Direct determination of lignin peroxidase released from Phanerochaete chrysosporium by in-capillary enzyme assay using micellar electrokinetic chromatography.
Identifieur interne : 000218 ( Main/Exploration ); précédent : 000217; suivant : 000219Direct determination of lignin peroxidase released from Phanerochaete chrysosporium by in-capillary enzyme assay using micellar electrokinetic chromatography.
Auteurs : Airi Harada [Japon] ; Keiko Sasaki [Japon] ; Takashi Kaneta [Japon]Source :
- Journal of chromatography. A [ 1873-3778 ] ; 2016.
Descripteurs français
- KwdFr :
- Alcools benzyliques (métabolisme), Chromatographie (instrumentation), Dodécyl-sulfate de sodium (composition chimique), Dosages enzymatiques (instrumentation), Dosages enzymatiques (méthodes), Milieux de culture (composition chimique), Peroxidases (analyse), Peroxidases (métabolisme), Phanerochaete (enzymologie), Spectrophotométrie (MeSH), Substances tampon (MeSH).
- MESH :
- analyse : Peroxidases.
- composition chimique : Dodécyl-sulfate de sodium, Milieux de culture.
- enzymologie : Phanerochaete.
- métabolisme : Alcools benzyliques, Chromatographie, Dosages enzymatiques, Peroxidases.
- méthodes : Dosages enzymatiques.
- Spectrophotométrie, Substances tampon.
English descriptors
- KwdEn :
- Benzyl Alcohols (metabolism), Buffers (MeSH), Chromatography (instrumentation), Culture Media (chemistry), Enzyme Assays (instrumentation), Enzyme Assays (methods), Peroxidases (analysis), Peroxidases (metabolism), Phanerochaete (enzymology), Sodium Dodecyl Sulfate (chemistry), Spectrophotometry (MeSH).
- MESH :
- chemical , analysis : Peroxidases.
- chemical , chemistry : Culture Media, Sodium Dodecyl Sulfate.
- chemical , metabolism : Benzyl Alcohols, Peroxidases.
- chemical : Buffers.
- enzymology : Phanerochaete.
- instrumentation : Chromatography, Enzyme Assays.
- methods : Enzyme Assays.
- Spectrophotometry.
Abstract
Here we describe the application of an in-capillary enzyme assay using micellar electrokinetic chromatography (MEKC) in the determination of enzyme activity in a crude culture medium containing lignin peroxidase released from Phanerochaete chrysosporium (P. chrysosporium). The method consists of a plug-plug reaction between lignin peroxidase and its substrate, veratryl alcohol, the separation of the product, veratraldehyde, from the other components including the enzyme and the culture medium, and the determination of the enzyme activity from the peak area of veratraldehyde produced by the plug-plug reaction. This method is more sensitive than conventional spectrophotometry since the background originates from the enzyme and the culture medium can be removed via MEKC separation. Veratraldehyde was separated at -10kV in a background electrolyte containing 50mM tartrate buffer (pH 2.5) and 50mM sodium dodecyl sulfate (SDS) after a plug-plug reaction in the capillary for 5min. The calibration curve of veratraldehyde was linear up to 4pmol (500μM) with a limit to quantification of 0.026pmol (3.2μM) (SN=10). The activity of lignin peroxidase was directly measured from the peak area of veratraldehyde. The activity of lignin peroxidase released from P. chrysosporium into the medium for 7 days was successfully determined to be 3.40UL(-1).
DOI: 10.1016/j.chroma.2016.02.062
PubMed: 26948760
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Direct determination of lignin peroxidase released from Phanerochaete chrysosporium by in-capillary enzyme assay using micellar electrokinetic chromatography.</title><author><name sortKey="Harada, Airi" sort="Harada, Airi" uniqKey="Harada A" first="Airi" last="Harada">Airi Harada</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, Graduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushimanaka, Okayama 700-8530, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Chemistry, Graduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushimanaka, Okayama 700-8530</wicri:regionArea><wicri:noRegion>Okayama 700-8530</wicri:noRegion></affiliation></author><author><name sortKey="Sasaki, Keiko" sort="Sasaki, Keiko" uniqKey="Sasaki K" first="Keiko" last="Sasaki">Keiko Sasaki</name><affiliation wicri:level="4"><nlm:affiliation>Department of Earth Resources Engineering, Graduate School of Engineering, Kyushu University, 744 Motooka, Fukuoka 819-0395, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Earth Resources Engineering, Graduate School of Engineering, Kyushu University, 744 Motooka, Fukuoka 819-0395</wicri:regionArea><orgName type="university">Université de Kyūshū</orgName><placeName><settlement type="city">Fukuoka</settlement><region type="province">Kyūshū</region><region type="prefecture">Préfecture de Fukuoka</region></placeName></affiliation></author><author><name sortKey="Kaneta, Takashi" sort="Kaneta, Takashi" uniqKey="Kaneta T" first="Takashi" last="Kaneta">Takashi Kaneta</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, Graduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushimanaka, Okayama 700-8530, Japan. Electronic address: kaneta@okayama-u.ac.jp.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Chemistry, Graduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushimanaka, Okayama 700-8530</wicri:regionArea><wicri:noRegion>Okayama 700-8530</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2016">2016</date><idno type="RBID">pubmed:26948760</idno><idno type="pmid">26948760</idno><idno type="doi">10.1016/j.chroma.2016.02.062</idno><idno type="wicri:Area/Main/Corpus">000220</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000220</idno><idno type="wicri:Area/Main/Curation">000220</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000220</idno><idno type="wicri:Area/Main/Exploration">000220</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Direct determination of lignin peroxidase released from Phanerochaete chrysosporium by in-capillary enzyme assay using micellar electrokinetic chromatography.</title><author><name sortKey="Harada, Airi" sort="Harada, Airi" uniqKey="Harada A" first="Airi" last="Harada">Airi Harada</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, Graduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushimanaka, Okayama 700-8530, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Chemistry, Graduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushimanaka, Okayama 700-8530</wicri:regionArea><wicri:noRegion>Okayama 700-8530</wicri:noRegion></affiliation></author><author><name sortKey="Sasaki, Keiko" sort="Sasaki, Keiko" uniqKey="Sasaki K" first="Keiko" last="Sasaki">Keiko Sasaki</name><affiliation wicri:level="4"><nlm:affiliation>Department of Earth Resources Engineering, Graduate School of Engineering, Kyushu University, 744 Motooka, Fukuoka 819-0395, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Earth Resources Engineering, Graduate School of Engineering, Kyushu University, 744 Motooka, Fukuoka 819-0395</wicri:regionArea><orgName type="university">Université de Kyūshū</orgName><placeName><settlement type="city">Fukuoka</settlement><region type="province">Kyūshū</region><region type="prefecture">Préfecture de Fukuoka</region></placeName></affiliation></author><author><name sortKey="Kaneta, Takashi" sort="Kaneta, Takashi" uniqKey="Kaneta T" first="Takashi" last="Kaneta">Takashi Kaneta</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, Graduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushimanaka, Okayama 700-8530, Japan. Electronic address: kaneta@okayama-u.ac.jp.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Chemistry, Graduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushimanaka, Okayama 700-8530</wicri:regionArea><wicri:noRegion>Okayama 700-8530</wicri:noRegion></affiliation></author></analytic><series><title level="j">Journal of chromatography. A</title><idno type="eISSN">1873-3778</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Benzyl Alcohols (metabolism)</term><term>Buffers (MeSH)</term><term>Chromatography (instrumentation)</term><term>Culture Media (chemistry)</term><term>Enzyme Assays (instrumentation)</term><term>Enzyme Assays (methods)</term><term>Peroxidases (analysis)</term><term>Peroxidases (metabolism)</term><term>Phanerochaete (enzymology)</term><term>Sodium Dodecyl Sulfate (chemistry)</term><term>Spectrophotometry (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alcools benzyliques (métabolisme)</term><term>Chromatographie (instrumentation)</term><term>Dodécyl-sulfate de sodium (composition chimique)</term><term>Dosages enzymatiques (instrumentation)</term><term>Dosages enzymatiques (méthodes)</term><term>Milieux de culture (composition chimique)</term><term>Peroxidases (analyse)</term><term>Peroxidases (métabolisme)</term><term>Phanerochaete (enzymologie)</term><term>Spectrophotométrie (MeSH)</term><term>Substances tampon (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Culture Media</term><term>Sodium Dodecyl Sulfate</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Benzyl Alcohols</term><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Buffers</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Dodécyl-sulfate de sodium</term><term>Milieux de culture</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="instrumentation" xml:lang="en"><term>Chromatography</term><term>Enzyme Assays</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Enzyme Assays</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Alcools benzyliques</term><term>Chromatographie</term><term>Dosages enzymatiques</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Dosages enzymatiques</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Spectrophotometry</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Spectrophotométrie</term><term>Substances tampon</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Here we describe the application of an in-capillary enzyme assay using micellar electrokinetic chromatography (MEKC) in the determination of enzyme activity in a crude culture medium containing lignin peroxidase released from Phanerochaete chrysosporium (P. chrysosporium). The method consists of a plug-plug reaction between lignin peroxidase and its substrate, veratryl alcohol, the separation of the product, veratraldehyde, from the other components including the enzyme and the culture medium, and the determination of the enzyme activity from the peak area of veratraldehyde produced by the plug-plug reaction. This method is more sensitive than conventional spectrophotometry since the background originates from the enzyme and the culture medium can be removed via MEKC separation. Veratraldehyde was separated at -10kV in a background electrolyte containing 50mM tartrate buffer (pH 2.5) and 50mM sodium dodecyl sulfate (SDS) after a plug-plug reaction in the capillary for 5min. The calibration curve of veratraldehyde was linear up to 4pmol (500μM) with a limit to quantification of 0.026pmol (3.2μM) (SN=10). The activity of lignin peroxidase was directly measured from the peak area of veratraldehyde. The activity of lignin peroxidase released from P. chrysosporium into the medium for 7 days was successfully determined to be 3.40UL(-1). </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" IndexingMethod="Curated" Owner="NLM"><PMID Version="1">26948760</PMID><DateCompleted><Year>2016</Year><Month>10</Month><Day>06</Day></DateCompleted><DateRevised><Year>2018</Year><Month>12</Month><Day>02</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-3778</ISSN><JournalIssue CitedMedium="Internet"><Volume>1440</Volume><PubDate><Year>2016</Year><Month>Apr</Month><Day>01</Day></PubDate></JournalIssue><Title>Journal of chromatography. A</Title><ISOAbbreviation>J Chromatogr A</ISOAbbreviation></Journal><ArticleTitle>Direct determination of lignin peroxidase released from Phanerochaete chrysosporium by in-capillary enzyme assay using micellar electrokinetic chromatography.</ArticleTitle><Pagination><MedlinePgn>145-149</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0021-9673(16)30207-2</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.chroma.2016.02.062</ELocationID><Abstract><AbstractText>Here we describe the application of an in-capillary enzyme assay using micellar electrokinetic chromatography (MEKC) in the determination of enzyme activity in a crude culture medium containing lignin peroxidase released from Phanerochaete chrysosporium (P. chrysosporium). The method consists of a plug-plug reaction between lignin peroxidase and its substrate, veratryl alcohol, the separation of the product, veratraldehyde, from the other components including the enzyme and the culture medium, and the determination of the enzyme activity from the peak area of veratraldehyde produced by the plug-plug reaction. This method is more sensitive than conventional spectrophotometry since the background originates from the enzyme and the culture medium can be removed via MEKC separation. Veratraldehyde was separated at -10kV in a background electrolyte containing 50mM tartrate buffer (pH 2.5) and 50mM sodium dodecyl sulfate (SDS) after a plug-plug reaction in the capillary for 5min. The calibration curve of veratraldehyde was linear up to 4pmol (500μM) with a limit to quantification of 0.026pmol (3.2μM) (SN=10). The activity of lignin peroxidase was directly measured from the peak area of veratraldehyde. The activity of lignin peroxidase released from P. chrysosporium into the medium for 7 days was successfully determined to be 3.40UL(-1). </AbstractText><CopyrightInformation>Copyright © 2016 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Harada</LastName><ForeName>Airi</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Graduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushimanaka, Okayama 700-8530, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sasaki</LastName><ForeName>Keiko</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Earth Resources Engineering, Graduate School of Engineering, Kyushu University, 744 Motooka, Fukuoka 819-0395, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kaneta</LastName><ForeName>Takashi</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Graduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushimanaka, Okayama 700-8530, Japan. Electronic address: kaneta@okayama-u.ac.jp.</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>2016</Year><Month>02</Month><Day>26</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>J Chromatogr A</MedlineTA><NlmUniqueID>9318488</NlmUniqueID><ISSNLinking>0021-9673</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001592">Benzyl Alcohols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002021">Buffers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003470">Culture Media</NameOfSubstance></Chemical><Chemical><RegistryNumber>368GB5141J</RegistryNumber><NameOfSubstance UI="D012967">Sodium Dodecyl Sulfate</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="C042858">lignin peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>MB4T4A711H</RegistryNumber><NameOfSubstance UI="C042197">veratryl alcohol</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001592" MajorTopicYN="N">Benzyl Alcohols</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002021" MajorTopicYN="N">Buffers</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002845" MajorTopicYN="Y">Chromatography</DescriptorName><QualifierName UI="Q000295" MajorTopicYN="N">instrumentation</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003470" MajorTopicYN="N">Culture Media</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D057075" MajorTopicYN="N">Enzyme Assays</DescriptorName><QualifierName UI="Q000295" MajorTopicYN="N">instrumentation</QualifierName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012967" MajorTopicYN="N">Sodium Dodecyl Sulfate</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013053" MajorTopicYN="N">Spectrophotometry</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Capillary electrophoresis</Keyword><Keyword MajorTopicYN="N">Enzyme assay</Keyword><Keyword MajorTopicYN="N">Lignin Peroxidase</Keyword><Keyword MajorTopicYN="N">Micellar electrokinetic chromatography</Keyword><Keyword MajorTopicYN="N">Phanerochaete chrysosporium</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>12</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2016</Year><Month>02</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>02</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>3</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>3</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>10</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26948760</ArticleId><ArticleId IdType="pii">S0021-9673(16)30207-2</ArticleId><ArticleId IdType="doi">10.1016/j.chroma.2016.02.062</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country><region><li>Kyūshū</li><li>Préfecture de Fukuoka</li></region><settlement><li>Fukuoka</li></settlement><orgName><li>Université de Kyūshū</li></orgName></list><tree><country name="Japon"><noRegion><name sortKey="Harada, Airi" sort="Harada, Airi" uniqKey="Harada A" first="Airi" last="Harada">Airi Harada</name></noRegion><name sortKey="Kaneta, Takashi" sort="Kaneta, Takashi" uniqKey="Kaneta T" first="Takashi" last="Kaneta">Takashi Kaneta</name><name sortKey="Sasaki, Keiko" sort="Sasaki, Keiko" uniqKey="Sasaki K" first="Keiko" last="Sasaki">Keiko Sasaki</name></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 000218 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000218 | 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:26948760
|texte= Direct determination of lignin peroxidase released from Phanerochaete chrysosporium by in-capillary enzyme assay using micellar electrokinetic chromatography.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:26948760" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a PhanerochaeteV1
| This area was generated with Dilib version V0.6.37. |  |