Accelerated degradation of lignin by lignin peroxidase isozyme H8 (LiPH8) from Phanerochaete chrysosporium with engineered 4-O-methyltransferase from Clarkia breweri.
Identifieur interne : 000345 ( Main/Exploration ); précédent : 000344; suivant : 000346Accelerated degradation of lignin by lignin peroxidase isozyme H8 (LiPH8) from Phanerochaete chrysosporium with engineered 4-O-methyltransferase from Clarkia breweri.
Auteurs : Le Thanh Mai Pham [Corée du Sud] ; Yong Hwan Kim [Corée du Sud]Source :
- Enzyme and microbial technology [ 1879-0909 ] ; 2014.
Descripteurs français
- KwdFr :
- Alcools benzyliques (métabolisme), Biomasse (MeSH), Clarkia (enzymologie), Clarkia (génétique), Dépollution biologique de l'environnement (MeSH), Ingénierie des protéines (MeSH), Isoenzymes (génétique), Isoenzymes (métabolisme), Lignine (métabolisme), Methyltransferases (génétique), Methyltransferases (métabolisme), Peroxidases (génétique), Peroxidases (métabolisme), Phanerochaete (enzymologie), Phanerochaete (génétique), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Protéines végétales (génétique), Protéines végétales (métabolisme).
- MESH :
- enzymologie : Clarkia, Phanerochaete.
- génétique : Clarkia, Isoenzymes, Methyltransferases, Peroxidases, Phanerochaete, Protéines fongiques, Protéines recombinantes, Protéines végétales.
- métabolisme : Alcools benzyliques, Isoenzymes, Lignine, Methyltransferases, Peroxidases, Protéines fongiques, Protéines recombinantes, Protéines végétales.
- Biomasse, Dépollution biologique de l'environnement, Ingénierie des protéines.
English descriptors
- KwdEn :
- Benzyl Alcohols (metabolism), Biodegradation, Environmental (MeSH), Biomass (MeSH), Clarkia (enzymology), Clarkia (genetics), Fungal Proteins (genetics), Fungal Proteins (metabolism), Isoenzymes (genetics), Isoenzymes (metabolism), Lignin (metabolism), Methyltransferases (genetics), Methyltransferases (metabolism), Peroxidases (genetics), Peroxidases (metabolism), Phanerochaete (enzymology), Phanerochaete (genetics), Plant Proteins (genetics), Plant Proteins (metabolism), Protein Engineering (MeSH), Recombinant Proteins (genetics), Recombinant Proteins (metabolism).
- MESH :
- chemical , genetics : Fungal Proteins, Isoenzymes, Methyltransferases, Peroxidases, Plant Proteins, Recombinant Proteins.
- chemical , metabolism : Benzyl Alcohols, Fungal Proteins, Isoenzymes, Lignin, Methyltransferases, Peroxidases, Plant Proteins, Recombinant Proteins.
- enzymology : Clarkia, Phanerochaete.
- genetics : Clarkia, Phanerochaete.
- Biodegradation, Environmental, Biomass, Protein Engineering.
Abstract
Free-hydroxyl phenolic units can decrease or even abort the catalytic activity of lignin peroxidase H8 during oxidation of veratryl alcohol and model lignin dimers, resulting in slow and inefficient lignin degradation. In this study we applied engineered 4-O-methyltransferase from Clarkia breweri to detoxify the inhibiting free-hydroxyl phenolic groups by converting them to methylated phenolic groups. The multistep, enzyme-catalyzed process that combines 4-O-methyltransferase and lignin peroxidase H8 suggested in this work can increase the efficiency of lignin-degradation. This study also suggests approaching the field of multi-enzyme in vitro systems to improve the understanding and development of plant biomass in biorefinery operations.
DOI: 10.1016/j.enzmictec.2014.08.011
PubMed: 25248703
Affiliations:
Links toward previous steps (curation, corpus...)
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Electronic address: metalkim@kw.ac.kr.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>Department of Chemical Engineering, Kwangwoon University, 447-1, Wolgye-Dong, Nowon-Gu, Seoul 139-701</wicri:regionArea><placeName><settlement type="city">Séoul</settlement><region type="capital">Région capitale de Séoul</region></placeName></affiliation></author></analytic><series><title level="j">Enzyme and microbial technology</title><idno type="eISSN">1879-0909</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Benzyl Alcohols (metabolism)</term><term>Biodegradation, Environmental (MeSH)</term><term>Biomass (MeSH)</term><term>Clarkia (enzymology)</term><term>Clarkia (genetics)</term><term>Fungal Proteins (genetics)</term><term>Fungal Proteins (metabolism)</term><term>Isoenzymes (genetics)</term><term>Isoenzymes (metabolism)</term><term>Lignin (metabolism)</term><term>Methyltransferases (genetics)</term><term>Methyltransferases (metabolism)</term><term>Peroxidases (genetics)</term><term>Peroxidases (metabolism)</term><term>Phanerochaete (enzymology)</term><term>Phanerochaete (genetics)</term><term>Plant Proteins (genetics)</term><term>Plant Proteins (metabolism)</term><term>Protein Engineering (MeSH)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alcools benzyliques (métabolisme)</term><term>Biomasse (MeSH)</term><term>Clarkia (enzymologie)</term><term>Clarkia (génétique)</term><term>Dépollution biologique de l'environnement (MeSH)</term><term>Ingénierie des protéines (MeSH)</term><term>Isoenzymes (génétique)</term><term>Isoenzymes (métabolisme)</term><term>Lignine (métabolisme)</term><term>Methyltransferases (génétique)</term><term>Methyltransferases (métabolisme)</term><term>Peroxidases (génétique)</term><term>Peroxidases (métabolisme)</term><term>Phanerochaete (enzymologie)</term><term>Phanerochaete (génétique)</term><term>Protéines fongiques (génétique)</term><term>Protéines fongiques (métabolisme)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Protéines végétales (génétique)</term><term>Protéines végétales (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Fungal Proteins</term><term>Isoenzymes</term><term>Methyltransferases</term><term>Peroxidases</term><term>Plant Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Benzyl Alcohols</term><term>Fungal Proteins</term><term>Isoenzymes</term><term>Lignin</term><term>Methyltransferases</term><term>Peroxidases</term><term>Plant Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Clarkia</term><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Clarkia</term><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Clarkia</term><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Clarkia</term><term>Isoenzymes</term><term>Methyltransferases</term><term>Peroxidases</term><term>Phanerochaete</term><term>Protéines fongiques</term><term>Protéines recombinantes</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Alcools benzyliques</term><term>Isoenzymes</term><term>Lignine</term><term>Methyltransferases</term><term>Peroxidases</term><term>Protéines fongiques</term><term>Protéines recombinantes</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biodegradation, Environmental</term><term>Biomass</term><term>Protein Engineering</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biomasse</term><term>Dépollution biologique de l'environnement</term><term>Ingénierie des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Free-hydroxyl phenolic units can decrease or even abort the catalytic activity of lignin peroxidase H8 during oxidation of veratryl alcohol and model lignin dimers, resulting in slow and inefficient lignin degradation. In this study we applied engineered 4-O-methyltransferase from Clarkia breweri to detoxify the inhibiting free-hydroxyl phenolic groups by converting them to methylated phenolic groups. The multistep, enzyme-catalyzed process that combines 4-O-methyltransferase and lignin peroxidase H8 suggested in this work can increase the efficiency of lignin-degradation. This study also suggests approaching the field of multi-enzyme in vitro systems to improve the understanding and development of plant biomass in biorefinery operations. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25248703</PMID><DateCompleted><Year>2015</Year><Month>06</Month><Day>22</Day></DateCompleted><DateRevised><Year>2014</Year><Month>09</Month><Day>24</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0909</ISSN><JournalIssue CitedMedium="Internet"><Volume>66</Volume><PubDate><Year>2014</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Enzyme and microbial technology</Title><ISOAbbreviation>Enzyme Microb Technol</ISOAbbreviation></Journal><ArticleTitle>Accelerated degradation of lignin by lignin peroxidase isozyme H8 (LiPH8) from Phanerochaete chrysosporium with engineered 4-O-methyltransferase from Clarkia breweri.</ArticleTitle><Pagination><MedlinePgn>74-9</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.enzmictec.2014.08.011</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0141-0229(14)00155-0</ELocationID><Abstract><AbstractText>Free-hydroxyl phenolic units can decrease or even abort the catalytic activity of lignin peroxidase H8 during oxidation of veratryl alcohol and model lignin dimers, resulting in slow and inefficient lignin degradation. In this study we applied engineered 4-O-methyltransferase from Clarkia breweri to detoxify the inhibiting free-hydroxyl phenolic groups by converting them to methylated phenolic groups. The multistep, enzyme-catalyzed process that combines 4-O-methyltransferase and lignin peroxidase H8 suggested in this work can increase the efficiency of lignin-degradation. This study also suggests approaching the field of multi-enzyme in vitro systems to improve the understanding and development of plant biomass in biorefinery operations. </AbstractText><CopyrightInformation>Copyright © 2014 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pham</LastName><ForeName>Le Thanh Mai</ForeName><Initials>le TM</Initials><AffiliationInfo><Affiliation>Department of Chemical Engineering, Kwangwoon University, 447-1, Wolgye-Dong, Nowon-Gu, Seoul 139-701, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Yong Hwan</ForeName><Initials>YH</Initials><AffiliationInfo><Affiliation>Department of Chemical Engineering, Kwangwoon University, 447-1, Wolgye-Dong, Nowon-Gu, Seoul 139-701, Republic of Korea. Electronic address: metalkim@kw.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>2014</Year><Month>09</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Enzyme Microb Technol</MedlineTA><NlmUniqueID>8003761</NlmUniqueID><ISSNLinking>0141-0229</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001592">Benzyl Alcohols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></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="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015202" MajorTopicYN="N">Protein Engineering</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Free-hydroxyl phenolic group</Keyword><Keyword MajorTopicYN="N">Lignin peroxidase</Keyword><Keyword MajorTopicYN="N">Lignin-degradation</Keyword><Keyword MajorTopicYN="N">O-Methyltransferase</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>06</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2014</Year><Month>08</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>08</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>9</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>9</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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