High-yield production of manganese peroxidase, lignin peroxidase, and versatile peroxidase in Phanerochaete chrysosporium.
Identifieur interne : 000317 ( Main/Exploration ); précédent : 000316; suivant : 000318High-yield production of manganese peroxidase, lignin peroxidase, and versatile peroxidase in Phanerochaete chrysosporium.
Auteurs : Nancy Coconi-Linares [Mexique] ; 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.
Descripteurs français
- KwdFr :
- Analyse de séquence d'ADN (MeSH), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Expression des gènes (MeSH), Génie métabolique (MeSH), Peroxidases (génétique), Peroxidases (métabolisme), Phanerochaete (génétique), Phanerochaete (métabolisme), Pleurotus (enzymologie), Pleurotus (génétique), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Transformation génétique (MeSH).
- MESH :
- enzymologie : Pleurotus.
- génétique : Peroxidases, Phanerochaete, Pleurotus, Protéines recombinantes.
- métabolisme : Peroxidases, Phanerochaete, Protéines recombinantes.
- Analyse de séquence d'ADN, Clonage moléculaire, Données de séquences moléculaires, Expression des gènes, Génie métabolique, Transformation génétique.
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
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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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 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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><affiliations><list><country><li>Mexique</li></country></list><tree><noCountry><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="Guzman Ortiz, Doralinda A" sort="Guzman Ortiz, Doralinda A" uniqKey="Guzman Ortiz D" first="Doralinda A" last="Guzmán-Ortiz">Doralinda A. Guzmán-Ortiz</name><name sortKey="Loske, Achim M" sort="Loske, Achim M" uniqKey="Loske A" first="Achim M" last="Loske">Achim M. Loske</name><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></noCountry><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></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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