Cloning and characterization of a thermostable endo-arabinanase from Phanerochaete chrysosporium and its synergistic action with endo-xylanase.
Identifieur interne : 000384 ( Main/Exploration ); précédent : 000383; suivant : 000385Cloning and characterization of a thermostable endo-arabinanase from Phanerochaete chrysosporium and its synergistic action with endo-xylanase.
Auteurs : Nguyen Duc Huy [Corée du Sud] ; Saravanakumar Thiyagarajan ; Yoon-E Choi ; Dae-Hyuk Kim ; Seung-Moon ParkSource :
- Bioprocess and biosystems engineering [ 1615-7605 ] ; 2013.
Descripteurs français
- KwdFr :
- Clonage moléculaire (MeSH), Endo-1,4-beta xylanases (biosynthèse), Endo-1,4-beta xylanases (composition chimique), Endo-1,4-beta xylanases (génétique), Phanerochaete (enzymologie), Phanerochaete (génétique), Pichia (enzymologie), Pichia (génétique), Polyosides (composition chimique), Protéines fongiques (biosynthèse), Protéines fongiques (composition chimique), Protéines fongiques (génétique), Protéines recombinantes (biosynthèse), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique), Stabilité enzymatique (MeSH), Température élevée (MeSH).
- MESH :
- biosynthèse : Endo-1,4-beta xylanases, Protéines fongiques, Protéines recombinantes.
- composition chimique : Endo-1,4-beta xylanases, Polyosides, Protéines fongiques, Protéines recombinantes.
- enzymologie : Phanerochaete, Pichia.
- génétique : Endo-1,4-beta xylanases, Phanerochaete, Pichia, Protéines fongiques, Protéines recombinantes.
- Clonage moléculaire, Stabilité enzymatique, Température élevée.
English descriptors
- KwdEn :
- Cloning, Molecular (MeSH), Endo-1,4-beta Xylanases (biosynthesis), Endo-1,4-beta Xylanases (chemistry), Endo-1,4-beta Xylanases (genetics), Enzyme Stability (MeSH), Fungal Proteins (biosynthesis), Fungal Proteins (chemistry), Fungal Proteins (genetics), Hot Temperature (MeSH), Phanerochaete (enzymology), Phanerochaete (genetics), Pichia (enzymology), Pichia (genetics), Polysaccharides (chemistry), Recombinant Proteins (biosynthesis), Recombinant Proteins (chemistry), Recombinant Proteins (genetics).
- MESH :
- chemical , biosynthesis : Endo-1,4-beta Xylanases, Fungal Proteins, Recombinant Proteins.
- chemical , chemistry : Endo-1,4-beta Xylanases, Fungal Proteins, Polysaccharides, Recombinant Proteins.
- chemical , genetics : Endo-1,4-beta Xylanases, Fungal Proteins, Recombinant Proteins.
- enzymology : Phanerochaete, Pichia.
- genetics : Phanerochaete, Pichia.
- Cloning, Molecular, Enzyme Stability, Hot Temperature.
Abstract
Putative arabinanase (PcARA) was cloned from cDNA of Phanerochaete chrysosporium. The gene sequencing indicated that PcARA consisted of 939 nucleotides that encodes for 312 amino acid arabinanase-polypeptide chain, including a signal peptide of 19 amino acids. Three-dimensional homology indicated that this enzyme is a five-bladed β-propeller, belonging to glycosidase family 43 and its secondary structure is consisted of 24 β-sheets. The PcARA-cDNA was expressed in Pichia pastoris using pPICZαC. SDS-PAGE of purified arabinanase showed a single band of 33 kDa that is very close to theoretical molecular mass of 33.9 kDa calculated by its amino acid content. Recombinant arabinanase (rPcARA) exhibited maximum activity at pH and temperature of 5.0 and 60 °C, respectively. End-product analysis of debranched arabinan hydrolysis by thin-layer chromatography indicated that rPcARA acted as endo-type. The synergistic action of rPcARA with recombinant xylanase resulted in 72 and 9.3 % release of total soluble sugar of arabinoxylan and NaOH-pretreated barley straw, respectively.
DOI: 10.1007/s00449-013-0891-9
PubMed: 23361183
Affiliations:
Links toward previous steps (curation, corpus...)
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first="Saravanakumar" last="Thiyagarajan">Saravanakumar Thiyagarajan</name></author><author><name sortKey="Choi, Yoon E" sort="Choi, Yoon E" uniqKey="Choi Y" first="Yoon-E" last="Choi">Yoon-E Choi</name></author><author><name sortKey="Kim, Dae Hyuk" sort="Kim, Dae Hyuk" uniqKey="Kim D" first="Dae-Hyuk" last="Kim">Dae-Hyuk Kim</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">Bioprocess and biosystems engineering</title><idno type="eISSN">1615-7605</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cloning, Molecular (MeSH)</term><term>Endo-1,4-beta Xylanases (biosynthesis)</term><term>Endo-1,4-beta Xylanases (chemistry)</term><term>Endo-1,4-beta Xylanases (genetics)</term><term>Enzyme Stability (MeSH)</term><term>Fungal Proteins (biosynthesis)</term><term>Fungal Proteins (chemistry)</term><term>Fungal Proteins (genetics)</term><term>Hot Temperature (MeSH)</term><term>Phanerochaete (enzymology)</term><term>Phanerochaete (genetics)</term><term>Pichia (enzymology)</term><term>Pichia (genetics)</term><term>Polysaccharides (chemistry)</term><term>Recombinant Proteins (biosynthesis)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Clonage moléculaire (MeSH)</term><term>Endo-1,4-beta xylanases (biosynthèse)</term><term>Endo-1,4-beta xylanases (composition chimique)</term><term>Endo-1,4-beta xylanases (génétique)</term><term>Phanerochaete (enzymologie)</term><term>Phanerochaete (génétique)</term><term>Pichia (enzymologie)</term><term>Pichia (génétique)</term><term>Polyosides (composition chimique)</term><term>Protéines fongiques (biosynthèse)</term><term>Protéines fongiques (composition chimique)</term><term>Protéines fongiques (génétique)</term><term>Protéines recombinantes (biosynthèse)</term><term>Protéines recombinantes (composition chimique)</term><term>Protéines recombinantes (génétique)</term><term>Stabilité enzymatique (MeSH)</term><term>Température élevée (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Endo-1,4-beta Xylanases</term><term>Fungal Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Endo-1,4-beta Xylanases</term><term>Fungal Proteins</term><term>Polysaccharides</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Endo-1,4-beta Xylanases</term><term>Fungal Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Endo-1,4-beta xylanases</term><term>Protéines fongiques</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Endo-1,4-beta xylanases</term><term>Polyosides</term><term>Protéines fongiques</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phanerochaete</term><term>Pichia</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term><term>Pichia</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>Endo-1,4-beta xylanases</term><term>Phanerochaete</term><term>Pichia</term><term>Protéines fongiques</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cloning, Molecular</term><term>Enzyme Stability</term><term>Hot Temperature</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Clonage moléculaire</term><term>Stabilité enzymatique</term><term>Température élevée</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Putative arabinanase (PcARA) was cloned from cDNA of Phanerochaete chrysosporium. The gene sequencing indicated that PcARA consisted of 939 nucleotides that encodes for 312 amino acid arabinanase-polypeptide chain, including a signal peptide of 19 amino acids. Three-dimensional homology indicated that this enzyme is a five-bladed β-propeller, belonging to glycosidase family 43 and its secondary structure is consisted of 24 β-sheets. The PcARA-cDNA was expressed in Pichia pastoris using pPICZαC. SDS-PAGE of purified arabinanase showed a single band of 33 kDa that is very close to theoretical molecular mass of 33.9 kDa calculated by its amino acid content. Recombinant arabinanase (rPcARA) exhibited maximum activity at pH and temperature of 5.0 and 60 °C, respectively. End-product analysis of debranched arabinan hydrolysis by thin-layer chromatography indicated that rPcARA acted as endo-type. The synergistic action of rPcARA with recombinant xylanase resulted in 72 and 9.3 % release of total soluble sugar of arabinoxylan and NaOH-pretreated barley straw, respectively.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23361183</PMID><DateCompleted><Year>2013</Year><Month>12</Month><Day>09</Day></DateCompleted><DateRevised><Year>2013</Year><Month>05</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1615-7605</ISSN><JournalIssue CitedMedium="Internet"><Volume>36</Volume><Issue>6</Issue><PubDate><Year>2013</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Bioprocess and biosystems engineering</Title><ISOAbbreviation>Bioprocess Biosyst Eng</ISOAbbreviation></Journal><ArticleTitle>Cloning and characterization of a thermostable endo-arabinanase from Phanerochaete chrysosporium and its synergistic action with endo-xylanase.</ArticleTitle><Pagination><MedlinePgn>677-85</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00449-013-0891-9</ELocationID><Abstract><AbstractText>Putative arabinanase (PcARA) was cloned from cDNA of Phanerochaete chrysosporium. The gene sequencing indicated that PcARA consisted of 939 nucleotides that encodes for 312 amino acid arabinanase-polypeptide chain, including a signal peptide of 19 amino acids. Three-dimensional homology indicated that this enzyme is a five-bladed β-propeller, belonging to glycosidase family 43 and its secondary structure is consisted of 24 β-sheets. The PcARA-cDNA was expressed in Pichia pastoris using pPICZαC. SDS-PAGE of purified arabinanase showed a single band of 33 kDa that is very close to theoretical molecular mass of 33.9 kDa calculated by its amino acid content. Recombinant arabinanase (rPcARA) exhibited maximum activity at pH and temperature of 5.0 and 60 °C, respectively. End-product analysis of debranched arabinan hydrolysis by thin-layer chromatography indicated that rPcARA acted as endo-type. The synergistic action of rPcARA with recombinant xylanase resulted in 72 and 9.3 % release of total soluble sugar of arabinoxylan and NaOH-pretreated barley straw, respectively.</AbstractText></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, Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Thiyagarajan</LastName><ForeName>Saravanakumar</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Choi</LastName><ForeName>Yoon-E</ForeName><Initials>YE</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>30</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Bioprocess Biosyst Eng</MedlineTA><NlmUniqueID>101088505</NlmUniqueID><ISSNLinking>1615-7591</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011134">Polysaccharides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>11078-27-6</RegistryNumber><NameOfSubstance UI="C030080">araban</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="D003001" MajorTopicYN="Y">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D043364" MajorTopicYN="Y">Endo-1,4-beta Xylanases</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="Y">Fungal Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006358" MajorTopicYN="Y">Hot Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="Y">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010843" MajorTopicYN="N">Pichia</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011134" MajorTopicYN="N">Polysaccharides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>12</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>01</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>1</Month><Day>31</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>1</Month><Day>31</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>12</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23361183</ArticleId><ArticleId IdType="doi">10.1007/s00449-013-0891-9</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Corée du Sud</li></country></list><tree><noCountry><name sortKey="Choi, Yoon E" sort="Choi, Yoon E" uniqKey="Choi Y" first="Yoon-E" last="Choi">Yoon-E Choi</name><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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