Characterization of a novel manganese dependent endoglucanase belongs in GH family 5 from Phanerochaete chrysosporium.
Identifieur interne : 000224 ( Main/Exploration ); précédent : 000223; suivant : 000225Characterization of a novel manganese dependent endoglucanase belongs in GH family 5 from Phanerochaete chrysosporium.
Auteurs : Nguyen Duc Huy [Viêt Nam] ; Cu Le Nguyen [Corée du Sud] ; Han-Sung Park [Corée du Sud] ; Nguyen Hoang Loc [Viêt Nam] ; Myoung-Suk Choi [Corée du Sud] ; Dae-Hyuk Kim [Corée du Sud] ; Jeong-Woo Seo [Corée du Sud] ; Seung-Moon Park [Corée du Sud]Source :
- Journal of bioscience and bioengineering [ 1347-4421 ] ; 2016.
Descripteurs français
- KwdFr :
- ADN complémentaire (génétique), Biomasse (MeSH), Cellulase (classification), Cellulase (composition chimique), Cellulase (génétique), Cellulase (métabolisme), Concentration en ions d'hydrogène (MeSH), Domaine catalytique (MeSH), Glucose (métabolisme), Manganèse (métabolisme), Masse moléculaire (MeSH), Phanerochaete (enzymologie), Phanerochaete (génétique), Pichia (génétique), Protéines recombinantes (biosynthèse), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Stabilité enzymatique (MeSH), Température (MeSH), bêta-Glucosidase (métabolisme), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
- biosynthèse : Protéines recombinantes.
- classification : Cellulase.
- composition chimique : Cellulase.
- enzymologie : Phanerochaete.
- génétique : ADN complémentaire, Cellulase, Phanerochaete, Pichia, Protéines recombinantes.
- métabolisme : Cellulase, Glucose, Manganèse, Protéines recombinantes, bêta-Glucosidase.
- Biomasse, Concentration en ions d'hydrogène, Domaine catalytique, Masse moléculaire, Stabilité enzymatique, Température, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Biomass (MeSH), Catalytic Domain (MeSH), Cellulase (chemistry), Cellulase (classification), Cellulase (genetics), Cellulase (metabolism), DNA, Complementary (genetics), Electrophoresis, Polyacrylamide Gel (MeSH), Enzyme Stability (MeSH), Glucose (metabolism), Hydrogen-Ion Concentration (MeSH), Manganese (metabolism), Molecular Weight (MeSH), Phanerochaete (enzymology), Phanerochaete (genetics), Pichia (genetics), Recombinant Proteins (biosynthesis), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Temperature (MeSH), beta-Glucosidase (metabolism).
- MESH :
- chemical , biosynthesis : Recombinant Proteins.
- chemical , chemistry : Cellulase.
- chemical , classification : Cellulase.
- chemical , genetics : Cellulase, DNA, Complementary, Recombinant Proteins.
- chemical , metabolism : Cellulase, Glucose, Manganese, Recombinant Proteins, beta-Glucosidase.
- enzymology : Phanerochaete.
- genetics : Phanerochaete, Pichia.
- Biomass, Catalytic Domain, Electrophoresis, Polyacrylamide Gel, Enzyme Stability, Hydrogen-Ion Concentration, Molecular Weight, Temperature.
Abstract
The cDNA encoding a putative glycoside hydrolase family 5, which has been predicted to be an endoglucanase (PcEg5A), was cloned from Phanerochaete chrysosporium and expressed in Pichia pastoris. PcEg5A contains a carbohydrate-binding domain and two important amino acids, E209 and E319, playing as proton donor and nucleophile in substrate catalytic domain. SDS-PAGE analysis indicated that the recombinant endoglucanase 5A (rPcEg5A) has a molecular size of 43 kDa which corresponds with the theoretical calculation. Optimum pH and temperature were found to be 4.5-6.0, and 50°C-60°C, respectively. Moreover, rPcEg5A exhibited maximal activity in the pH range of 3.0-8.0, whereas over 50% of activity still remained at 20°C and 80°C. rPcEg5A was stable at 60°C for 12 h incubation, indicating that rPcEg5A is a thermostable enzyme. Manganese ion enhanced the enzyme activity by 77%, indicating that rPcEg5A is a metal dependent enzyme. The addition of rPcEg5A to cellobiase (cellobiohydrolase and β-glucosidase) resulted in a 53% increasing saccharification of NaOH-pretreated barley straw, whereas the glucose release was 47% higher than that cellobiase treatment alone. Our study suggested that rPcEg5A is an enzyme with great potential for biomass saccharification.
DOI: 10.1016/j.jbiosc.2015.06.009
PubMed: 26173955
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biomass (MeSH)</term>
<term>Catalytic Domain (MeSH)</term>
<term>Cellulase (chemistry)</term>
<term>Cellulase (classification)</term>
<term>Cellulase (genetics)</term>
<term>Cellulase (metabolism)</term>
<term>DNA, Complementary (genetics)</term>
<term>Electrophoresis, Polyacrylamide Gel (MeSH)</term>
<term>Enzyme Stability (MeSH)</term>
<term>Glucose (metabolism)</term>
<term>Hydrogen-Ion Concentration (MeSH)</term>
<term>Manganese (metabolism)</term>
<term>Molecular Weight (MeSH)</term>
<term>Phanerochaete (enzymology)</term>
<term>Phanerochaete (genetics)</term>
<term>Pichia (genetics)</term>
<term>Recombinant Proteins (biosynthesis)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>Temperature (MeSH)</term>
<term>beta-Glucosidase (metabolism)</term>
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<term>Biomasse (MeSH)</term>
<term>Cellulase (classification)</term>
<term>Cellulase (composition chimique)</term>
<term>Cellulase (génétique)</term>
<term>Cellulase (métabolisme)</term>
<term>Concentration en ions d'hydrogène (MeSH)</term>
<term>Domaine catalytique (MeSH)</term>
<term>Glucose (métabolisme)</term>
<term>Manganèse (métabolisme)</term>
<term>Masse moléculaire (MeSH)</term>
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<term>Phanerochaete (génétique)</term>
<term>Pichia (génétique)</term>
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<term>Protéines recombinantes (génétique)</term>
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<term>bêta-Glucosidase (métabolisme)</term>
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<term>beta-Glucosidase</term>
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<term>Temperature</term>
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<term>Concentration en ions d'hydrogène</term>
<term>Domaine catalytique</term>
<term>Masse moléculaire</term>
<term>Stabilité enzymatique</term>
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<front><div type="abstract" xml:lang="en">The cDNA encoding a putative glycoside hydrolase family 5, which has been predicted to be an endoglucanase (PcEg5A), was cloned from Phanerochaete chrysosporium and expressed in Pichia pastoris. PcEg5A contains a carbohydrate-binding domain and two important amino acids, E209 and E319, playing as proton donor and nucleophile in substrate catalytic domain. SDS-PAGE analysis indicated that the recombinant endoglucanase 5A (rPcEg5A) has a molecular size of 43 kDa which corresponds with the theoretical calculation. Optimum pH and temperature were found to be 4.5-6.0, and 50°C-60°C, respectively. Moreover, rPcEg5A exhibited maximal activity in the pH range of 3.0-8.0, whereas over 50% of activity still remained at 20°C and 80°C. rPcEg5A was stable at 60°C for 12 h incubation, indicating that rPcEg5A is a thermostable enzyme. Manganese ion enhanced the enzyme activity by 77%, indicating that rPcEg5A is a metal dependent enzyme. The addition of rPcEg5A to cellobiase (cellobiohydrolase and β-glucosidase) resulted in a 53% increasing saccharification of NaOH-pretreated barley straw, whereas the glucose release was 47% higher than that cellobiase treatment alone. Our study suggested that rPcEg5A is an enzyme with great potential for biomass saccharification. </div>
</front>
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<Month>09</Month>
<Day>01</Day>
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<Month>12</Month>
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<Title>Journal of bioscience and bioengineering</Title>
<ISOAbbreviation>J Biosci Bioeng</ISOAbbreviation>
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<ArticleTitle>Characterization of a novel manganese dependent endoglucanase belongs in GH family 5 from Phanerochaete chrysosporium.</ArticleTitle>
<Pagination><MedlinePgn>154-9</MedlinePgn>
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<Abstract><AbstractText>The cDNA encoding a putative glycoside hydrolase family 5, which has been predicted to be an endoglucanase (PcEg5A), was cloned from Phanerochaete chrysosporium and expressed in Pichia pastoris. PcEg5A contains a carbohydrate-binding domain and two important amino acids, E209 and E319, playing as proton donor and nucleophile in substrate catalytic domain. SDS-PAGE analysis indicated that the recombinant endoglucanase 5A (rPcEg5A) has a molecular size of 43 kDa which corresponds with the theoretical calculation. Optimum pH and temperature were found to be 4.5-6.0, and 50°C-60°C, respectively. Moreover, rPcEg5A exhibited maximal activity in the pH range of 3.0-8.0, whereas over 50% of activity still remained at 20°C and 80°C. rPcEg5A was stable at 60°C for 12 h incubation, indicating that rPcEg5A is a thermostable enzyme. Manganese ion enhanced the enzyme activity by 77%, indicating that rPcEg5A is a metal dependent enzyme. The addition of rPcEg5A to cellobiase (cellobiohydrolase and β-glucosidase) resulted in a 53% increasing saccharification of NaOH-pretreated barley straw, whereas the glucose release was 47% higher than that cellobiase treatment alone. Our study suggested that rPcEg5A is an enzyme with great potential for biomass saccharification. </AbstractText>
<CopyrightInformation>Copyright © 2015 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; Institute of Biotechnology, Hue University, Hue 530000, Viet Nam.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Nguyen</LastName>
<ForeName>Cu Le</ForeName>
<Initials>CL</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>Park</LastName>
<ForeName>Han-Sung</ForeName>
<Initials>HS</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>Loc</LastName>
<ForeName>Nguyen Hoang</ForeName>
<Initials>NH</Initials>
<AffiliationInfo><Affiliation>College of Sciences, Hue University, Hue 530000, Viet Nam.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Choi</LastName>
<ForeName>Myoung-Suk</ForeName>
<Initials>MS</Initials>
<AffiliationInfo><Affiliation>Institute of Molecular Biology and Genetics, College of Natural Sciences, Chonbuk National University, Jeonju, Jeonbuk 561-756, Republic of Korea.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kim</LastName>
<ForeName>Dae-Hyuk</ForeName>
<Initials>DH</Initials>
<AffiliationInfo><Affiliation>Institute of Molecular Biology and Genetics, College of Natural Sciences, Chonbuk National University, Jeonju, Jeonbuk 561-756, Republic of Korea.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Seo</LastName>
<ForeName>Jeong-Woo</ForeName>
<Initials>JW</Initials>
<AffiliationInfo><Affiliation>Applied Microbiology Research Center, Bio-Materials Research Institute, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Jeongeup, Jeonbuk 580-185, Republic of Korea.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Park</LastName>
<ForeName>Seung-Moon</ForeName>
<Initials>SM</Initials>
<AffiliationInfo><Affiliation>Division of Biotechnology, College of Environmental and Bioresource Sciences, Chonbuk National University, Iksan, Jeonbuk 570-752, Republic of Korea. Electronic address: smpark@chonbuk.ac.kr.</Affiliation>
</AffiliationInfo>
</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>2015</Year>
<Month>07</Month>
<Day>11</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="D018076">DNA, Complementary</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>42Z2K6ZL8P</RegistryNumber>
<NameOfSubstance UI="D008345">Manganese</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.2.1.21</RegistryNumber>
<NameOfSubstance UI="D001617">beta-Glucosidase</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.2.1.4</RegistryNumber>
<NameOfSubstance UI="D002480">Cellulase</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>IY9XDZ35W2</RegistryNumber>
<NameOfSubstance UI="D005947">Glucose</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D018533" MajorTopicYN="N">Biomass</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002480" MajorTopicYN="N">Cellulase</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000145" MajorTopicYN="Y">classification</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018076" MajorTopicYN="N">DNA, Complementary</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005947" MajorTopicYN="N">Glucose</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008345" MajorTopicYN="N">Manganese</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</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="Q000096" MajorTopicYN="N">biosynthesis</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001617" MajorTopicYN="N">beta-Glucosidase</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Barley straw</Keyword>
<Keyword MajorTopicYN="N">Endoglucanase</Keyword>
<Keyword MajorTopicYN="N">Manganese dependent enzyme</Keyword>
<Keyword MajorTopicYN="N">Phanerochaete chrysosporium</Keyword>
<Keyword MajorTopicYN="N">Saccharification</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year>
<Month>04</Month>
<Day>10</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2015</Year>
<Month>05</Month>
<Day>31</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2015</Year>
<Month>06</Month>
<Day>18</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2015</Year>
<Month>7</Month>
<Day>16</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2015</Year>
<Month>7</Month>
<Day>16</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2016</Year>
<Month>9</Month>
<Day>2</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">26173955</ArticleId>
<ArticleId IdType="pii">S1389-1723(15)00239-X</ArticleId>
<ArticleId IdType="doi">10.1016/j.jbiosc.2015.06.009</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>Corée du Sud</li>
<li>Viêt Nam</li>
</country>
</list>
<tree><country name="Viêt Nam"><noRegion><name sortKey="Huy, Nguyen Duc" sort="Huy, Nguyen Duc" uniqKey="Huy N" first="Nguyen Duc" last="Huy">Nguyen Duc Huy</name>
</noRegion>
<name sortKey="Loc, Nguyen Hoang" sort="Loc, Nguyen Hoang" uniqKey="Loc N" first="Nguyen Hoang" last="Loc">Nguyen Hoang Loc</name>
</country>
<country name="Corée du Sud"><noRegion><name sortKey="Nguyen, Cu Le" sort="Nguyen, Cu Le" uniqKey="Nguyen C" first="Cu Le" last="Nguyen">Cu Le Nguyen</name>
</noRegion>
<name sortKey="Choi, Myoung Suk" sort="Choi, Myoung Suk" uniqKey="Choi M" first="Myoung-Suk" last="Choi">Myoung-Suk 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, Han Sung" sort="Park, Han Sung" uniqKey="Park H" first="Han-Sung" last="Park">Han-Sung Park</name>
<name sortKey="Park, Seung Moon" sort="Park, Seung Moon" uniqKey="Park S" first="Seung-Moon" last="Park">Seung-Moon Park</name>
<name sortKey="Seo, Jeong Woo" sort="Seo, Jeong Woo" uniqKey="Seo J" first="Jeong-Woo" last="Seo">Jeong-Woo Seo</name>
</country>
</tree>
</affiliations>
</record>
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