Improvement of ethanol production by recombinant expression of pyruvate decarboxylase in the white-rot fungus Phanerochaete sordida YK-624.
Identifieur interne : 000202 ( Main/Exploration ); précédent : 000201; suivant : 000203Improvement of ethanol production by recombinant expression of pyruvate decarboxylase in the white-rot fungus Phanerochaete sordida YK-624.
Auteurs : Jianqiao Wang [Japon] ; Sho Hirabayashi [Japon] ; Toshio Mori [Japon] ; Hirokazu Kawagishi [Japon] ; Hirofumi Hirai [Japon]Source :
- Journal of bioscience and bioengineering [ 1347-4421 ] ; 2016.
Descripteurs français
- KwdFr :
- MESH :
- génétique : Phanerochaete, Protéines recombinantes, Pyruvate decarboxylase.
- métabolisme : Phanerochaete, Protéines recombinantes, Pyruvate decarboxylase, Éthanol.
- Bioréacteurs, Fermentation, Génie métabolique.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Pyruvate Decarboxylase, Recombinant Proteins.
- chemical , metabolism : Ethanol, Pyruvate Decarboxylase, Recombinant Proteins.
- genetics : Phanerochaete.
- metabolism : Phanerochaete.
- Bioreactors, Fermentation, Metabolic Engineering.
Abstract
To improve ethanol production by Phanerochaete sordida YK-624, the pyruvate decarboxylase (PDC) gene was cloned from and reintroduced into this hyper lignin-degrading fungus; the gene encodes a key enzyme in alcoholic fermentation. We screened 16 transformant P. sordida YK-624 strains that each expressed a second, recombinant PDC gene (pdc) and then identified the transformant strain (designated GP7) with the highest ethanol production. Direct ethanol production from hardwood was 1.41 higher with GP7 than with wild-type P. sordida YK-624. RT-PCR analysis indicated that the increased PDC activity was caused by elevated recombinant pdc expression. Taken together, these results suggested that ethanol production by P. sordida YK-624 can be improved by the stable expression of an additional, recombinant pdc.
DOI: 10.1016/j.jbiosc.2015.12.002
PubMed: 26766784
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Electronic address: hirai.hirofumi@shizuoka.ac.jp.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Faculty of Agriculture, Shizuoka University, 836 Ohya, Suruga-ku, Shizuoka 422-8529, Japan; Research Institute of Green Science and Technology, Shizuoka University, 836 Ohya, Suruga-ku, Shizuoka 422-8529</wicri:regionArea><wicri:noRegion>Shizuoka 422-8529</wicri:noRegion></affiliation></author></analytic><series><title level="j">Journal of bioscience and bioengineering</title><idno type="eISSN">1347-4421</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bioreactors (MeSH)</term><term>Ethanol (metabolism)</term><term>Fermentation (MeSH)</term><term>Metabolic Engineering (MeSH)</term><term>Phanerochaete (genetics)</term><term>Phanerochaete (metabolism)</term><term>Pyruvate Decarboxylase (genetics)</term><term>Pyruvate Decarboxylase (metabolism)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Bioréacteurs (MeSH)</term><term>Fermentation (MeSH)</term><term>Génie métabolique (MeSH)</term><term>Phanerochaete (génétique)</term><term>Phanerochaete (métabolisme)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Pyruvate decarboxylase (génétique)</term><term>Pyruvate decarboxylase (métabolisme)</term><term>Éthanol (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Pyruvate Decarboxylase</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Ethanol</term><term>Pyruvate Decarboxylase</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Phanerochaete</term><term>Protéines recombinantes</term><term>Pyruvate decarboxylase</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Phanerochaete</term><term>Protéines recombinantes</term><term>Pyruvate decarboxylase</term><term>Éthanol</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Bioreactors</term><term>Fermentation</term><term>Metabolic Engineering</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Bioréacteurs</term><term>Fermentation</term><term>Génie métabolique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">To improve ethanol production by Phanerochaete sordida YK-624, the pyruvate decarboxylase (PDC) gene was cloned from and reintroduced into this hyper lignin-degrading fungus; the gene encodes a key enzyme in alcoholic fermentation. We screened 16 transformant P. sordida YK-624 strains that each expressed a second, recombinant PDC gene (pdc) and then identified the transformant strain (designated GP7) with the highest ethanol production. Direct ethanol production from hardwood was 1.41 higher with GP7 than with wild-type P. sordida YK-624. RT-PCR analysis indicated that the increased PDC activity was caused by elevated recombinant pdc expression. Taken together, these results suggested that ethanol production by P. sordida YK-624 can be improved by the stable expression of an additional, recombinant pdc. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" IndexingMethod="Curated" Owner="NLM"><PMID Version="1">26766784</PMID><DateCompleted><Year>2017</Year><Month>03</Month><Day>09</Day></DateCompleted><DateRevised><Year>2018</Year><Month>12</Month><Day>02</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1347-4421</ISSN><JournalIssue CitedMedium="Internet"><Volume>122</Volume><Issue>1</Issue><PubDate><Year>2016</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Journal of bioscience and bioengineering</Title><ISOAbbreviation>J Biosci Bioeng</ISOAbbreviation></Journal><ArticleTitle>Improvement of ethanol production by recombinant expression of pyruvate decarboxylase in the white-rot fungus Phanerochaete sordida YK-624.</ArticleTitle><Pagination><MedlinePgn>17-21</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jbiosc.2015.12.002</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S1389-1723(15)00439-9</ELocationID><Abstract><AbstractText>To improve ethanol production by Phanerochaete sordida YK-624, the pyruvate decarboxylase (PDC) gene was cloned from and reintroduced into this hyper lignin-degrading fungus; the gene encodes a key enzyme in alcoholic fermentation. We screened 16 transformant P. sordida YK-624 strains that each expressed a second, recombinant PDC gene (pdc) and then identified the transformant strain (designated GP7) with the highest ethanol production. Direct ethanol production from hardwood was 1.41 higher with GP7 than with wild-type P. sordida YK-624. RT-PCR analysis indicated that the increased PDC activity was caused by elevated recombinant pdc expression. Taken together, these results suggested that ethanol production by P. sordida YK-624 can be improved by the stable expression of an additional, recombinant pdc. </AbstractText><CopyrightInformation>Copyright © 2015 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Jianqiao</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Faculty of Agriculture, Shizuoka University, 836 Ohya, Suruga-ku, Shizuoka 422-8529, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hirabayashi</LastName><ForeName>Sho</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Graduate School of Agriculture, Shizuoka University, 836 Ohya, Suruga-ku, Shizuoka 422-8529, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mori</LastName><ForeName>Toshio</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Faculty of Agriculture, Shizuoka University, 836 Ohya, Suruga-ku, Shizuoka 422-8529, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kawagishi</LastName><ForeName>Hirokazu</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Faculty of Agriculture, Shizuoka University, 836 Ohya, Suruga-ku, Shizuoka 422-8529, Japan; Research Institute of Green Science and Technology, Shizuoka University, 836 Ohya, Suruga-ku, Shizuoka 422-8529, Japan; Graduate School of Science and Technology, Shizuoka University, 836 Ohya, Suruga-ku, Shizuoka 422-8529, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hirai</LastName><ForeName>Hirofumi</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Faculty of Agriculture, Shizuoka University, 836 Ohya, Suruga-ku, Shizuoka 422-8529, Japan; Research Institute of Green Science and Technology, Shizuoka University, 836 Ohya, Suruga-ku, Shizuoka 422-8529, Japan. Electronic address: hirai.hirofumi@shizuoka.ac.jp.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>01</Month><Day>04</Day></ArticleDate></Article><MedlineJournalInfo><Country>Japan</Country><MedlineTA>J Biosci Bioeng</MedlineTA><NlmUniqueID>100888800</NlmUniqueID><ISSNLinking>1347-4421</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>3K9958V90M</RegistryNumber><NameOfSubstance UI="D000431">Ethanol</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.1.1.1</RegistryNumber><NameOfSubstance UI="D011767">Pyruvate Decarboxylase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D019149" MajorTopicYN="N">Bioreactors</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000431" MajorTopicYN="N">Ethanol</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005285" MajorTopicYN="Y">Fermentation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D060847" MajorTopicYN="N">Metabolic Engineering</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011767" MajorTopicYN="N">Pyruvate Decarboxylase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">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></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Ethanol production</Keyword><Keyword MajorTopicYN="N">Phanerochaete sordida YK-624</Keyword><Keyword MajorTopicYN="N">Pyruvate decarboxylase</Keyword><Keyword MajorTopicYN="N">Recombinant expression</Keyword><Keyword MajorTopicYN="N">White-rot fungi</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>07</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>12</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>12</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>1</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>1</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>3</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26766784</ArticleId><ArticleId IdType="pii">S1389-1723(15)00439-9</ArticleId><ArticleId IdType="doi">10.1016/j.jbiosc.2015.12.002</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country></list><tree><country name="Japon"><noRegion><name sortKey="Wang, Jianqiao" sort="Wang, Jianqiao" uniqKey="Wang J" first="Jianqiao" last="Wang">Jianqiao Wang</name></noRegion><name sortKey="Hirabayashi, Sho" sort="Hirabayashi, Sho" uniqKey="Hirabayashi S" first="Sho" last="Hirabayashi">Sho Hirabayashi</name><name sortKey="Hirai, Hirofumi" sort="Hirai, Hirofumi" uniqKey="Hirai H" first="Hirofumi" last="Hirai">Hirofumi Hirai</name><name sortKey="Kawagishi, Hirokazu" sort="Kawagishi, Hirokazu" uniqKey="Kawagishi H" first="Hirokazu" last="Kawagishi">Hirokazu Kawagishi</name><name sortKey="Mori, Toshio" sort="Mori, Toshio" uniqKey="Mori T" first="Toshio" last="Mori">Toshio Mori</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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