Cloning and characterization of a novel bifunctional acetyl xylan esterase with carbohydrate binding module from Phanerochaete chrysosporium.
Identifieur interne : 000385 ( Main/Exploration ); précédent : 000384; suivant : 000386Cloning and characterization of a novel bifunctional acetyl xylan esterase with carbohydrate binding module from Phanerochaete chrysosporium.
Auteurs : Nguyen Duc Huy [Corée du Sud] ; Saravanakumar Thiyagarajan ; Dae-Hyuk Kim ; Seung-Moon ParkSource :
- Journal of bioscience and bioengineering [ 1347-4421 ] ; 2013.
Descripteurs français
- KwdFr :
- Acetylesterase (composition chimique), Acetylesterase (génétique), Acetylesterase (métabolisme), Acide peracétique (métabolisme), Alignement de séquences (MeSH), Cellulose (métabolisme), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Endo-1,4-beta xylanases (métabolisme), Phanerochaete (enzymologie), Pichia (génétique), Protéines recombinantes (composition chimique), Protéines recombinantes (métabolisme), Séquence d'acides aminés (MeSH), Température (MeSH), Xylanes (métabolisme).
- MESH :
- composition chimique : Acetylesterase, Protéines recombinantes.
- enzymologie : Phanerochaete.
- génétique : Acetylesterase, Pichia.
- métabolisme : Acetylesterase, Acide peracétique, Cellulose, Endo-1,4-beta xylanases, Protéines recombinantes, Xylanes.
- Alignement de séquences, Clonage moléculaire, Données de séquences moléculaires, Séquence d'acides aminés, Température.
English descriptors
- KwdEn :
- Acetylesterase (chemistry), Acetylesterase (genetics), Acetylesterase (metabolism), Amino Acid Sequence (MeSH), Cellulose (metabolism), Cloning, Molecular (MeSH), Endo-1,4-beta Xylanases (metabolism), Molecular Sequence Data (MeSH), Peracetic Acid (metabolism), Phanerochaete (enzymology), Pichia (genetics), Recombinant Proteins (chemistry), Recombinant Proteins (metabolism), Sequence Alignment (MeSH), Temperature (MeSH), Xylans (metabolism).
- MESH :
- chemical , chemistry : Acetylesterase, Recombinant Proteins.
- chemical , genetics : Acetylesterase.
- chemical , metabolism : Acetylesterase, Cellulose, Endo-1,4-beta Xylanases, Peracetic Acid, Recombinant Proteins, Xylans.
- enzymology : Phanerochaete.
- genetics : Pichia.
- Amino Acid Sequence, Cloning, Molecular, Molecular Sequence Data, Sequence Alignment, Temperature.
Abstract
The cDNA of acetyl xylan esterase 2 (PcAxe2) gene containing a carbohydrate binding module (CBM) sequence from Phanerochaete chrysosporium was cloned and expressed in Pichia pastoris. The recombinant PcAxe2 protein (rPcAxe2) was efficiently produced, reaching a maximum of 1058 U l(-1) after 6 days of cultivation. Molecular mass of the rPcAxe2 on SDS-PAGE was approximately 63 kDa under hyperglycosylation. Optimal activity of the purified rPcAxe2 enzyme was observed at pH and temperature of 7.0 and 30-35°C, respectively. In addition to acetyl xylan esterase activity, rPcAxe2 also exhibited a xylanase activity at an optimum pH and temperature of 5.0 and 80°C, respectively. The synergistic action of rPcAxe2 with rPcXynC on birchwood xylan, beechwood xylan and wheat arabinoxylan enhanced the total reducing soluble sugar.
DOI: 10.1016/j.jbiosc.2012.11.018
PubMed: 23287498
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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(enzymology)</term><term>Pichia (genetics)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (metabolism)</term><term>Sequence Alignment (MeSH)</term><term>Temperature (MeSH)</term><term>Xylans (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acetylesterase (composition chimique)</term><term>Acetylesterase (génétique)</term><term>Acetylesterase (métabolisme)</term><term>Acide peracétique (métabolisme)</term><term>Alignement de séquences (MeSH)</term><term>Cellulose (métabolisme)</term><term>Clonage moléculaire (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Endo-1,4-beta xylanases (métabolisme)</term><term>Phanerochaete (enzymologie)</term><term>Pichia (génétique)</term><term>Protéines recombinantes (composition chimique)</term><term>Protéines recombinantes (métabolisme)</term><term>Séquence d'acides aminés (MeSH)</term><term>Température (MeSH)</term><term>Xylanes (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Acetylesterase</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Acetylesterase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Acetylesterase</term><term>Cellulose</term><term>Endo-1,4-beta Xylanases</term><term>Peracetic Acid</term><term>Recombinant Proteins</term><term>Xylans</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Acetylesterase</term><term>Protéines recombinantes</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>Pichia</term></keywords><keywords scheme="MESH" qualifier="génétique" 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pastoris. The recombinant PcAxe2 protein (rPcAxe2) was efficiently produced, reaching a maximum of 1058 U l(-1) after 6 days of cultivation. Molecular mass of the rPcAxe2 on SDS-PAGE was approximately 63 kDa under hyperglycosylation. Optimal activity of the purified rPcAxe2 enzyme was observed at pH and temperature of 7.0 and 30-35°C, respectively. In addition to acetyl xylan esterase activity, rPcAxe2 also exhibited a xylanase activity at an optimum pH and temperature of 5.0 and 80°C, respectively. The synergistic action of rPcAxe2 with rPcXynC on birchwood xylan, beechwood xylan and wheat arabinoxylan enhanced the total reducing soluble sugar.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" IndexingMethod="Curated" Owner="NLM"><PMID Version="1">23287498</PMID><DateCompleted><Year>2014</Year><Month>01</Month><Day>22</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>115</Volume><Issue>5</Issue><PubDate><Year>2013</Year><Month>May</Month></PubDate></JournalIssue><Title>Journal of bioscience and bioengineering</Title><ISOAbbreviation>J Biosci Bioeng</ISOAbbreviation></Journal><ArticleTitle>Cloning and characterization of a novel bifunctional acetyl xylan esterase with carbohydrate binding module from Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>507-13</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jbiosc.2012.11.018</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S1389-1723(12)00469-0</ELocationID><Abstract><AbstractText>The cDNA of acetyl xylan esterase 2 (PcAxe2) gene containing a carbohydrate binding module (CBM) sequence from Phanerochaete chrysosporium was cloned and expressed in Pichia pastoris. The recombinant PcAxe2 protein (rPcAxe2) was efficiently produced, reaching a maximum of 1058 U l(-1) after 6 days of cultivation. Molecular mass of the rPcAxe2 on SDS-PAGE was approximately 63 kDa under hyperglycosylation. Optimal activity of the purified rPcAxe2 enzyme was observed at pH and temperature of 7.0 and 30-35°C, respectively. In addition to acetyl xylan esterase activity, rPcAxe2 also exhibited a xylanase activity at an optimum pH and temperature of 5.0 and 80°C, respectively. The synergistic action of rPcAxe2 with rPcXynC on birchwood xylan, beechwood xylan and wheat arabinoxylan enhanced the total reducing soluble sugar.</AbstractText><CopyrightInformation>Copyright © 2012 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, 194-5 Madong, Iksan, Jeonbuk 570-752, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Thiyagarajan</LastName><ForeName>Saravanakumar</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Dae-Hyuk</ForeName><Initials>DH</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>01</Month><Day>01</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>0</RegistryNumber><NameOfSubstance UI="D014990">Xylans</NameOfSubstance></Chemical><Chemical><RegistryNumber>9004-34-6</RegistryNumber><NameOfSubstance UI="D002482">Cellulose</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.1.6</RegistryNumber><NameOfSubstance UI="D000115">Acetylesterase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.1.72</RegistryNumber><NameOfSubstance UI="C081851">acetylxylan esterase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.8</RegistryNumber><NameOfSubstance UI="D043364">Endo-1,4-beta 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PubStatus="pubmed"><Year>2013</Year><Month>1</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>1</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23287498</ArticleId><ArticleId IdType="pii">S1389-1723(12)00469-0</ArticleId><ArticleId IdType="doi">10.1016/j.jbiosc.2012.11.018</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Corée du Sud</li></country></list><tree><noCountry><name sortKey="Kim, Dae Hyuk" sort="Kim, Dae Hyuk" uniqKey="Kim D" first="Dae-Hyuk" last="Kim">Dae-Hyuk Kim</name><name sortKey="Park, Seung Moon" sort="Park, Seung Moon" uniqKey="Park S" first="Seung-Moon" last="Park">Seung-Moon Park</name><name sortKey="Thiyagarajan, Saravanakumar" sort="Thiyagarajan, Saravanakumar" uniqKey="Thiyagarajan S" first="Saravanakumar" last="Thiyagarajan">Saravanakumar Thiyagarajan</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)
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