High-yield production of manganese peroxidase, lignin peroxidase, and versatile peroxidase in Phanerochaete chrysosporium.
Identifieur interne : 000294 ( Main/Corpus ); précédent : 000293; suivant : 000295High-yield production of manganese peroxidase, lignin peroxidase, and versatile peroxidase in Phanerochaete chrysosporium.
Auteurs : Nancy Coconi-Linares ; Denis Maga A-Ortíz ; Doralinda A. Guzmán-Ortiz ; Francisco Fernández ; Achim M. Loske ; Miguel A. G Mez-LimSource :
- Applied microbiology and biotechnology [ 1432-0614 ] ; 2014.
English descriptors
- KwdEn :
- Cloning, Molecular (MeSH), Gene Expression (MeSH), Metabolic Engineering (MeSH), Molecular Sequence Data (MeSH), Peroxidases (genetics), Peroxidases (metabolism), Phanerochaete (genetics), Phanerochaete (metabolism), Pleurotus (enzymology), Pleurotus (genetics), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Sequence Analysis, DNA (MeSH), Transformation, Genetic (MeSH).
- MESH :
- chemical , genetics : Peroxidases, Recombinant Proteins.
- chemical , metabolism : Peroxidases, Recombinant Proteins.
- enzymology : Pleurotus.
- genetics : Phanerochaete, Pleurotus.
- metabolism : Phanerochaete.
- Cloning, Molecular, Gene Expression, Metabolic Engineering, Molecular Sequence Data, Sequence Analysis, DNA, Transformation, Genetic.
Abstract
The white-rot fungus Phanerochaete chrysosporium secretes extracellular oxidative enzymes during secondary metabolism, but lacks versatile peroxidase, an enzyme important in ligninolysis and diverse biotechnology processes. In this study, we report the genetic modification of a P. chrysosporium strain capable of co-expressing two endogenous genes constitutively, manganese peroxidase (mnp1) and lignin peroxidase (lipH8), and the codon-optimized vpl2 gene from Pleurotus eryngii. For this purpose, we employed a highly efficient transformation method based on the use of shock waves developed by our group. The expression of recombinant genes was verified by PCR, Southern blot, quantitative real-time PCR (qRT-PCR), and assays of enzymatic activity. The production yield of ligninolytic enzymes was up to four times higher in comparison to previously published reports. These results may represent significant progress toward the stable production of ligninolytic enzymes and the development of an effective fungal strain with promising biotechnological applications.
DOI: 10.1007/s00253-014-6105-9
PubMed: 25269601
Links to Exploration step
pubmed:25269601Le document en format XML
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Guzmán-Ortiz</name></author><author><name sortKey="Fernandez, Francisco" sort="Fernandez, Francisco" uniqKey="Fernandez F" first="Francisco" last="Fernández">Francisco Fernández</name></author><author><name sortKey="Loske, Achim M" sort="Loske, Achim M" uniqKey="Loske A" first="Achim M" last="Loske">Achim M. Loske</name></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></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:25269601</idno><idno type="pmid">25269601</idno><idno type="doi">10.1007/s00253-014-6105-9</idno><idno type="wicri:Area/Main/Corpus">000294</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000294</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">High-yield production of manganese peroxidase, lignin peroxidase, and versatile peroxidase in Phanerochaete chrysosporium.</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><nlm:affiliation>Centro de Investigación y de Estudios Avanzados del IPN, Unidad Irapuato, Km. 9.6 Carretera Irapuato-León, 36821, Irapuato, Gto, Mexico.</nlm:affiliation></affiliation></author><author><name sortKey="Maga A Ortiz, Denis" sort="Maga A Ortiz, Denis" uniqKey="Maga A Ortiz D" first="Denis" last="Maga A-Ortíz">Denis Maga A-Ortíz</name></author><author><name sortKey="Guzman Ortiz, Doralinda A" sort="Guzman Ortiz, Doralinda A" uniqKey="Guzman Ortiz D" first="Doralinda A" last="Guzmán-Ortiz">Doralinda A. Guzmán-Ortiz</name></author><author><name sortKey="Fernandez, Francisco" sort="Fernandez, Francisco" uniqKey="Fernandez F" first="Francisco" last="Fernández">Francisco Fernández</name></author><author><name sortKey="Loske, Achim M" sort="Loske, Achim M" uniqKey="Loske A" first="Achim M" last="Loske">Achim M. Loske</name></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></author></analytic><series><title level="j">Applied microbiology and biotechnology</title><idno type="eISSN">1432-0614</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cloning, Molecular (MeSH)</term><term>Gene Expression (MeSH)</term><term>Metabolic Engineering (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Peroxidases (genetics)</term><term>Peroxidases (metabolism)</term><term>Phanerochaete (genetics)</term><term>Phanerochaete (metabolism)</term><term>Pleurotus (enzymology)</term><term>Pleurotus (genetics)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Sequence Analysis, DNA (MeSH)</term><term>Transformation, Genetic (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Peroxidases</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peroxidases</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Phanerochaete</term><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cloning, Molecular</term><term>Gene Expression</term><term>Metabolic Engineering</term><term>Molecular Sequence Data</term><term>Sequence Analysis, DNA</term><term>Transformation, Genetic</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The white-rot fungus Phanerochaete chrysosporium secretes extracellular oxidative enzymes during secondary metabolism, but lacks versatile peroxidase, an enzyme important in ligninolysis and diverse biotechnology processes. In this study, we report the genetic modification of a P. chrysosporium strain capable of co-expressing two endogenous genes constitutively, manganese peroxidase (mnp1) and lignin peroxidase (lipH8), and the codon-optimized vpl2 gene from Pleurotus eryngii. For this purpose, we employed a highly efficient transformation method based on the use of shock waves developed by our group. The expression of recombinant genes was verified by PCR, Southern blot, quantitative real-time PCR (qRT-PCR), and assays of enzymatic activity. The production yield of ligninolytic enzymes was up to four times higher in comparison to previously published reports. These results may represent significant progress toward the stable production of ligninolytic enzymes and the development of an effective fungal strain with promising biotechnological applications.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25269601</PMID><DateCompleted><Year>2015</Year><Month>06</Month><Day>19</Day></DateCompleted><DateRevised><Year>2014</Year><Month>10</Month><Day>28</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1432-0614</ISSN><JournalIssue CitedMedium="Internet"><Volume>98</Volume><Issue>22</Issue><PubDate><Year>2014</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Applied microbiology and biotechnology</Title><ISOAbbreviation>Appl Microbiol Biotechnol</ISOAbbreviation></Journal><ArticleTitle>High-yield production of manganese peroxidase, lignin peroxidase, and versatile peroxidase in Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>9283-94</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00253-014-6105-9</ELocationID><Abstract><AbstractText>The white-rot fungus Phanerochaete chrysosporium secretes extracellular oxidative enzymes during secondary metabolism, but lacks versatile peroxidase, an enzyme important in ligninolysis and diverse biotechnology processes. In this study, we report the genetic modification of a P. chrysosporium strain capable of co-expressing two endogenous genes constitutively, manganese peroxidase (mnp1) and lignin peroxidase (lipH8), and the codon-optimized vpl2 gene from Pleurotus eryngii. For this purpose, we employed a highly efficient transformation method based on the use of shock waves developed by our group. The expression of recombinant genes was verified by PCR, Southern blot, quantitative real-time PCR (qRT-PCR), and assays of enzymatic activity. The production yield of ligninolytic enzymes was up to four times higher in comparison to previously published reports. These results may represent significant progress toward the stable production of ligninolytic enzymes and the development of an effective fungal strain with promising biotechnological applications.</AbstractText></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 Carretera Irapuato-León, 36821, Irapuato, Gto, Mexico.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Magaña-Ortíz</LastName><ForeName>Denis</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Guzmán-Ortiz</LastName><ForeName>Doralinda A</ForeName><Initials>DA</Initials></Author><Author ValidYN="Y"><LastName>Fernández</LastName><ForeName>Francisco</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Loske</LastName><ForeName>Achim M</ForeName><Initials>AM</Initials></Author><Author ValidYN="Y"><LastName>Gómez-Lim</LastName><ForeName>Miguel A</ForeName><Initials>MA</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>KM206768</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>10</Month><Day>01</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="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="ErratumIn"><RefSource>Appl Microbiol Biotechnol. 2014 Nov;98(22):9519</RefSource></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D060847" MajorTopicYN="Y">Metabolic Engineering</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></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="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020076" MajorTopicYN="N">Pleurotus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</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="D017422" MajorTopicYN="N">Sequence Analysis, DNA</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014170" MajorTopicYN="N">Transformation, Genetic</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>06</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>09</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2014</Year><Month>09</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>10</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>10</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>6</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25269601</ArticleId><ArticleId IdType="doi">10.1007/s00253-014-6105-9</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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