A novel laccase from white rot fungus Trametes orientalis: Purification, characterization, and application.
Identifieur interne : 000631 ( Main/Exploration ); précédent : 000630; suivant : 000632A novel laccase from white rot fungus Trametes orientalis: Purification, characterization, and application.
Auteurs : Fei Zheng [République populaire de Chine] ; Qi An [République populaire de Chine] ; Ge Meng [République populaire de Chine] ; Xue-Jun Wu [République populaire de Chine] ; Yu-Cheng Dai [République populaire de Chine] ; Jing Si [République populaire de Chine] ; Bao-Kai Cui [République populaire de Chine]Source :
- International journal of biological macromolecules [ 1879-0003 ] ; 2017.
Descripteurs français
- KwdFr :
- Antienzymes (pharmacologie), Concentration en ions d'hydrogène (MeSH), Dépollution biologique de l'environnement (MeSH), Laccase (antagonistes et inhibiteurs), Laccase (composition chimique), Laccase (isolement et purification), Laccase (métabolisme), Masse moléculaire (MeSH), Métaux (pharmacologie), Polluants environnementaux (isolement et purification), Polluants environnementaux (métabolisme), Spécificité du substrat (MeSH), Stabilité enzymatique (MeSH), Séquence d'acides aminés (MeSH), Température (MeSH), Trametes (enzymologie).
- MESH :
- antagonistes et inhibiteurs : Laccase.
- composition chimique : Laccase.
- enzymologie : Trametes.
- isolement et purification : Laccase, Polluants environnementaux.
- métabolisme : Laccase, Polluants environnementaux.
- pharmacologie : Antienzymes, Métaux.
- Concentration en ions d'hydrogène, Dépollution biologique de l'environnement, Masse moléculaire, Spécificité du substrat, Stabilité enzymatique, Séquence d'acides aminés, Température.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Biodegradation, Environmental (MeSH), Environmental Pollutants (isolation & purification), Environmental Pollutants (metabolism), Enzyme Inhibitors (pharmacology), Enzyme Stability (MeSH), Hydrogen-Ion Concentration (MeSH), Laccase (antagonists & inhibitors), Laccase (chemistry), Laccase (isolation & purification), Laccase (metabolism), Metals (pharmacology), Molecular Weight (MeSH), Substrate Specificity (MeSH), Temperature (MeSH), Trametes (enzymology).
- MESH :
- chemical , antagonists & inhibitors : Laccase.
- chemical , chemistry : Laccase.
- chemical , isolation & purification : Environmental Pollutants, Laccase.
- chemical , metabolism : Environmental Pollutants, Laccase.
- chemical , pharmacology : Enzyme Inhibitors, Metals.
- enzymology : Trametes.
- Amino Acid Sequence, Biodegradation, Environmental, Enzyme Stability, Hydrogen-Ion Concentration, Molecular Weight, Substrate Specificity, Temperature.
Abstract
A novel laccase (Tolacc-T) from white rot fungus Trametes orientalis was enriched to apparent homogeneity with a specific activity of 20.667U/mg protein and recovery yield of 47.33%. The SDS-PAGE gave a single band indicating that Tolacc-T appears as a monomeric protein with a molecular mass of 44.0kDa. Domain structure analysis revealed that Tolacc-T contained a typical copper II binding domain and shared three potential N-glycosylation sites, but had no copper I binding domain, demonstrating that the enzyme is really a laccase, but a novel laccase. Optimal pH and temperature of Tolacc-T was 4.0 and 80°C, respectively, and it retained more than 80% of its original activity after 2h incubation at 10°C to 50°C. The enzyme exhibited strict substrate specificity towards ABTS but showed no or trace activities towards other substrates. Among the metals tested, Mn2+ was proved to be the best activator for enhancing the laccase activity. A strongly inhibiting effect was found when NaN3, L-cysteine, and DTT were added to the enzyme. However, Tolacc-T activity was little bit inhibited in the presence of chelator EDTA. Furthermore, the enzyme was capable of degrading structurally different synthetic dyes in the absence of a redox mediator.
DOI: 10.1016/j.ijbiomac.2017.04.089
PubMed: 28455255
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Electronic address: jingsi1788@126.com.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Institute of Microbiology, Beijing Forestry University, Beijing 100083</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author><author><name sortKey="Cui, Bao Kai" sort="Cui, Bao Kai" uniqKey="Cui B" first="Bao-Kai" last="Cui">Bao-Kai Cui</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Microbiology, Beijing Forestry University, Beijing 100083, China. Electronic address: cuibaokai@yahoo.com.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Institute of Microbiology, Beijing Forestry University, Beijing 100083</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author></analytic><series><title level="j">International journal of biological macromolecules</title><idno type="eISSN">1879-0003</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Biodegradation, Environmental (MeSH)</term><term>Environmental Pollutants (isolation & purification)</term><term>Environmental Pollutants (metabolism)</term><term>Enzyme Inhibitors (pharmacology)</term><term>Enzyme Stability (MeSH)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Laccase (antagonists & inhibitors)</term><term>Laccase (chemistry)</term><term>Laccase (isolation & purification)</term><term>Laccase (metabolism)</term><term>Metals (pharmacology)</term><term>Molecular Weight (MeSH)</term><term>Substrate Specificity (MeSH)</term><term>Temperature (MeSH)</term><term>Trametes (enzymology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antienzymes (pharmacologie)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Dépollution biologique de l'environnement (MeSH)</term><term>Laccase (antagonistes et inhibiteurs)</term><term>Laccase (composition chimique)</term><term>Laccase (isolement et purification)</term><term>Laccase (métabolisme)</term><term>Masse moléculaire (MeSH)</term><term>Métaux (pharmacologie)</term><term>Polluants environnementaux (isolement et purification)</term><term>Polluants environnementaux (métabolisme)</term><term>Spécificité du substrat (MeSH)</term><term>Stabilité enzymatique (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Température (MeSH)</term><term>Trametes (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Laccase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Laccase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Environmental Pollutants</term><term>Laccase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Environmental Pollutants</term><term>Laccase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Enzyme Inhibitors</term><term>Metals</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Laccase</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Laccase</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Trametes</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Trametes</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Laccase</term><term>Polluants environnementaux</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Laccase</term><term>Polluants environnementaux</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antienzymes</term><term>Métaux</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Biodegradation, Environmental</term><term>Enzyme Stability</term><term>Hydrogen-Ion Concentration</term><term>Molecular Weight</term><term>Substrate Specificity</term><term>Temperature</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Concentration en ions d'hydrogène</term><term>Dépollution biologique de l'environnement</term><term>Masse moléculaire</term><term>Spécificité du substrat</term><term>Stabilité enzymatique</term><term>Séquence d'acides aminés</term><term>Température</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A novel laccase (Tolacc-T) from white rot fungus Trametes orientalis was enriched to apparent homogeneity with a specific activity of 20.667U/mg protein and recovery yield of 47.33%. The SDS-PAGE gave a single band indicating that Tolacc-T appears as a monomeric protein with a molecular mass of 44.0kDa. Domain structure analysis revealed that Tolacc-T contained a typical copper II binding domain and shared three potential N-glycosylation sites, but had no copper I binding domain, demonstrating that the enzyme is really a laccase, but a novel laccase. Optimal pH and temperature of Tolacc-T was 4.0 and 80°C, respectively, and it retained more than 80% of its original activity after 2h incubation at 10°C to 50°C. The enzyme exhibited strict substrate specificity towards ABTS but showed no or trace activities towards other substrates. Among the metals tested, Mn<sup>2+</sup> was proved to be the best activator for enhancing the laccase activity. A strongly inhibiting effect was found when NaN<sub>3</sub>, <sub>L</sub>-cysteine, and DTT were added to the enzyme. However, Tolacc-T activity was little bit inhibited in the presence of chelator EDTA. Furthermore, the enzyme was capable of degrading structurally different synthetic dyes in the absence of a redox mediator.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28455255</PMID><DateCompleted><Year>2018</Year><Month>03</Month><Day>12</Day></DateCompleted><DateRevised><Year>2018</Year><Month>03</Month><Day>12</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0003</ISSN><JournalIssue CitedMedium="Internet"><Volume>102</Volume><PubDate><Year>2017</Year><Month>Sep</Month></PubDate></JournalIssue><Title>International journal of biological macromolecules</Title><ISOAbbreviation>Int J Biol Macromol</ISOAbbreviation></Journal><ArticleTitle>A novel laccase from white rot fungus Trametes orientalis: Purification, characterization, and application.</ArticleTitle><Pagination><MedlinePgn>758-770</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0141-8130(16)31601-4</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ijbiomac.2017.04.089</ELocationID><Abstract><AbstractText>A novel laccase (Tolacc-T) from white rot fungus Trametes orientalis was enriched to apparent homogeneity with a specific activity of 20.667U/mg protein and recovery yield of 47.33%. The SDS-PAGE gave a single band indicating that Tolacc-T appears as a monomeric protein with a molecular mass of 44.0kDa. Domain structure analysis revealed that Tolacc-T contained a typical copper II binding domain and shared three potential N-glycosylation sites, but had no copper I binding domain, demonstrating that the enzyme is really a laccase, but a novel laccase. Optimal pH and temperature of Tolacc-T was 4.0 and 80°C, respectively, and it retained more than 80% of its original activity after 2h incubation at 10°C to 50°C. The enzyme exhibited strict substrate specificity towards ABTS but showed no or trace activities towards other substrates. Among the metals tested, Mn<sup>2+</sup> was proved to be the best activator for enhancing the laccase activity. A strongly inhibiting effect was found when NaN<sub>3</sub>, <sub>L</sub>-cysteine, and DTT were added to the enzyme. However, Tolacc-T activity was little bit inhibited in the presence of chelator EDTA. Furthermore, the enzyme was capable of degrading structurally different synthetic dyes in the absence of a redox mediator.</AbstractText><CopyrightInformation>Copyright © 2017 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zheng</LastName><ForeName>Fei</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Institute of Microbiology, Beijing Forestry University, Beijing 100083, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>An</LastName><ForeName>Qi</ForeName><Initials>Q</Initials><AffiliationInfo><Affiliation>Institute of Microbiology, Beijing Forestry University, Beijing 100083, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Meng</LastName><ForeName>Ge</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Institute of Microbiology, Beijing Forestry University, Beijing 100083, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>Xue-Jun</ForeName><Initials>XJ</Initials><AffiliationInfo><Affiliation>Institute of Microbiology, Beijing Forestry University, Beijing 100083, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dai</LastName><ForeName>Yu-Cheng</ForeName><Initials>YC</Initials><AffiliationInfo><Affiliation>Institute of Microbiology, Beijing Forestry University, Beijing 100083, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Si</LastName><ForeName>Jing</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Institute of Microbiology, Beijing Forestry University, Beijing 100083, China. Electronic address: jingsi1788@126.com.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cui</LastName><ForeName>Bao-Kai</ForeName><Initials>BK</Initials><AffiliationInfo><Affiliation>Institute of Microbiology, Beijing Forestry University, Beijing 100083, China. Electronic address: cuibaokai@yahoo.com.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>04</Month><Day>26</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Int J Biol Macromol</MedlineTA><NlmUniqueID>7909578</NlmUniqueID><ISSNLinking>0141-8130</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004785">Environmental Pollutants</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008670">Metals</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.10.3.2</RegistryNumber><NameOfSubstance UI="D042845">Laccase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001673" MajorTopicYN="N">Biodegradation, Environmental</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004785" MajorTopicYN="N">Environmental Pollutants</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D042845" MajorTopicYN="N">Laccase</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008670" MajorTopicYN="N">Metals</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055454" MajorTopicYN="N">Trametes</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Characterization</Keyword><Keyword MajorTopicYN="N">Laccase</Keyword><Keyword MajorTopicYN="N">Purification</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>09</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2017</Year><Month>04</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2017</Year><Month>04</Month><Day>24</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>4</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2018</Year><Month>3</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>4</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">28455255</ArticleId><ArticleId IdType="pii">S0141-8130(16)31601-4</ArticleId><ArticleId IdType="doi">10.1016/j.ijbiomac.2017.04.089</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>République populaire de Chine</li></country><settlement><li>Pékin</li></settlement></list><tree><country name="République populaire de Chine"><noRegion><name sortKey="Zheng, Fei" sort="Zheng, Fei" uniqKey="Zheng F" first="Fei" last="Zheng">Fei Zheng</name></noRegion><name sortKey="An, Qi" sort="An, Qi" uniqKey="An Q" first="Qi" last="An">Qi An</name><name sortKey="Cui, Bao Kai" sort="Cui, Bao Kai" uniqKey="Cui B" first="Bao-Kai" last="Cui">Bao-Kai Cui</name><name sortKey="Dai, Yu Cheng" sort="Dai, Yu Cheng" uniqKey="Dai Y" first="Yu-Cheng" last="Dai">Yu-Cheng Dai</name><name sortKey="Meng, Ge" sort="Meng, Ge" uniqKey="Meng G" first="Ge" last="Meng">Ge Meng</name><name sortKey="Si, Jing" sort="Si, Jing" uniqKey="Si J" first="Jing" last="Si">Jing Si</name><name sortKey="Wu, Xue Jun" sort="Wu, Xue Jun" uniqKey="Wu X" first="Xue-Jun" last="Wu">Xue-Jun Wu</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|texte= A novel laccase from white rot fungus Trametes orientalis: Purification, characterization, and application.
}}
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HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:28455255" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a WhiteRotV1
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