Recombinant expression of four oxidoreductases in Phanerochaete chrysosporium improves degradation of phenolic and non-phenolic substrates.
Identifieur interne : 000252 ( Main/Exploration ); précédent : 000251; suivant : 000253Recombinant expression of four oxidoreductases in Phanerochaete chrysosporium improves degradation of phenolic and non-phenolic substrates.
Auteurs : Nancy Coconi-Linares [Mexique] ; Elizabeth Ortiz-Vázquez [Mexique] ; Francisco Fernández [Mexique] ; Achim M. Loske [Mexique] ; Miguel A. G Mez-Lim [Mexique]Source :
- Journal of biotechnology [ 1873-4863 ] ; 2015.
Descripteurs français
- KwdFr :
- Clonage moléculaire (MeSH), Génie métabolique (méthodes), Laccase (génétique), Laccase (métabolisme), Peroxidases (génétique), Peroxidases (métabolisme), Phanerochaete (enzymologie), Phanerochaete (génétique), Phanerochaete (métabolisme), Phénols (métabolisme), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Transformation génétique (MeSH).
- MESH :
- enzymologie : Phanerochaete.
- génétique : Laccase, Peroxidases, Phanerochaete, Protéines fongiques, Protéines recombinantes.
- métabolisme : Laccase, Peroxidases, Phanerochaete, Phénols, Protéines fongiques, Protéines recombinantes.
- méthodes : Génie métabolique.
- Clonage moléculaire, Transformation génétique.
English descriptors
- KwdEn :
- Cloning, Molecular (MeSH), Fungal Proteins (genetics), Fungal Proteins (metabolism), Laccase (genetics), Laccase (metabolism), Metabolic Engineering (methods), Peroxidases (genetics), Peroxidases (metabolism), Phanerochaete (enzymology), Phanerochaete (genetics), Phanerochaete (metabolism), Phenols (metabolism), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Transformation, Genetic (MeSH).
- MESH :
- chemical , genetics : Fungal Proteins, Laccase, Peroxidases, Recombinant Proteins.
- chemical , metabolism : Fungal Proteins, Laccase, Peroxidases, Phenols, Recombinant Proteins.
- enzymology : Phanerochaete.
- genetics : Phanerochaete.
- metabolism : Phanerochaete.
- methods : Metabolic Engineering.
- Cloning, Molecular, Transformation, Genetic.
Abstract
Phanerochaete chrysosporium belongs to a group of lignin-degrading fungi that secretes various oxidoreductive enzymes, including lignin peroxidase (LiP) and manganese peroxidase (MnP). Previously, we demonstrated that the heterologous expression of a versatile peroxidase (VP) in P. chrysosporium recombinant strains is possible. However, the production of laccases (Lac) in this fungus has not been completely demonstrated and remains controversial. In order to investigate if the co-expression of Lac and VP in P. chrysosporium would improve the degradation of phenolic and non-phenolic substrates, we tested the constitutive co-expression of the lacIIIb gene from Trametes versicolor and the vpl2 gene from Pleurotus eryngii, and also the endogenous genes mnp1 and lipH8 by shock wave mediated transformation. The co-overexpression of peroxidases and laccases was improved up to five-fold as compared with wild type species. Transformant strains showed a broad spectrum in phenolic/non-phenolic biotransformation and a high percentage in synthetic dye decolorization in comparison with the parental strain. Our results show that the four enzymes can be constitutively expressed in a single transformant of P. chrysosporium in minimal medium. These data offer new possibilities for an easy and efficient co-expression of laccases and peroxidases in suitable basidiomycete species.
DOI: 10.1016/j.jbiotec.2015.06.401
PubMed: 26113215
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Recombinant expression of four oxidoreductases in Phanerochaete chrysosporium improves degradation of phenolic and non-phenolic substrates.</title><author><name sortKey="Coconi Linares, Nancy" sort="Coconi Linares, Nancy" uniqKey="Coconi Linares N" first="Nancy" last="Coconi-Linares">Nancy Coconi-Linares</name><affiliation wicri:level="1"><nlm:affiliation>Centro de Investigación y de Estudios Avanzados del IPN, Unidad Irapuato, Km. 9.6 Libramiento Norte, Carretera Irapuato-León, 36500 Irapuato, Guanajuato, Mexico.</nlm:affiliation><country xml:lang="fr">Mexique</country><wicri:regionArea>Centro de Investigación y de Estudios Avanzados del IPN, Unidad Irapuato, Km. 9.6 Libramiento Norte, Carretera Irapuato-León, 36500 Irapuato, Guanajuato</wicri:regionArea><wicri:noRegion>Guanajuato</wicri:noRegion></affiliation></author><author><name sortKey="Ortiz Vazquez, Elizabeth" sort="Ortiz Vazquez, Elizabeth" uniqKey="Ortiz Vazquez E" first="Elizabeth" last="Ortiz-Vázquez">Elizabeth Ortiz-Vázquez</name><affiliation wicri:level="1"><nlm:affiliation>Instituto Tecnológico de Mérida, Av. Tecnológico, 97118 Mérida, Yucatán, Mexico.</nlm:affiliation><country xml:lang="fr">Mexique</country><wicri:regionArea>Instituto Tecnológico de Mérida, Av. Tecnológico, 97118 Mérida, Yucatán</wicri:regionArea><wicri:noRegion>Yucatán</wicri:noRegion></affiliation></author><author><name sortKey="Fernandez, Francisco" sort="Fernandez, Francisco" uniqKey="Fernandez F" first="Francisco" last="Fernández">Francisco Fernández</name><affiliation wicri:level="1"><nlm:affiliation>Centro de Física Aplicada y Tecnología Avanzada, Universidad Nacional Autónoma de México, Boulevard Juriquilla 3001, 76230 Querétaro, Mexico.</nlm:affiliation><country xml:lang="fr">Mexique</country><wicri:regionArea>Centro de Física Aplicada y Tecnología Avanzada, Universidad Nacional Autónoma de México, Boulevard Juriquilla 3001, 76230 Querétaro</wicri:regionArea><wicri:noRegion>76230 Querétaro</wicri:noRegion></affiliation></author><author><name sortKey="Loske, Achim M" sort="Loske, Achim M" uniqKey="Loske A" first="Achim M" last="Loske">Achim M. Loske</name><affiliation wicri:level="1"><nlm:affiliation>Centro de Física Aplicada y Tecnología Avanzada, Universidad Nacional Autónoma de México, Boulevard Juriquilla 3001, 76230 Querétaro, Mexico; División de Ciencias de la Salud, Universidad del Valle de México, Villas del Mesón 1000, 76230 Querétaro, Mexico.</nlm:affiliation><country xml:lang="fr">Mexique</country><wicri:regionArea>Centro de Física Aplicada y Tecnología Avanzada, Universidad Nacional Autónoma de México, Boulevard Juriquilla 3001, 76230 Querétaro, Mexico; División de Ciencias de la Salud, Universidad del Valle de México, Villas del Mesón 1000, 76230 Querétaro</wicri:regionArea><wicri:noRegion>76230 Querétaro</wicri:noRegion></affiliation></author><author><name sortKey="G Mez Lim, Miguel A" sort="G Mez Lim, Miguel A" uniqKey="G Mez Lim M" first="Miguel A" last="G Mez-Lim">Miguel A. G Mez-Lim</name><affiliation wicri:level="1"><nlm:affiliation>Centro de Investigación y de Estudios Avanzados del IPN, Unidad Irapuato, Km. 9.6 Libramiento Norte, Carretera Irapuato-León, 36500 Irapuato, Guanajuato, Mexico. Electronic address: mgomez@ira.cinvestav.mx.</nlm:affiliation><country xml:lang="fr">Mexique</country><wicri:regionArea>Centro de Investigación y de Estudios Avanzados del IPN, Unidad Irapuato, Km. 9.6 Libramiento Norte, Carretera Irapuato-León, 36500 Irapuato, Guanajuato</wicri:regionArea><wicri:noRegion>Guanajuato</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:26113215</idno><idno type="pmid">26113215</idno><idno type="doi">10.1016/j.jbiotec.2015.06.401</idno><idno type="wicri:Area/Main/Corpus">000250</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000250</idno><idno type="wicri:Area/Main/Curation">000250</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000250</idno><idno type="wicri:Area/Main/Exploration">000250</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Recombinant expression of four oxidoreductases in Phanerochaete chrysosporium improves degradation of phenolic and non-phenolic substrates.</title><author><name sortKey="Coconi Linares, Nancy" sort="Coconi Linares, Nancy" uniqKey="Coconi Linares N" first="Nancy" last="Coconi-Linares">Nancy Coconi-Linares</name><affiliation wicri:level="1"><nlm:affiliation>Centro de Investigación y de Estudios Avanzados del IPN, Unidad Irapuato, Km. 9.6 Libramiento Norte, Carretera Irapuato-León, 36500 Irapuato, Guanajuato, Mexico.</nlm:affiliation><country xml:lang="fr">Mexique</country><wicri:regionArea>Centro de Investigación y de Estudios Avanzados del IPN, Unidad Irapuato, Km. 9.6 Libramiento Norte, Carretera Irapuato-León, 36500 Irapuato, Guanajuato</wicri:regionArea><wicri:noRegion>Guanajuato</wicri:noRegion></affiliation></author><author><name sortKey="Ortiz Vazquez, Elizabeth" sort="Ortiz Vazquez, Elizabeth" uniqKey="Ortiz Vazquez E" first="Elizabeth" last="Ortiz-Vázquez">Elizabeth Ortiz-Vázquez</name><affiliation wicri:level="1"><nlm:affiliation>Instituto Tecnológico de Mérida, Av. Tecnológico, 97118 Mérida, Yucatán, Mexico.</nlm:affiliation><country xml:lang="fr">Mexique</country><wicri:regionArea>Instituto Tecnológico de Mérida, Av. Tecnológico, 97118 Mérida, Yucatán</wicri:regionArea><wicri:noRegion>Yucatán</wicri:noRegion></affiliation></author><author><name sortKey="Fernandez, Francisco" sort="Fernandez, Francisco" uniqKey="Fernandez F" first="Francisco" last="Fernández">Francisco Fernández</name><affiliation wicri:level="1"><nlm:affiliation>Centro de Física Aplicada y Tecnología Avanzada, Universidad Nacional Autónoma de México, Boulevard Juriquilla 3001, 76230 Querétaro, Mexico.</nlm:affiliation><country xml:lang="fr">Mexique</country><wicri:regionArea>Centro de Física Aplicada y Tecnología Avanzada, Universidad Nacional Autónoma de México, Boulevard Juriquilla 3001, 76230 Querétaro</wicri:regionArea><wicri:noRegion>76230 Querétaro</wicri:noRegion></affiliation></author><author><name sortKey="Loske, Achim M" sort="Loske, Achim M" uniqKey="Loske A" first="Achim M" last="Loske">Achim M. Loske</name><affiliation wicri:level="1"><nlm:affiliation>Centro de Física Aplicada y Tecnología Avanzada, Universidad Nacional Autónoma de México, Boulevard Juriquilla 3001, 76230 Querétaro, Mexico; División de Ciencias de la Salud, Universidad del Valle de México, Villas del Mesón 1000, 76230 Querétaro, Mexico.</nlm:affiliation><country xml:lang="fr">Mexique</country><wicri:regionArea>Centro de Física Aplicada y Tecnología Avanzada, Universidad Nacional Autónoma de México, Boulevard Juriquilla 3001, 76230 Querétaro, Mexico; División de Ciencias de la Salud, Universidad del Valle de México, Villas del Mesón 1000, 76230 Querétaro</wicri:regionArea><wicri:noRegion>76230 Querétaro</wicri:noRegion></affiliation></author><author><name sortKey="G Mez Lim, Miguel A" sort="G Mez Lim, Miguel A" uniqKey="G Mez Lim M" first="Miguel A" last="G Mez-Lim">Miguel A. G Mez-Lim</name><affiliation wicri:level="1"><nlm:affiliation>Centro de Investigación y de Estudios Avanzados del IPN, Unidad Irapuato, Km. 9.6 Libramiento Norte, Carretera Irapuato-León, 36500 Irapuato, Guanajuato, Mexico. Electronic address: mgomez@ira.cinvestav.mx.</nlm:affiliation><country xml:lang="fr">Mexique</country><wicri:regionArea>Centro de Investigación y de Estudios Avanzados del IPN, Unidad Irapuato, Km. 9.6 Libramiento Norte, Carretera Irapuato-León, 36500 Irapuato, Guanajuato</wicri:regionArea><wicri:noRegion>Guanajuato</wicri:noRegion></affiliation></author></analytic><series><title level="j">Journal of biotechnology</title><idno type="eISSN">1873-4863</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cloning, Molecular (MeSH)</term><term>Fungal Proteins (genetics)</term><term>Fungal Proteins (metabolism)</term><term>Laccase (genetics)</term><term>Laccase (metabolism)</term><term>Metabolic Engineering (methods)</term><term>Peroxidases (genetics)</term><term>Peroxidases (metabolism)</term><term>Phanerochaete (enzymology)</term><term>Phanerochaete (genetics)</term><term>Phanerochaete (metabolism)</term><term>Phenols (metabolism)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Transformation, Genetic (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Clonage moléculaire (MeSH)</term><term>Génie métabolique (méthodes)</term><term>Laccase (génétique)</term><term>Laccase (métabolisme)</term><term>Peroxidases (génétique)</term><term>Peroxidases (métabolisme)</term><term>Phanerochaete (enzymologie)</term><term>Phanerochaete (génétique)</term><term>Phanerochaete (métabolisme)</term><term>Phénols (métabolisme)</term><term>Protéines fongiques (génétique)</term><term>Protéines fongiques (métabolisme)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Transformation génétique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Fungal Proteins</term><term>Laccase</term><term>Peroxidases</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fungal Proteins</term><term>Laccase</term><term>Peroxidases</term><term>Phenols</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Laccase</term><term>Peroxidases</term><term>Phanerochaete</term><term>Protéines fongiques</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Metabolic Engineering</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Laccase</term><term>Peroxidases</term><term>Phanerochaete</term><term>Phénols</term><term>Protéines fongiques</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Génie métabolique</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cloning, Molecular</term><term>Transformation, Genetic</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Clonage moléculaire</term><term>Transformation génétique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Phanerochaete chrysosporium belongs to a group of lignin-degrading fungi that secretes various oxidoreductive enzymes, including lignin peroxidase (LiP) and manganese peroxidase (MnP). Previously, we demonstrated that the heterologous expression of a versatile peroxidase (VP) in P. chrysosporium recombinant strains is possible. However, the production of laccases (Lac) in this fungus has not been completely demonstrated and remains controversial. In order to investigate if the co-expression of Lac and VP in P. chrysosporium would improve the degradation of phenolic and non-phenolic substrates, we tested the constitutive co-expression of the lacIIIb gene from Trametes versicolor and the vpl2 gene from Pleurotus eryngii, and also the endogenous genes mnp1 and lipH8 by shock wave mediated transformation. The co-overexpression of peroxidases and laccases was improved up to five-fold as compared with wild type species. Transformant strains showed a broad spectrum in phenolic/non-phenolic biotransformation and a high percentage in synthetic dye decolorization in comparison with the parental strain. Our results show that the four enzymes can be constitutively expressed in a single transformant of P. chrysosporium in minimal medium. These data offer new possibilities for an easy and efficient co-expression of laccases and peroxidases in suitable basidiomycete species. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26113215</PMID><DateCompleted><Year>2016</Year><Month>05</Month><Day>04</Day></DateCompleted><DateRevised><Year>2015</Year><Month>08</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-4863</ISSN><JournalIssue CitedMedium="Internet"><Volume>209</Volume><PubDate><Year>2015</Year><Month>Sep</Month><Day>10</Day></PubDate></JournalIssue><Title>Journal of biotechnology</Title><ISOAbbreviation>J Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Recombinant expression of four oxidoreductases in Phanerochaete chrysosporium improves degradation of phenolic and non-phenolic substrates.</ArticleTitle><Pagination><MedlinePgn>76-84</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jbiotec.2015.06.401</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0168-1656(15)30027-4</ELocationID><Abstract><AbstractText>Phanerochaete chrysosporium belongs to a group of lignin-degrading fungi that secretes various oxidoreductive enzymes, including lignin peroxidase (LiP) and manganese peroxidase (MnP). Previously, we demonstrated that the heterologous expression of a versatile peroxidase (VP) in P. chrysosporium recombinant strains is possible. However, the production of laccases (Lac) in this fungus has not been completely demonstrated and remains controversial. In order to investigate if the co-expression of Lac and VP in P. chrysosporium would improve the degradation of phenolic and non-phenolic substrates, we tested the constitutive co-expression of the lacIIIb gene from Trametes versicolor and the vpl2 gene from Pleurotus eryngii, and also the endogenous genes mnp1 and lipH8 by shock wave mediated transformation. The co-overexpression of peroxidases and laccases was improved up to five-fold as compared with wild type species. Transformant strains showed a broad spectrum in phenolic/non-phenolic biotransformation and a high percentage in synthetic dye decolorization in comparison with the parental strain. Our results show that the four enzymes can be constitutively expressed in a single transformant of P. chrysosporium in minimal medium. These data offer new possibilities for an easy and efficient co-expression of laccases and peroxidases in suitable basidiomycete species. </AbstractText><CopyrightInformation>Copyright © 2015 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Coconi-Linares</LastName><ForeName>Nancy</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Centro de Investigación y de Estudios Avanzados del IPN, Unidad Irapuato, Km. 9.6 Libramiento Norte, Carretera Irapuato-León, 36500 Irapuato, Guanajuato, Mexico.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ortiz-Vázquez</LastName><ForeName>Elizabeth</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Instituto Tecnológico de Mérida, Av. Tecnológico, 97118 Mérida, Yucatán, Mexico.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fernández</LastName><ForeName>Francisco</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Centro de Física Aplicada y Tecnología Avanzada, Universidad Nacional Autónoma de México, Boulevard Juriquilla 3001, 76230 Querétaro, Mexico.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Loske</LastName><ForeName>Achim M</ForeName><Initials>AM</Initials><AffiliationInfo><Affiliation>Centro de Física Aplicada y Tecnología Avanzada, Universidad Nacional Autónoma de México, Boulevard Juriquilla 3001, 76230 Querétaro, Mexico; División de Ciencias de la Salud, Universidad del Valle de México, Villas del Mesón 1000, 76230 Querétaro, Mexico.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gómez-Lim</LastName><ForeName>Miguel A</ForeName><Initials>MA</Initials><AffiliationInfo><Affiliation>Centro de Investigación y de Estudios Avanzados del IPN, Unidad Irapuato, Km. 9.6 Libramiento Norte, Carretera Irapuato-León, 36500 Irapuato, Guanajuato, Mexico. Electronic address: mgomez@ira.cinvestav.mx.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>06</Month><Day>22</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>J Biotechnol</MedlineTA><NlmUniqueID>8411927</NlmUniqueID><ISSNLinking>0168-1656</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010636">Phenols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.10.3.2</RegistryNumber><NameOfSubstance UI="D042845">Laccase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D042845" MajorTopicYN="N">Laccase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D060847" MajorTopicYN="N">Metabolic Engineering</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</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="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010636" MajorTopicYN="N">Phenols</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014170" MajorTopicYN="N">Transformation, Genetic</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Fungal oxidoreductases</Keyword><Keyword MajorTopicYN="N">Heterologous expression</Keyword><Keyword MajorTopicYN="N">Laccase</Keyword><Keyword MajorTopicYN="N">Phanerochaete chrysosporium</Keyword><Keyword MajorTopicYN="N">Phenolic compounds degradation</Keyword><Keyword MajorTopicYN="N">Shock waves</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>04</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>06</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>06</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>6</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>6</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>5</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26113215</ArticleId><ArticleId IdType="pii">S0168-1656(15)30027-4</ArticleId><ArticleId IdType="doi">10.1016/j.jbiotec.2015.06.401</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Mexique</li></country></list><tree><country name="Mexique"><noRegion><name sortKey="Coconi Linares, Nancy" sort="Coconi Linares, Nancy" uniqKey="Coconi Linares N" first="Nancy" last="Coconi-Linares">Nancy Coconi-Linares</name></noRegion><name sortKey="Fernandez, Francisco" sort="Fernandez, Francisco" uniqKey="Fernandez F" first="Francisco" last="Fernández">Francisco Fernández</name><name sortKey="G Mez Lim, Miguel A" sort="G Mez Lim, Miguel A" uniqKey="G Mez Lim M" first="Miguel A" last="G Mez-Lim">Miguel A. G Mez-Lim</name><name sortKey="Loske, Achim M" sort="Loske, Achim M" uniqKey="Loske A" first="Achim M" last="Loske">Achim M. Loske</name><name sortKey="Ortiz Vazquez, Elizabeth" sort="Ortiz Vazquez, Elizabeth" uniqKey="Ortiz Vazquez E" first="Elizabeth" last="Ortiz-Vázquez">Elizabeth Ortiz-Vázquez</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PhanerochaeteV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000252 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000252 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= PhanerochaeteV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:26113215
|texte= Recombinant expression of four oxidoreductases in Phanerochaete chrysosporium improves degradation of phenolic and non-phenolic substrates.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:26113215" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a PhanerochaeteV1
| This area was generated with Dilib version V0.6.37. |  |