with distinct pI values, Lac-3.5 and Lac-4.8, were purified from peptone-spruce sawdust-charcoal cultures of P. rivulosus. Both laccases showed thermal stability at up to 60 degrees C. Lac-4.8 was thermally activated at 50 degrees C. Surprisingly, both laccases displayed atypically low pH optima (pH 3.0-3.5) in oxidation of the commonly used laccase substrates syringaldazine (4-hydroxy-3,5-dimethoxybenzaldehyde azine), 2,6-dimethoxyphenol and guaiacol (2-methoxyphenol). Steady-state kinetic measurements pointed to unusually low affinity to guaiacol at low pH, whereas the kinetic constants for the methoxyphenols and ABTS were within the ranges reported for other fungal laccases. The combination of thermotolerance with low pH optima for methoxylated phenol substrates suggests that the two P. rivulosus T241i laccases possess potential for use in biotechnological applications.
DOI: 10.1007/s00253-007-1155-x
PubMed: 17805527
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Hakala</name></author><author><name sortKey="Maijala, Pekka" sort="Maijala, Pekka" uniqKey="Maijala P" first="Pekka" last="Maijala">Pekka Maijala</name></author><author><name sortKey="Lundell, Taina K" sort="Lundell, Taina K" uniqKey="Lundell T" first="Taina K" last="Lundell">Taina K. 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Hakala</name></author><author><name sortKey="Maijala, Pekka" sort="Maijala, Pekka" uniqKey="Maijala P" first="Pekka" last="Maijala">Pekka Maijala</name></author><author><name sortKey="Lundell, Taina K" sort="Lundell, Taina K" uniqKey="Lundell T" first="Taina K" last="Lundell">Taina K. Lundell</name></author><author><name sortKey="Hatakka, Annele" sort="Hatakka, Annele" uniqKey="Hatakka A" first="Annele" last="Hatakka">Annele Hatakka</name></author></analytic><series><title level="j">Applied microbiology and biotechnology</title><idno type="ISSN">0175-7598</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Culture Media (MeSH)</term><term>Enzyme Stability (MeSH)</term><term>Hot Temperature (MeSH)</term><term>Industrial Microbiology (methods)</term><term>Isoenzymes (biosynthesis)</term><term>Kinetics (MeSH)</term><term>Laccase (biosynthesis)</term><term>Lignin (metabolism)</term><term>Picea (metabolism)</term><term>Polyporaceae (enzymology)</term><term>Polyporaceae (genetics)</term><term>Polyporaceae (growth & development)</term><term>Wood (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Bois (métabolisme)</term><term>Cinétique (MeSH)</term><term>Isoenzymes (biosynthèse)</term><term>Laccase (biosynthèse)</term><term>Lignine (métabolisme)</term><term>Microbiologie industrielle (méthodes)</term><term>Milieux de culture (MeSH)</term><term>Picea (métabolisme)</term><term>Polyporaceae (croissance et développement)</term><term>Polyporaceae (enzymologie)</term><term>Polyporaceae (génétique)</term><term>Stabilité enzymatique (MeSH)</term><term>Température élevée (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Isoenzymes</term><term>Laccase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lignin</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Culture Media</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Isoenzymes</term><term>Laccase</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Polyporaceae</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Polyporaceae</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Polyporaceae</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Polyporaceae</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Polyporaceae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Polyporaceae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Picea</term><term>Wood</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Industrial Microbiology</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Bois</term><term>Lignine</term><term>Picea</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Microbiologie industrielle</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Enzyme Stability</term><term>Hot Temperature</term><term>Kinetics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Milieux de culture</term><term>Stabilité enzymatique</term><term>Température élevée</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The white-rot basidiomycete Physisporinus rivulosus strain T241i is highly selective for degradation of softwood lignin, which makes this fungus suitable for biopulping. In order to promote laccase production, P. rivulosus was cultivated in nutrient-nitrogen sufficient liquid media containing either charcoal or spruce sawdust as supplements. Two laccases with distinct pI values, Lac-3.5 and Lac-4.8, were purified from peptone-spruce sawdust-charcoal cultures of P. rivulosus. Both laccases showed thermal stability at up to 60 degrees C. Lac-4.8 was thermally activated at 50 degrees C. Surprisingly, both laccases displayed atypically low pH optima (pH 3.0-3.5) in oxidation of the commonly used laccase substrates syringaldazine (4-hydroxy-3,5-dimethoxybenzaldehyde azine), 2,6-dimethoxyphenol and guaiacol (2-methoxyphenol). Steady-state kinetic measurements pointed to unusually low affinity to guaiacol at low pH, whereas the kinetic constants for the methoxyphenols and ABTS were within the ranges reported for other fungal laccases. The combination of thermotolerance with low pH optima for methoxylated phenol substrates suggests that the two P. rivulosus T241i laccases possess potential for use in biotechnological applications.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17805527</PMID><DateCompleted><Year>2008</Year><Month>01</Month><Day>08</Day></DateCompleted><DateRevised><Year>2008</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0175-7598</ISSN><JournalIssue CitedMedium="Print"><Volume>77</Volume><Issue>2</Issue><PubDate><Year>2007</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Applied microbiology and biotechnology</Title><ISOAbbreviation>Appl Microbiol Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Novel thermotolerant laccases produced by the white-rot fungus Physisporinus rivulosus.</ArticleTitle><Pagination><MedlinePgn>301-9</MedlinePgn></Pagination><Abstract><AbstractText>The white-rot basidiomycete Physisporinus rivulosus strain T241i is highly selective for degradation of softwood lignin, which makes this fungus suitable for biopulping. In order to promote laccase production, P. rivulosus was cultivated in nutrient-nitrogen sufficient liquid media containing either charcoal or spruce sawdust as supplements. Two laccases with distinct pI values, Lac-3.5 and Lac-4.8, were purified from peptone-spruce sawdust-charcoal cultures of P. rivulosus. Both laccases showed thermal stability at up to 60 degrees C. Lac-4.8 was thermally activated at 50 degrees C. Surprisingly, both laccases displayed atypically low pH optima (pH 3.0-3.5) in oxidation of the commonly used laccase substrates syringaldazine (4-hydroxy-3,5-dimethoxybenzaldehyde azine), 2,6-dimethoxyphenol and guaiacol (2-methoxyphenol). Steady-state kinetic measurements pointed to unusually low affinity to guaiacol at low pH, whereas the kinetic constants for the methoxyphenols and ABTS were within the ranges reported for other fungal laccases. The combination of thermotolerance with low pH optima for methoxylated phenol substrates suggests that the two P. rivulosus T241i laccases possess potential for use in biotechnological applications.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hildén</LastName><ForeName>Kristiina</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Applied Chemistry and Microbiology, Viikki Biocenter, University of Helsinki, Helsinki, Finland. kristiina.s.hilden@helsinki.fi</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hakala</LastName><ForeName>Terhi K</ForeName><Initials>TK</Initials></Author><Author ValidYN="Y"><LastName>Maijala</LastName><ForeName>Pekka</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Lundell</LastName><ForeName>Taina K</ForeName><Initials>TK</Initials></Author><Author ValidYN="Y"><LastName>Hatakka</LastName><ForeName>Annele</ForeName><Initials>A</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><ArticleDate DateType="Electronic"><Year>2007</Year><Month>09</Month><Day>06</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Appl Microbiol Biotechnol</MedlineTA><NlmUniqueID>8406612</NlmUniqueID><ISSNLinking>0175-7598</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>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.10.3.2</RegistryNumber><NameOfSubstance UI="D042845">Laccase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003470" MajorTopicYN="N">Culture Media</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="Y">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006358" MajorTopicYN="Y">Hot Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007218" MajorTopicYN="N">Industrial Microbiology</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007527" MajorTopicYN="N">Isoenzymes</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D042845" MajorTopicYN="N">Laccase</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D028222" MajorTopicYN="N">Picea</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011124" MajorTopicYN="N">Polyporaceae</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000254" MajorTopicYN="Y">growth & development</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014934" MajorTopicYN="N">Wood</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2007</Year><Month>06</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2007</Year><Month>08</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2007</Year><Month>08</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>9</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>1</Month><Day>9</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>9</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17805527</ArticleId><ArticleId IdType="doi">10.1007/s00253-007-1155-x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Finlande</li></country><region><li>Uusimaa</li></region><settlement><li>Helsinki</li></settlement><orgName><li>Université d'Helsinki</li></orgName></list><tree><noCountry><name sortKey="Hakala, Terhi K" sort="Hakala, Terhi K" uniqKey="Hakala T" first="Terhi K" last="Hakala">Terhi K. Hakala</name><name sortKey="Hatakka, Annele" sort="Hatakka, Annele" uniqKey="Hatakka A" first="Annele" last="Hatakka">Annele Hatakka</name><name sortKey="Lundell, Taina K" sort="Lundell, Taina K" uniqKey="Lundell T" first="Taina K" last="Lundell">Taina K. Lundell</name><name sortKey="Maijala, Pekka" sort="Maijala, Pekka" uniqKey="Maijala P" first="Pekka" last="Maijala">Pekka Maijala</name></noCountry><country name="Finlande"><region name="Uusimaa"><name sortKey="Hilden, Kristiina" sort="Hilden, Kristiina" uniqKey="Hilden K" first="Kristiina" last="Hildén">Kristiina Hildén</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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