Heterologous expression of endo-1,4-β-xylanase A from Schizophyllum commune in Pichia pastoris and functional characterization of the recombinant enzyme.
Identifieur interne : 002654 ( Main/Exploration ); précédent : 002653; suivant : 002655Heterologous expression of endo-1,4-β-xylanase A from Schizophyllum commune in Pichia pastoris and functional characterization of the recombinant enzyme.
Auteurs : Younho Song [Corée du Sud] ; Yoon Gyo Lee ; In Seong Choi ; Kwang Ho Lee ; Eun Jin Cho ; Hyeun-Jong BaeSource :
- Enzyme and microbial technology [ 1879-0909 ] ; 2013.
Descripteurs français
- KwdFr :
- ADN complémentaire (génétique), Acide édétique (pharmacologie), Analyse de séquence d'ADN (MeSH), Bois (MeSH), Cadres ouverts de lecture (MeSH), Cations (pharmacologie), Chélateurs (pharmacologie), Cinétique (MeSH), Clonage moléculaire (MeSH), Endo-1,4-beta xylanases (antagonistes et inhibiteurs), Endo-1,4-beta xylanases (génétique), Endo-1,4-beta xylanases (isolement et purification), Endo-1,4-beta xylanases (métabolisme), Fagus (MeSH), Gènes fongiques (MeSH), Hydrolyse (MeSH), Immunohistochimie (MeSH), Pichia (métabolisme), Populus (MeSH), Protéines de fusion recombinantes (métabolisme), Protéines fongiques (antagonistes et inhibiteurs), Protéines fongiques (génétique), Protéines fongiques (isolement et purification), Protéines fongiques (métabolisme), Schizophyllum (enzymologie), Schizophyllum (génétique), Spécificité du substrat (MeSH), Xylanes (métabolisme).
- MESH :
- antagonistes et inhibiteurs : Endo-1,4-beta xylanases, Protéines fongiques.
- enzymologie : Schizophyllum.
- génétique : ADN complémentaire, Endo-1,4-beta xylanases, Protéines fongiques, Schizophyllum.
- isolement et purification : Endo-1,4-beta xylanases, Protéines fongiques.
- métabolisme : Endo-1,4-beta xylanases, Pichia, Protéines de fusion recombinantes, Protéines fongiques, Xylanes.
- pharmacologie : Acide édétique, Cations, Chélateurs.
- Analyse de séquence d'ADN, Bois, Cadres ouverts de lecture, Cinétique, Clonage moléculaire, Fagus, Gènes fongiques, Hydrolyse, Immunohistochimie, Populus, Spécificité du substrat.
English descriptors
- KwdEn :
- Cations (pharmacology), Chelating Agents (pharmacology), Cloning, Molecular (MeSH), DNA, Complementary (genetics), Edetic Acid (pharmacology), Endo-1,4-beta Xylanases (antagonists & inhibitors), Endo-1,4-beta Xylanases (genetics), Endo-1,4-beta Xylanases (isolation & purification), Endo-1,4-beta Xylanases (metabolism), Fagus (MeSH), Fungal Proteins (antagonists & inhibitors), Fungal Proteins (genetics), Fungal Proteins (isolation & purification), Fungal Proteins (metabolism), Genes, Fungal (MeSH), Hydrolysis (MeSH), Immunohistochemistry (MeSH), Kinetics (MeSH), Open Reading Frames (MeSH), Pichia (metabolism), Populus (MeSH), Recombinant Fusion Proteins (metabolism), Schizophyllum (enzymology), Schizophyllum (genetics), Sequence Analysis, DNA (MeSH), Substrate Specificity (MeSH), Wood (MeSH), Xylans (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Endo-1,4-beta Xylanases, Fungal Proteins.
- chemical , genetics : DNA, Complementary, Endo-1,4-beta Xylanases, Fungal Proteins.
- chemical , isolation & purification : Endo-1,4-beta Xylanases, Fungal Proteins.
- chemical , metabolism : Endo-1,4-beta Xylanases, Fungal Proteins, Recombinant Fusion Proteins, Xylans.
- chemical , pharmacology : Cations, Chelating Agents, Edetic Acid.
- enzymology : Schizophyllum.
- genetics : Schizophyllum.
- metabolism : Pichia.
- Cloning, Molecular, Fagus, Genes, Fungal, Hydrolysis, Immunohistochemistry, Kinetics, Open Reading Frames, Populus, Sequence Analysis, DNA, Substrate Specificity, Wood.
Abstract
Endo-1,4-β-xylanase A (XynA) from Schizophyllum commune was cloned into pPCZαA and expressed in Pichia pastoris GS115. The open reading frame of the xynA gene is composed of 684 bp, encoding 278 amino acids with a molecular weight of 26 kDa. Based on sequence similarity, XynA belongs to the CAZy glycoside hydrolase family 11. The optimal activity of XynA was at pH 5 and 50 °C on beechwood xylan. Under these conditions, the K(m), V(max) and specific activity of XynA were 5768 units mg(-1), 4 mg ml(-1) and 9000 μmol min(-1)mg(-1), respectively. XynA activity was enhanced in the presence of cations, such as K(+), Na(+), Li(2+), Cd(2+), and Co(2+). However, in the presence of EDTA, Hg(2+) and Fe(3+), xylanase activity was significantly inhibited. This enzyme effectively degraded approximately 45% of unsubstituted xylans in the cell wall from poplar stems. The high level of XynA activity might increase the yield of enzyme hydrolysis from biomass. Thus, XynA could be used as a major component of a lignocellulosic degrading enzyme cocktail.
DOI: 10.1016/j.enzmictec.2012.12.012
PubMed: 23410928
Affiliations:
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sort="Choi, In Seong" uniqKey="Choi I" first="In Seong" last="Choi">In Seong Choi</name></author><author><name sortKey="Lee, Kwang Ho" sort="Lee, Kwang Ho" uniqKey="Lee K" first="Kwang Ho" last="Lee">Kwang Ho Lee</name></author><author><name sortKey="Cho, Eun Jin" sort="Cho, Eun Jin" uniqKey="Cho E" first="Eun Jin" last="Cho">Eun Jin Cho</name></author><author><name sortKey="Bae, Hyeun Jong" sort="Bae, Hyeun Jong" uniqKey="Bae H" first="Hyeun-Jong" last="Bae">Hyeun-Jong Bae</name></author></analytic><series><title level="j">Enzyme and microbial technology</title><idno type="eISSN">1879-0909</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cations (pharmacology)</term><term>Chelating Agents (pharmacology)</term><term>Cloning, Molecular (MeSH)</term><term>DNA, Complementary (genetics)</term><term>Edetic Acid (pharmacology)</term><term>Endo-1,4-beta Xylanases (antagonists & inhibitors)</term><term>Endo-1,4-beta Xylanases (genetics)</term><term>Endo-1,4-beta Xylanases (isolation & purification)</term><term>Endo-1,4-beta Xylanases (metabolism)</term><term>Fagus (MeSH)</term><term>Fungal Proteins (antagonists & inhibitors)</term><term>Fungal Proteins (genetics)</term><term>Fungal Proteins (isolation & purification)</term><term>Fungal Proteins (metabolism)</term><term>Genes, Fungal (MeSH)</term><term>Hydrolysis (MeSH)</term><term>Immunohistochemistry (MeSH)</term><term>Kinetics (MeSH)</term><term>Open Reading Frames (MeSH)</term><term>Pichia (metabolism)</term><term>Populus (MeSH)</term><term>Recombinant Fusion Proteins (metabolism)</term><term>Schizophyllum (enzymology)</term><term>Schizophyllum (genetics)</term><term>Sequence Analysis, DNA (MeSH)</term><term>Substrate Specificity (MeSH)</term><term>Wood (MeSH)</term><term>Xylans (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN complémentaire (génétique)</term><term>Acide édétique (pharmacologie)</term><term>Analyse de séquence d'ADN (MeSH)</term><term>Bois (MeSH)</term><term>Cadres ouverts de lecture (MeSH)</term><term>Cations (pharmacologie)</term><term>Chélateurs (pharmacologie)</term><term>Cinétique (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Endo-1,4-beta xylanases (antagonistes et inhibiteurs)</term><term>Endo-1,4-beta xylanases (génétique)</term><term>Endo-1,4-beta xylanases (isolement et purification)</term><term>Endo-1,4-beta xylanases (métabolisme)</term><term>Fagus (MeSH)</term><term>Gènes fongiques (MeSH)</term><term>Hydrolyse (MeSH)</term><term>Immunohistochimie (MeSH)</term><term>Pichia (métabolisme)</term><term>Populus (MeSH)</term><term>Protéines de fusion recombinantes (métabolisme)</term><term>Protéines fongiques (antagonistes et inhibiteurs)</term><term>Protéines fongiques (génétique)</term><term>Protéines fongiques (isolement et purification)</term><term>Protéines fongiques (métabolisme)</term><term>Schizophyllum (enzymologie)</term><term>Schizophyllum (génétique)</term><term>Spécificité du substrat (MeSH)</term><term>Xylanes (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Endo-1,4-beta Xylanases</term><term>Fungal Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA, Complementary</term><term>Endo-1,4-beta Xylanases</term><term>Fungal Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Endo-1,4-beta Xylanases</term><term>Fungal Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Endo-1,4-beta Xylanases</term><term>Fungal Proteins</term><term>Recombinant Fusion Proteins</term><term>Xylans</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" 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scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Endo-1,4-beta xylanases</term><term>Pichia</term><term>Protéines de fusion recombinantes</term><term>Protéines fongiques</term><term>Xylanes</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Acide édétique</term><term>Cations</term><term>Chélateurs</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cloning, Molecular</term><term>Fagus</term><term>Genes, Fungal</term><term>Hydrolysis</term><term>Immunohistochemistry</term><term>Kinetics</term><term>Open Reading Frames</term><term>Populus</term><term>Sequence Analysis, DNA</term><term>Substrate Specificity</term><term>Wood</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse de séquence d'ADN</term><term>Bois</term><term>Cadres ouverts de lecture</term><term>Cinétique</term><term>Clonage moléculaire</term><term>Fagus</term><term>Gènes fongiques</term><term>Hydrolyse</term><term>Immunohistochimie</term><term>Populus</term><term>Spécificité du substrat</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Endo-1,4-β-xylanase A (XynA) from Schizophyllum commune was cloned into pPCZαA and expressed in Pichia pastoris GS115. The open reading frame of the xynA gene is composed of 684 bp, encoding 278 amino acids with a molecular weight of 26 kDa. Based on sequence similarity, XynA belongs to the CAZy glycoside hydrolase family 11. The optimal activity of XynA was at pH 5 and 50 °C on beechwood xylan. Under these conditions, the K(m), V(max) and specific activity of XynA were 5768 units mg(-1), 4 mg ml(-1) and 9000 μmol min(-1)mg(-1), respectively. XynA activity was enhanced in the presence of cations, such as K(+), Na(+), Li(2+), Cd(2+), and Co(2+). However, in the presence of EDTA, Hg(2+) and Fe(3+), xylanase activity was significantly inhibited. This enzyme effectively degraded approximately 45% of unsubstituted xylans in the cell wall from poplar stems. The high level of XynA activity might increase the yield of enzyme hydrolysis from biomass. Thus, XynA could be used as a major component of a lignocellulosic degrading enzyme cocktail.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23410928</PMID><DateCompleted><Year>2013</Year><Month>08</Month><Day>14</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0909</ISSN><JournalIssue CitedMedium="Internet"><Volume>52</Volume><Issue>3</Issue><PubDate><Year>2013</Year><Month>Mar</Month><Day>05</Day></PubDate></JournalIssue><Title>Enzyme and microbial technology</Title><ISOAbbreviation>Enzyme Microb Technol</ISOAbbreviation></Journal><ArticleTitle>Heterologous expression of endo-1,4-β-xylanase A from Schizophyllum commune in Pichia pastoris and functional characterization of the recombinant enzyme.</ArticleTitle><Pagination><MedlinePgn>170-6</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.enzmictec.2012.12.012</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0141-0229(13)00005-7</ELocationID><Abstract><AbstractText>Endo-1,4-β-xylanase A (XynA) from Schizophyllum commune was cloned into pPCZαA and expressed in Pichia pastoris GS115. The open reading frame of the xynA gene is composed of 684 bp, encoding 278 amino acids with a molecular weight of 26 kDa. Based on sequence similarity, XynA belongs to the CAZy glycoside hydrolase family 11. The optimal activity of XynA was at pH 5 and 50 °C on beechwood xylan. Under these conditions, the K(m), V(max) and specific activity of XynA were 5768 units mg(-1), 4 mg ml(-1) and 9000 μmol min(-1)mg(-1), respectively. XynA activity was enhanced in the presence of cations, such as K(+), Na(+), Li(2+), Cd(2+), and Co(2+). However, in the presence of EDTA, Hg(2+) and Fe(3+), xylanase activity was significantly inhibited. This enzyme effectively degraded approximately 45% of unsubstituted xylans in the cell wall from poplar stems. The high level of XynA activity might increase the yield of enzyme hydrolysis from biomass. Thus, XynA could be used as a major component of a lignocellulosic degrading enzyme cocktail.</AbstractText><CopyrightInformation>Copyright © 2013 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Song</LastName><ForeName>Younho</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Bioenergy Science and Technology, Chonnam National University, Gwangju 500-757, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Yoon Gyo</ForeName><Initials>YG</Initials></Author><Author ValidYN="Y"><LastName>Choi</LastName><ForeName>In Seong</ForeName><Initials>IS</Initials></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Kwang Ho</ForeName><Initials>KH</Initials></Author><Author ValidYN="Y"><LastName>Cho</LastName><ForeName>Eun Jin</ForeName><Initials>EJ</Initials></Author><Author ValidYN="Y"><LastName>Bae</LastName><ForeName>Hyeun-Jong</ForeName><Initials>HJ</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><ArticleDate DateType="Electronic"><Year>2013</Year><Month>01</Month><Day>07</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Enzyme Microb Technol</MedlineTA><NlmUniqueID>8003761</NlmUniqueID><ISSNLinking>0141-0229</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002412">Cations</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002614">Chelating Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018076">DNA, Complementary</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014990">Xylans</NameOfSubstance></Chemical><Chemical><RegistryNumber>9G34HU7RV0</RegistryNumber><NameOfSubstance UI="D004492">Edetic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.8</RegistryNumber><NameOfSubstance UI="D043364">Endo-1,4-beta Xylanases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002412" MajorTopicYN="N">Cations</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002614" MajorTopicYN="N">Chelating Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018076" MajorTopicYN="N">DNA, Complementary</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004492" MajorTopicYN="N">Edetic Acid</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D043364" MajorTopicYN="N">Endo-1,4-beta Xylanases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029964" MajorTopicYN="N">Fagus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005800" MajorTopicYN="N">Genes, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006868" MajorTopicYN="N">Hydrolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007150" MajorTopicYN="N">Immunohistochemistry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016366" MajorTopicYN="N">Open Reading Frames</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010843" MajorTopicYN="N">Pichia</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012567" MajorTopicYN="N">Schizophyllum</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017422" MajorTopicYN="N">Sequence Analysis, DNA</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014934" MajorTopicYN="N">Wood</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014990" MajorTopicYN="N">Xylans</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>09</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2012</Year><Month>12</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2012</Year><Month>12</Month><Day>31</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>2</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>2</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>8</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23410928</ArticleId><ArticleId IdType="pii">S0141-0229(13)00005-7</ArticleId><ArticleId IdType="doi">10.1016/j.enzmictec.2012.12.012</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Corée du Sud</li></country></list><tree><noCountry><name sortKey="Bae, Hyeun Jong" sort="Bae, Hyeun Jong" uniqKey="Bae H" first="Hyeun-Jong" last="Bae">Hyeun-Jong Bae</name><name sortKey="Cho, Eun Jin" sort="Cho, Eun Jin" uniqKey="Cho E" first="Eun Jin" last="Cho">Eun Jin Cho</name><name sortKey="Choi, In Seong" sort="Choi, In Seong" uniqKey="Choi I" first="In Seong" last="Choi">In Seong Choi</name><name sortKey="Lee, Kwang Ho" sort="Lee, Kwang Ho" uniqKey="Lee K" first="Kwang Ho" last="Lee">Kwang Ho Lee</name><name sortKey="Lee, Yoon Gyo" sort="Lee, Yoon Gyo" uniqKey="Lee Y" first="Yoon Gyo" last="Lee">Yoon Gyo Lee</name></noCountry><country name="Corée du Sud"><noRegion><name sortKey="Song, Younho" sort="Song, Younho" uniqKey="Song Y" first="Younho" last="Song">Younho Song</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document 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|texte= Heterologous expression of endo-1,4-β-xylanase A from Schizophyllum commune in Pichia pastoris and functional characterization of the recombinant enzyme.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:23410928" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a PoplarV1
| This area was generated with Dilib version V0.6.37. |  |