Production and characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase in the methylotrophic yeast Pichia pastoris.
Identifieur interne : 000A30 ( Main/Curation ); précédent : 000A29; suivant : 000A31Production and characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase in the methylotrophic yeast Pichia pastoris.
Auteurs : M. Yoshida [Japon] ; T. Ohira ; K. Igarashi ; H. Nagasawa ; K. Aida ; B M Hallberg ; C. Divne ; T. Nishino ; M. SamejimaSource :
- Bioscience, biotechnology, and biochemistry [ 0916-8451 ] ; 2001.
Descripteurs français
- KwdFr :
- Carbohydrate dehydrogenases (composition chimique), Carbohydrate dehydrogenases (génétique), Carbohydrate dehydrogenases (métabolisme), Cellulose (métabolisme), Cinétique (MeSH), Clonage moléculaire (MeSH), Ingénierie des protéines (méthodes), Phanerochaete (enzymologie), Phanerochaete (génétique), Pichia (génétique), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Transformation génétique (MeSH), Vecteurs génétiques (MeSH).
- MESH :
- composition chimique : Carbohydrate dehydrogenases.
- enzymologie : Phanerochaete.
- génétique : Carbohydrate dehydrogenases, Phanerochaete, Pichia, Protéines recombinantes.
- métabolisme : Carbohydrate dehydrogenases, Cellulose, Protéines recombinantes.
- méthodes : Ingénierie des protéines.
- Cinétique, Clonage moléculaire, Transformation génétique, Vecteurs génétiques.
English descriptors
- KwdEn :
- Carbohydrate Dehydrogenases (chemistry), Carbohydrate Dehydrogenases (genetics), Carbohydrate Dehydrogenases (metabolism), Cellulose (metabolism), Cloning, Molecular (MeSH), Genetic Vectors (MeSH), Kinetics (MeSH), Phanerochaete (enzymology), Phanerochaete (genetics), Pichia (genetics), Protein Engineering (methods), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Transformation, Genetic (MeSH).
- MESH :
- chemical , chemistry : Carbohydrate Dehydrogenases.
- chemical , genetics : Carbohydrate Dehydrogenases, Recombinant Proteins.
- chemical , metabolism : Carbohydrate Dehydrogenases, Cellulose, Recombinant Proteins.
- enzymology : Phanerochaete.
- genetics : Phanerochaete, Pichia.
- methods : Protein Engineering.
- Cloning, Molecular, Genetic Vectors, Kinetics, Transformation, Genetic.
Abstract
The hemoflavoenzyme cellobiose dehydrogenase (CDH) from the white-rot fungus Phanerochaete chrysosporium has been heterologously expressed in the methylotrophic yeast Pichia pastoris. After 4 days of cultivation in the induction medium, the expression level reached 1800 U/L (79 mg/L) of CDH activity, which is considerably higher than that obtained previously for wild-type CDH (wtCDH) and recombinant CDH (rCDH) produced by P. chrysosporium. Analysis with SDS-PAGE and Coomassie Brilliant Blue (CBB) staining revealed a major protein band with an approximate molecular mass of 100 kDa, which was identified as rCDH by Western blotting. The absorption spectrum of rCDH shows that the protein contains one flavin and one heme cofactor per protein molecule, as does wtCDH. The kinetic parameters for rCDH using cellobiose, ubiquinone, and cytochrome c, as well as the cellulose-binding properties of rCDH were nearly identical to those of wtCDH. From these results, we conclude that the rCDH produced by Pichia pastoris retains the catalytic and cellulose-binding properties of the wild-type enzyme, and that the Pichia expression system is well suited for high-level production of rCDH.
DOI: 10.1271/bbb.65.2050
PubMed: 11676020
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pubmed:11676020Le document en format XML
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After 4 days of cultivation in the induction medium, the expression level reached 1800 U/L (79 mg/L) of CDH activity, which is considerably higher than that obtained previously for wild-type CDH (wtCDH) and recombinant CDH (rCDH) produced by P. chrysosporium. Analysis with SDS-PAGE and Coomassie Brilliant Blue (CBB) staining revealed a major protein band with an approximate molecular mass of 100 kDa, which was identified as rCDH by Western blotting. The absorption spectrum of rCDH shows that the protein contains one flavin and one heme cofactor per protein molecule, as does wtCDH. The kinetic parameters for rCDH using cellobiose, ubiquinone, and cytochrome c, as well as the cellulose-binding properties of rCDH were nearly identical to those of wtCDH. From these results, we conclude that the rCDH produced by Pichia pastoris retains the catalytic and cellulose-binding properties of the wild-type enzyme, and that the Pichia expression system is well suited for high-level production of rCDH.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11676020</PMID><DateCompleted><Year>2002</Year><Month>05</Month><Day>06</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>10</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0916-8451</ISSN><JournalIssue CitedMedium="Print"><Volume>65</Volume><Issue>9</Issue><PubDate><Year>2001</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Bioscience, biotechnology, and biochemistry</Title><ISOAbbreviation>Biosci Biotechnol Biochem</ISOAbbreviation></Journal><ArticleTitle>Production and characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase in the methylotrophic yeast Pichia pastoris.</ArticleTitle><Pagination><MedlinePgn>2050-7</MedlinePgn></Pagination><Abstract><AbstractText>The hemoflavoenzyme cellobiose dehydrogenase (CDH) from the white-rot fungus Phanerochaete chrysosporium has been heterologously expressed in the methylotrophic yeast Pichia pastoris. After 4 days of cultivation in the induction medium, the expression level reached 1800 U/L (79 mg/L) of CDH activity, which is considerably higher than that obtained previously for wild-type CDH (wtCDH) and recombinant CDH (rCDH) produced by P. chrysosporium. Analysis with SDS-PAGE and Coomassie Brilliant Blue (CBB) staining revealed a major protein band with an approximate molecular mass of 100 kDa, which was identified as rCDH by Western blotting. The absorption spectrum of rCDH shows that the protein contains one flavin and one heme cofactor per protein molecule, as does wtCDH. The kinetic parameters for rCDH using cellobiose, ubiquinone, and cytochrome c, as well as the cellulose-binding properties of rCDH were nearly identical to those of wtCDH. From these results, we conclude that the rCDH produced by Pichia pastoris retains the catalytic and cellulose-binding properties of the wild-type enzyme, and that the Pichia expression system is well suited for high-level production of rCDH.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yoshida</LastName><ForeName>M</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Graduate School of Agricultural and Life Sciences, The University of Tokyo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ohira</LastName><ForeName>T</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Igarashi</LastName><ForeName>K</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Nagasawa</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Aida</LastName><ForeName>K</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Hallberg</LastName><ForeName>B M</ForeName><Initials>BM</Initials></Author><Author ValidYN="Y"><LastName>Divne</LastName><ForeName>C</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Nishino</LastName><ForeName>T</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Samejima</LastName><ForeName>M</ForeName><Initials>M</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></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Biosci Biotechnol Biochem</MedlineTA><NlmUniqueID>9205717</NlmUniqueID><ISSNLinking>0916-8451</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9004-34-6</RegistryNumber><NameOfSubstance UI="D002482">Cellulose</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D002237">Carbohydrate Dehydrogenases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.99.18</RegistryNumber><NameOfSubstance UI="C019859">cellobiose-quinone oxidoreductase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002237" MajorTopicYN="N">Carbohydrate Dehydrogenases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002482" MajorTopicYN="N">Cellulose</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005822" MajorTopicYN="N">Genetic Vectors</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010843" MajorTopicYN="N">Pichia</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015202" MajorTopicYN="N">Protein Engineering</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</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></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2001</Year><Month>10</Month><Day>26</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2002</Year><Month>5</Month><Day>7</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2001</Year><Month>10</Month><Day>26</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11676020</ArticleId><ArticleId IdType="doi">10.1271/bbb.65.2050</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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