Characterization of a recombinant bifunctional xylosidase/arabinofuranosidase from Phanerochaete chrysosporium.
Identifieur interne : 000387 ( Main/Exploration ); précédent : 000386; suivant : 000388Characterization of a recombinant bifunctional xylosidase/arabinofuranosidase from Phanerochaete chrysosporium.
Auteurs : Nguyen Duc Huy [Corée du Sud] ; Palvannan Thayumanavan ; Tae-Ho Kwon ; Seung-Moon ParkSource :
- Journal of bioscience and bioengineering [ 1347-4421 ] ; 2013.
Descripteurs français
- KwdFr :
- Arabinose (génétique), Clonage moléculaire (MeSH), Diholoside (métabolisme), Données de séquences moléculaires (MeSH), Glycosidases (composition chimique), Glycosidases (génétique), Glycosidases (métabolisme), Phanerochaete (enzymologie), Phanerochaete (génétique), Pichia (génétique), Protéines recombinantes (métabolisme), Séquence d'acides aminés (MeSH), Xylanes (métabolisme), Xylose (métabolisme), Xylosidases (composition chimique), Xylosidases (génétique), Xylosidases (métabolisme).
- MESH :
- composition chimique : Glycosidases, Xylosidases.
- enzymologie : Phanerochaete.
- génétique : Arabinose, Glycosidases, Phanerochaete, Pichia, Xylosidases.
- métabolisme : Diholoside, Glycosidases, Protéines recombinantes, Xylanes, Xylose, Xylosidases.
- Clonage moléculaire, Données de séquences moléculaires, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Arabinose (genetics), Cloning, Molecular (MeSH), Disaccharides (metabolism), Glycoside Hydrolases (chemistry), Glycoside Hydrolases (genetics), Glycoside Hydrolases (metabolism), Molecular Sequence Data (MeSH), Phanerochaete (enzymology), Phanerochaete (genetics), Pichia (genetics), Recombinant Proteins (metabolism), Xylans (metabolism), Xylose (metabolism), Xylosidases (chemistry), Xylosidases (genetics), Xylosidases (metabolism).
- MESH :
- chemical , chemistry : Glycoside Hydrolases, Xylosidases.
- chemical , genetics : Arabinose, Glycoside Hydrolases, Xylosidases.
- chemical , metabolism : Disaccharides, Glycoside Hydrolases, Recombinant Proteins, Xylans, Xylose, Xylosidases.
- enzymology : Phanerochaete.
- genetics : Phanerochaete, Pichia.
- Amino Acid Sequence, Cloning, Molecular, Molecular Sequence Data.
Abstract
A bifunctional xylosidase/arabinofuranosidase gene (PcXyl) was cloned from the cDNA library of Phanerochaete chrysosporium and further expressed in Pichia pastoris. Enzymatic assay indicated that P. pastoris produced rPcXyl at a level of 26,141 U l⁻¹. The xylosidase and arabinofuranosidase activities of rPcXyl were maximized, respectively, at pHs of 5.0 and 5.5 and temperatures of 45°C and 50°C. SDS-PAGE revealed a single band of purified rPcXyl of 83 kDa. Cu²⁺ and Zn²⁺ completely inhibited the enzyme activity of rPcXyl. The enzyme activity of rPcXyl was increased 151%, 126% and 123%, respectively, in the presence of glucose, xylose and arabinose at concentrations of 5 mM. rPcXyl hydrolyzed xylobiose to xylose and xylotriose to xylose and xylobiose, indicating rPcXyl acts as an exo-type enzyme. Additionally, rPcXyl enhanced xylose release from xylan substrates in synergy with rPcXynC.
DOI: 10.1016/j.jbiosc.2013.02.004
PubMed: 23474097
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Characterization of a recombinant bifunctional xylosidase/arabinofuranosidase from Phanerochaete chrysosporium.</title><author><name sortKey="Huy, Nguyen Duc" sort="Huy, Nguyen Duc" uniqKey="Huy N" first="Nguyen Duc" last="Huy">Nguyen Duc Huy</name><affiliation wicri:level="1"><nlm:affiliation>Division of Biotechnology, College of Environmental and Bioresource Sciences, Chonbuk National University, Iksan, Jeonbuk 570-752, Republic of Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>Division of Biotechnology, College of Environmental and Bioresource Sciences, Chonbuk National University, Iksan, Jeonbuk 570-752</wicri:regionArea><wicri:noRegion>Jeonbuk 570-752</wicri:noRegion></affiliation></author><author><name sortKey="Thayumanavan, Palvannan" sort="Thayumanavan, Palvannan" uniqKey="Thayumanavan P" first="Palvannan" last="Thayumanavan">Palvannan Thayumanavan</name></author><author><name sortKey="Kwon, Tae Ho" sort="Kwon, Tae Ho" uniqKey="Kwon T" first="Tae-Ho" last="Kwon">Tae-Ho Kwon</name></author><author><name sortKey="Park, Seung Moon" sort="Park, Seung Moon" uniqKey="Park S" first="Seung-Moon" last="Park">Seung-Moon Park</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23474097</idno><idno type="pmid">23474097</idno><idno type="doi">10.1016/j.jbiosc.2013.02.004</idno><idno type="wicri:Area/Main/Corpus">000375</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000375</idno><idno type="wicri:Area/Main/Curation">000375</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000375</idno><idno type="wicri:Area/Main/Exploration">000375</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Characterization of a recombinant bifunctional xylosidase/arabinofuranosidase from Phanerochaete chrysosporium.</title><author><name sortKey="Huy, Nguyen Duc" sort="Huy, Nguyen Duc" uniqKey="Huy N" first="Nguyen Duc" last="Huy">Nguyen Duc Huy</name><affiliation wicri:level="1"><nlm:affiliation>Division of Biotechnology, College of Environmental and Bioresource Sciences, Chonbuk National University, Iksan, Jeonbuk 570-752, Republic of Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>Division of Biotechnology, College of Environmental and Bioresource Sciences, Chonbuk National University, Iksan, Jeonbuk 570-752</wicri:regionArea><wicri:noRegion>Jeonbuk 570-752</wicri:noRegion></affiliation></author><author><name sortKey="Thayumanavan, Palvannan" sort="Thayumanavan, Palvannan" uniqKey="Thayumanavan P" first="Palvannan" last="Thayumanavan">Palvannan Thayumanavan</name></author><author><name sortKey="Kwon, Tae Ho" sort="Kwon, Tae Ho" uniqKey="Kwon T" first="Tae-Ho" last="Kwon">Tae-Ho Kwon</name></author><author><name sortKey="Park, Seung Moon" sort="Park, Seung Moon" uniqKey="Park S" first="Seung-Moon" last="Park">Seung-Moon Park</name></author></analytic><series><title level="j">Journal of bioscience and bioengineering</title><idno type="eISSN">1347-4421</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Arabinose (genetics)</term><term>Cloning, Molecular (MeSH)</term><term>Disaccharides (metabolism)</term><term>Glycoside Hydrolases (chemistry)</term><term>Glycoside Hydrolases (genetics)</term><term>Glycoside Hydrolases (metabolism)</term><term>Molecular Sequence Data (MeSH)</term><term>Phanerochaete (enzymology)</term><term>Phanerochaete (genetics)</term><term>Pichia (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Xylans (metabolism)</term><term>Xylose (metabolism)</term><term>Xylosidases (chemistry)</term><term>Xylosidases (genetics)</term><term>Xylosidases (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Arabinose (génétique)</term><term>Clonage moléculaire (MeSH)</term><term>Diholoside (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glycosidases (composition chimique)</term><term>Glycosidases (génétique)</term><term>Glycosidases (métabolisme)</term><term>Phanerochaete (enzymologie)</term><term>Phanerochaete (génétique)</term><term>Pichia (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Séquence d'acides aminés (MeSH)</term><term>Xylanes (métabolisme)</term><term>Xylose (métabolisme)</term><term>Xylosidases (composition chimique)</term><term>Xylosidases (génétique)</term><term>Xylosidases (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glycoside Hydrolases</term><term>Xylosidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Arabinose</term><term>Glycoside Hydrolases</term><term>Xylosidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Disaccharides</term><term>Glycoside Hydrolases</term><term>Recombinant Proteins</term><term>Xylans</term><term>Xylose</term><term>Xylosidases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glycosidases</term><term>Xylosidases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Phanerochaete</term><term>Pichia</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Arabinose</term><term>Glycosidases</term><term>Phanerochaete</term><term>Pichia</term><term>Xylosidases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Diholoside</term><term>Glycosidases</term><term>Protéines recombinantes</term><term>Xylanes</term><term>Xylose</term><term>Xylosidases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Cloning, Molecular</term><term>Molecular Sequence Data</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A bifunctional xylosidase/arabinofuranosidase gene (PcXyl) was cloned from the cDNA library of Phanerochaete chrysosporium and further expressed in Pichia pastoris. Enzymatic assay indicated that P. pastoris produced rPcXyl at a level of 26,141 U l⁻¹. The xylosidase and arabinofuranosidase activities of rPcXyl were maximized, respectively, at pHs of 5.0 and 5.5 and temperatures of 45°C and 50°C. SDS-PAGE revealed a single band of purified rPcXyl of 83 kDa. Cu²⁺ and Zn²⁺ completely inhibited the enzyme activity of rPcXyl. The enzyme activity of rPcXyl was increased 151%, 126% and 123%, respectively, in the presence of glucose, xylose and arabinose at concentrations of 5 mM. rPcXyl hydrolyzed xylobiose to xylose and xylotriose to xylose and xylobiose, indicating rPcXyl acts as an exo-type enzyme. Additionally, rPcXyl enhanced xylose release from xylan substrates in synergy with rPcXynC.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" IndexingMethod="Curated" Owner="NLM"><PMID Version="1">23474097</PMID><DateCompleted><Year>2014</Year><Month>02</Month><Day>19</Day></DateCompleted><DateRevised><Year>2019</Year><Month>03</Month><Day>18</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1347-4421</ISSN><JournalIssue CitedMedium="Internet"><Volume>116</Volume><Issue>2</Issue><PubDate><Year>2013</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Journal of bioscience and bioengineering</Title><ISOAbbreviation>J Biosci Bioeng</ISOAbbreviation></Journal><ArticleTitle>Characterization of a recombinant bifunctional xylosidase/arabinofuranosidase from Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>152-9</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jbiosc.2013.02.004</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S1389-1723(13)00044-3</ELocationID><Abstract><AbstractText>A bifunctional xylosidase/arabinofuranosidase gene (PcXyl) was cloned from the cDNA library of Phanerochaete chrysosporium and further expressed in Pichia pastoris. Enzymatic assay indicated that P. pastoris produced rPcXyl at a level of 26,141 U l⁻¹. The xylosidase and arabinofuranosidase activities of rPcXyl were maximized, respectively, at pHs of 5.0 and 5.5 and temperatures of 45°C and 50°C. SDS-PAGE revealed a single band of purified rPcXyl of 83 kDa. Cu²⁺ and Zn²⁺ completely inhibited the enzyme activity of rPcXyl. The enzyme activity of rPcXyl was increased 151%, 126% and 123%, respectively, in the presence of glucose, xylose and arabinose at concentrations of 5 mM. rPcXyl hydrolyzed xylobiose to xylose and xylotriose to xylose and xylobiose, indicating rPcXyl acts as an exo-type enzyme. Additionally, rPcXyl enhanced xylose release from xylan substrates in synergy with rPcXynC.</AbstractText><CopyrightInformation>Copyright © 2013 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Huy</LastName><ForeName>Nguyen Duc</ForeName><Initials>ND</Initials><AffiliationInfo><Affiliation>Division of Biotechnology, College of Environmental and Bioresource Sciences, Chonbuk National University, Iksan, Jeonbuk 570-752, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Thayumanavan</LastName><ForeName>Palvannan</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Kwon</LastName><ForeName>Tae-Ho</ForeName><Initials>TH</Initials></Author><Author ValidYN="Y"><LastName>Park</LastName><ForeName>Seung-Moon</ForeName><Initials>SM</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>03</Month><Day>07</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="D004187">Disaccharides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014990">Xylans</NameOfSubstance></Chemical><Chemical><RegistryNumber>A1TA934AKO</RegistryNumber><NameOfSubstance UI="D014994">Xylose</NameOfSubstance></Chemical><Chemical><RegistryNumber>B40ROO395Z</RegistryNumber><NameOfSubstance UI="D001089">Arabinose</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.-</RegistryNumber><NameOfSubstance UI="D006026">Glycoside Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.-</RegistryNumber><NameOfSubstance UI="D014995">Xylosidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.37</RegistryNumber><NameOfSubstance UI="C026579">exo-1,4-beta-D-xylosidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.55</RegistryNumber><NameOfSubstance UI="C019713">alpha-N-arabinofuranosidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>ID02R0EG7P</RegistryNumber><NameOfSubstance UI="C004173">xylobiose</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001089" MajorTopicYN="N">Arabinose</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004187" MajorTopicYN="N">Disaccharides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006026" MajorTopicYN="N">Glycoside Hydrolases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</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="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014990" MajorTopicYN="N">Xylans</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014994" MajorTopicYN="N">Xylose</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014995" MajorTopicYN="N">Xylosidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>11</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2013</Year><Month>01</Month><Day>31</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>02</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>3</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>3</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>2</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23474097</ArticleId><ArticleId IdType="pii">S1389-1723(13)00044-3</ArticleId><ArticleId IdType="doi">10.1016/j.jbiosc.2013.02.004</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Corée du Sud</li></country></list><tree><noCountry><name sortKey="Kwon, Tae Ho" sort="Kwon, Tae Ho" uniqKey="Kwon T" first="Tae-Ho" last="Kwon">Tae-Ho Kwon</name><name sortKey="Park, Seung Moon" sort="Park, Seung Moon" uniqKey="Park S" first="Seung-Moon" last="Park">Seung-Moon Park</name><name sortKey="Thayumanavan, Palvannan" sort="Thayumanavan, Palvannan" uniqKey="Thayumanavan P" first="Palvannan" last="Thayumanavan">Palvannan Thayumanavan</name></noCountry><country name="Corée du Sud"><noRegion><name sortKey="Huy, Nguyen Duc" sort="Huy, Nguyen Duc" uniqKey="Huy N" first="Nguyen Duc" last="Huy">Nguyen Duc Huy</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PhanerochaeteV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000387 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000387 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= PhanerochaeteV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:23474097
|texte= Characterization of a recombinant bifunctional xylosidase/arabinofuranosidase from Phanerochaete chrysosporium.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:23474097" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a PhanerochaeteV1
| This area was generated with Dilib version V0.6.37. |  |