Increased PCP removal by Amylomyces rouxii transformants with heterologous Phanerochaete chrysosporium peroxidases supplementing their natural degradative pathway.
Identifieur interne : 000622 ( Main/Exploration ); précédent : 000621; suivant : 000623Increased PCP removal by Amylomyces rouxii transformants with heterologous Phanerochaete chrysosporium peroxidases supplementing their natural degradative pathway.
Auteurs : A M Montiel-González [Mexique] ; F J Fernández ; N. Keer ; A. TomasiniSource :
- Applied microbiology and biotechnology [ 1432-0614 ] ; 2009.
Descripteurs français
- KwdFr :
- Biomasse (MeSH), Cinétique (MeSH), Dépollution biologique de l'environnement (MeSH), Gènes fongiques (MeSH), Mucorales (enzymologie), Mucorales (génétique), Pentachlorophénol (métabolisme), Peroxidases (génétique), Peroxidases (métabolisme), Phanerochaete (enzymologie), Polluants environnementaux (métabolisme), Régulation de l'expression des gènes fongiques (MeSH), Voies et réseaux métaboliques (MeSH).
- MESH :
- enzymologie : Mucorales, Phanerochaete.
- génétique : Mucorales, Peroxidases.
- métabolisme : Pentachlorophénol, Peroxidases, Polluants environnementaux.
- Biomasse, Cinétique, Dépollution biologique de l'environnement, Gènes fongiques, Régulation de l'expression des gènes fongiques, Voies et réseaux métaboliques.
English descriptors
- KwdEn :
- Biodegradation, Environmental (MeSH), Biomass (MeSH), Environmental Pollutants (metabolism), Gene Expression Regulation, Fungal (MeSH), Genes, Fungal (MeSH), Kinetics (MeSH), Metabolic Networks and Pathways (MeSH), Mucorales (enzymology), Mucorales (genetics), Pentachlorophenol (metabolism), Peroxidases (genetics), Peroxidases (metabolism), Phanerochaete (enzymology).
- MESH :
- chemical , genetics : Peroxidases.
- chemical , metabolism : Environmental Pollutants, Pentachlorophenol, Peroxidases.
- enzymology : Mucorales, Phanerochaete.
- genetics : Mucorales.
- Biodegradation, Environmental, Biomass, Gene Expression Regulation, Fungal, Genes, Fungal, Kinetics, Metabolic Networks and Pathways.
Abstract
Fungal peroxidases and phenoloxidases are widely used in aromatic toxic compounds degradation. Peroxidases, such as lignin peroxidase and manganese peroxidase, as well as laccases are mainly produced by basidiomycetes and to a lower extent by other fungi, such as ascomycetes. Peroxidase-encoding genes have been described and homologous expression has been achieved in basidiomycetes. Heterologous expression has also been achieved in some non-producing peroxidase ascomycetes, like Penicillium and Aspergillus. In this work, heterologous expression of peroxidase-encoding genes, lignin peroxidase, and manganese peroxidase was achieved in a zygomycete producing only phenoloxidases (Amylomyces rouxii), aimed at coupling two different pathways used in nature for PCP removal in only one microbial strain. The ability of PCP removal was assayed with one of the obtained transformants, resulting in increased activity with respect to the ability of the parental strain cultured free of the inducer tyrosine (95% and 45%, respectively, of the initial PCP (12.5 mg L(-1)) in 120 h, or 100% and 49%, respectively, of the initial PCP after 144 h of liquid culture).
DOI: 10.1007/s00253-009-1981-0
PubMed: 19340422
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Keer</name></author><author><name sortKey="Tomasini, A" sort="Tomasini, A" uniqKey="Tomasini A" first="A" last="Tomasini">A. 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Peroxidases, such as lignin peroxidase and manganese peroxidase, as well as laccases are mainly produced by basidiomycetes and to a lower extent by other fungi, such as ascomycetes. Peroxidase-encoding genes have been described and homologous expression has been achieved in basidiomycetes. Heterologous expression has also been achieved in some non-producing peroxidase ascomycetes, like Penicillium and Aspergillus. In this work, heterologous expression of peroxidase-encoding genes, lignin peroxidase, and manganese peroxidase was achieved in a zygomycete producing only phenoloxidases (Amylomyces rouxii), aimed at coupling two different pathways used in nature for PCP removal in only one microbial strain. The ability of PCP removal was assayed with one of the obtained transformants, resulting in increased activity with respect to the ability of the parental strain cultured free of the inducer tyrosine (95% and 45%, respectively, of the initial PCP (12.5 mg L(-1)) in 120 h, or 100% and 49%, respectively, of the initial PCP after 144 h of liquid culture).</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19340422</PMID><DateCompleted><Year>2009</Year><Month>10</Month><Day>22</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1432-0614</ISSN><JournalIssue CitedMedium="Internet"><Volume>84</Volume><Issue>2</Issue><PubDate><Year>2009</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Applied microbiology and biotechnology</Title><ISOAbbreviation>Appl Microbiol Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Increased PCP removal by Amylomyces rouxii transformants with heterologous Phanerochaete chrysosporium peroxidases supplementing their natural degradative pathway.</ArticleTitle><Pagination><MedlinePgn>335-40</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00253-009-1981-0</ELocationID><Abstract><AbstractText>Fungal peroxidases and phenoloxidases are widely used in aromatic toxic compounds degradation. Peroxidases, such as lignin peroxidase and manganese peroxidase, as well as laccases are mainly produced by basidiomycetes and to a lower extent by other fungi, such as ascomycetes. Peroxidase-encoding genes have been described and homologous expression has been achieved in basidiomycetes. Heterologous expression has also been achieved in some non-producing peroxidase ascomycetes, like Penicillium and Aspergillus. In this work, heterologous expression of peroxidase-encoding genes, lignin peroxidase, and manganese peroxidase was achieved in a zygomycete producing only phenoloxidases (Amylomyces rouxii), aimed at coupling two different pathways used in nature for PCP removal in only one microbial strain. The ability of PCP removal was assayed with one of the obtained transformants, resulting in increased activity with respect to the ability of the parental strain cultured free of the inducer tyrosine (95% and 45%, respectively, of the initial PCP (12.5 mg L(-1)) in 120 h, or 100% and 49%, respectively, of the initial PCP after 144 h of liquid culture).</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Montiel-González</LastName><ForeName>A M</ForeName><Initials>AM</Initials><AffiliationInfo><Affiliation>Departamento de Biotecnología, CBS, Universidad Autónoma Metropolitana-Iztapalapa Avda, San Rafael Atlixco #186 Colonia Vicentina, Delegación Iztapalapa, 09340, México D.F., México.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fernández</LastName><ForeName>F J</ForeName><Initials>FJ</Initials></Author><Author ValidYN="Y"><LastName>Keer</LastName><ForeName>N</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Tomasini</LastName><ForeName>A</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>2009</Year><Month>04</Month><Day>02</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="D004785">Environmental Pollutants</NameOfSubstance></Chemical><Chemical><RegistryNumber>D9BSU0SE4T</RegistryNumber><NameOfSubstance UI="D010416">Pentachlorophenol</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>EC 1.11.1.13</RegistryNumber><NameOfSubstance UI="C051129">manganese peroxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001673" MajorTopicYN="N">Biodegradation, Environmental</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018533" MajorTopicYN="N">Biomass</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004785" MajorTopicYN="N">Environmental Pollutants</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="N">Gene Expression Regulation, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005800" MajorTopicYN="N">Genes, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053858" MajorTopicYN="N">Metabolic Networks and Pathways</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009090" MajorTopicYN="N">Mucorales</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010416" MajorTopicYN="N">Pentachlorophenol</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</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></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2009</Year><Month>02</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2009</Year><Month>03</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2009</Year><Month>03</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>4</Month><Day>3</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>4</Month><Day>3</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>10</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19340422</ArticleId><ArticleId IdType="doi">10.1007/s00253-009-1981-0</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Mexique</li></country></list><tree><noCountry><name sortKey="Fernandez, F J" sort="Fernandez, F J" uniqKey="Fernandez F" first="F J" last="Fernández">F J Fernández</name><name sortKey="Keer, N" sort="Keer, N" uniqKey="Keer N" first="N" last="Keer">N. Keer</name><name sortKey="Tomasini, A" sort="Tomasini, A" uniqKey="Tomasini A" first="A" last="Tomasini">A. Tomasini</name></noCountry><country name="Mexique"><noRegion><name sortKey="Montiel Gonzalez, A M" sort="Montiel Gonzalez, A M" uniqKey="Montiel Gonzalez A" first="A M" last="Montiel-González">A M Montiel-González</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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