Expression in yeast of secreted lignin peroxidase with improved 2,4-dichlorophenol degradability by DNA shuffling.
Identifieur interne : 000693 ( Main/Exploration ); précédent : 000692; suivant : 000694Expression in yeast of secreted lignin peroxidase with improved 2,4-dichlorophenol degradability by DNA shuffling.
Auteurs : Kang Ryu [Corée du Sud] ; Jung Hye Kang ; Lishi Wang ; E K LeeSource :
- Journal of biotechnology [ 0168-1656 ] ; 2008.
Descripteurs français
- KwdFr :
- Brassage d'ADN (MeSH), Chlorophénols (métabolisme), Cinétique (MeSH), Colorimétrie (MeSH), Dépollution biologique de l'environnement (MeSH), Milieux de culture (MeSH), Mutation (génétique), Peroxidases (métabolisme), Phanerochaete (enzymologie), Saccharomyces cerevisiae (génétique), Structure secondaire des protéines (MeSH), Substitution d'acide aminé (MeSH).
- MESH :
- enzymologie : Phanerochaete.
- génétique : Mutation, Saccharomyces cerevisiae.
- métabolisme : Chlorophénols, Peroxidases.
- Brassage d'ADN, Cinétique, Colorimétrie, Dépollution biologique de l'environnement, Milieux de culture, Structure secondaire des protéines, Substitution d'acide aminé.
English descriptors
- KwdEn :
- Amino Acid Substitution (MeSH), Biodegradation, Environmental (MeSH), Chlorophenols (metabolism), Colorimetry (MeSH), Culture Media (MeSH), DNA Shuffling (MeSH), Kinetics (MeSH), Mutation (genetics), Peroxidases (metabolism), Phanerochaete (enzymology), Protein Structure, Secondary (MeSH), Saccharomyces cerevisiae (genetics).
- MESH :
- chemical , metabolism : Chlorophenols, Peroxidases.
- enzymology : Phanerochaete.
- genetics : Mutation, Saccharomyces cerevisiae.
- Amino Acid Substitution, Biodegradation, Environmental, Colorimetry, Culture Media, DNA Shuffling, Kinetics, Protein Structure, Secondary.
Abstract
Lignin peroxidase (LiP) from Phanerochaete chrysosporium was shown to mineralize a variety of recalcitrant aromatic compounds and oxidize a number of polycyclic aromatic and phenolic compounds. The major problem of the wild type LiP is that it can be inactivated by excess H(2)O(2) and high concentrations of aromatic compounds. We applied a directed evolution technique coupled with a rapid colorimetric screening method to obtain mutant genes with improved H(2)O(2) stability and polychlorinated phenol degradability, and they were successfully expressed as the secretive LiPs in recombinant Saccharomyces cerevisiae. The resulting variants showed approximately 1.6-fold improved 2,4-dichlorophenol (2,4-DCP) degradation activity and stability against H(2)O(2) compared with the parent strain. The kinetic properties of the variants toward 2,4-DCP and H(2)O(2) were also increased compared with the wild type for all three mutants studied. Amino acid sequence analysis indicated that the greatest number of amino acid substitutions was located near the surface or Ca(2+) binding sites of the enzyme.
DOI: 10.1016/j.jbiotec.2008.04.007
PubMed: 18514942
Affiliations:
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Kang</name></author><author><name sortKey="Wang, Lishi" sort="Wang, Lishi" uniqKey="Wang L" first="Lishi" last="Wang">Lishi Wang</name></author><author><name sortKey="Lee, E K" sort="Lee, E K" uniqKey="Lee E" first="E K" last="Lee">E K Lee</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2008">2008</date><idno type="RBID">pubmed:18514942</idno><idno type="pmid">18514942</idno><idno type="doi">10.1016/j.jbiotec.2008.04.007</idno><idno type="wicri:Area/Main/Corpus">000690</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000690</idno><idno type="wicri:Area/Main/Curation">000690</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000690</idno><idno type="wicri:Area/Main/Exploration">000690</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Expression in yeast of secreted lignin peroxidase with improved 2,4-dichlorophenol degradability by DNA 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uniqKey="Lee E" first="E K" last="Lee">E K Lee</name></author></analytic><series><title level="j">Journal of biotechnology</title><idno type="ISSN">0168-1656</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Substitution (MeSH)</term><term>Biodegradation, Environmental (MeSH)</term><term>Chlorophenols (metabolism)</term><term>Colorimetry (MeSH)</term><term>Culture Media (MeSH)</term><term>DNA Shuffling (MeSH)</term><term>Kinetics (MeSH)</term><term>Mutation (genetics)</term><term>Peroxidases (metabolism)</term><term>Phanerochaete (enzymology)</term><term>Protein Structure, Secondary (MeSH)</term><term>Saccharomyces cerevisiae (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Brassage d'ADN (MeSH)</term><term>Chlorophénols (métabolisme)</term><term>Cinétique (MeSH)</term><term>Colorimétrie (MeSH)</term><term>Dépollution biologique de l'environnement (MeSH)</term><term>Milieux de culture (MeSH)</term><term>Mutation (génétique)</term><term>Peroxidases (métabolisme)</term><term>Phanerochaete (enzymologie)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Structure secondaire des protéines (MeSH)</term><term>Substitution d'acide aminé (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Chlorophenols</term><term>Peroxidases</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>Mutation</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Mutation</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Chlorophénols</term><term>Peroxidases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term><term>Biodegradation, Environmental</term><term>Colorimetry</term><term>Culture Media</term><term>DNA Shuffling</term><term>Kinetics</term><term>Protein Structure, Secondary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Brassage d'ADN</term><term>Cinétique</term><term>Colorimétrie</term><term>Dépollution biologique de l'environnement</term><term>Milieux de culture</term><term>Structure secondaire des protéines</term><term>Substitution d'acide aminé</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Lignin peroxidase (LiP) from Phanerochaete chrysosporium was shown to mineralize a variety of recalcitrant aromatic compounds and oxidize a number of polycyclic aromatic and phenolic compounds. The major problem of the wild type LiP is that it can be inactivated by excess H(2)O(2) and high concentrations of aromatic compounds. We applied a directed evolution technique coupled with a rapid colorimetric screening method to obtain mutant genes with improved H(2)O(2) stability and polychlorinated phenol degradability, and they were successfully expressed as the secretive LiPs in recombinant Saccharomyces cerevisiae. The resulting variants showed approximately 1.6-fold improved 2,4-dichlorophenol (2,4-DCP) degradation activity and stability against H(2)O(2) compared with the parent strain. The kinetic properties of the variants toward 2,4-DCP and H(2)O(2) were also increased compared with the wild type for all three mutants studied. Amino acid sequence analysis indicated that the greatest number of amino acid substitutions was located near the surface or Ca(2+) binding sites of the enzyme.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18514942</PMID><DateCompleted><Year>2008</Year><Month>10</Month><Day>06</Day></DateCompleted><DateRevised><Year>2018</Year><Month>12</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0168-1656</ISSN><JournalIssue CitedMedium="Print"><Volume>135</Volume><Issue>3</Issue><PubDate><Year>2008</Year><Month>Jun</Month><Day>30</Day></PubDate></JournalIssue><Title>Journal of biotechnology</Title><ISOAbbreviation>J Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Expression in yeast of secreted lignin peroxidase with improved 2,4-dichlorophenol degradability by DNA shuffling.</ArticleTitle><Pagination><MedlinePgn>241-6</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jbiotec.2008.04.007</ELocationID><Abstract><AbstractText>Lignin peroxidase (LiP) from Phanerochaete chrysosporium was shown to mineralize a variety of recalcitrant aromatic compounds and oxidize a number of polycyclic aromatic and phenolic compounds. The major problem of the wild type LiP is that it can be inactivated by excess H(2)O(2) and high concentrations of aromatic compounds. We applied a directed evolution technique coupled with a rapid colorimetric screening method to obtain mutant genes with improved H(2)O(2) stability and polychlorinated phenol degradability, and they were successfully expressed as the secretive LiPs in recombinant Saccharomyces cerevisiae. The resulting variants showed approximately 1.6-fold improved 2,4-dichlorophenol (2,4-DCP) degradation activity and stability against H(2)O(2) compared with the parent strain. The kinetic properties of the variants toward 2,4-DCP and H(2)O(2) were also increased compared with the wild type for all three mutants studied. Amino acid sequence analysis indicated that the greatest number of amino acid substitutions was located near the surface or Ca(2+) binding sites of the enzyme.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ryu</LastName><ForeName>Kang</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Catholic Research Institute of Medical Science, College of Medicine, The Catholic University of Korea, 505 Banpo-dong, Seocho-gu, Seoul, Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kang</LastName><ForeName>Jung Hye</ForeName><Initials>JH</Initials></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Lishi</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>E K</ForeName><Initials>EK</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, 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Séoul</li></region><settlement><li>Séoul</li></settlement></list><tree><noCountry><name sortKey="Kang, Jung Hye" sort="Kang, Jung Hye" uniqKey="Kang J" first="Jung Hye" last="Kang">Jung Hye Kang</name><name sortKey="Lee, E K" sort="Lee, E K" uniqKey="Lee E" first="E K" last="Lee">E K Lee</name><name sortKey="Wang, Lishi" sort="Wang, Lishi" uniqKey="Wang L" first="Lishi" last="Wang">Lishi Wang</name></noCountry><country name="Corée du Sud"><region name="Région capitale de Séoul"><name sortKey="Ryu, Kang" sort="Ryu, Kang" uniqKey="Ryu K" first="Kang" last="Ryu">Kang Ryu</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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