Optimization of rhamnetin production in Escherichia coli.
Identifieur interne : 002D72 ( Main/Exploration ); précédent : 002D71; suivant : 002D73Optimization of rhamnetin production in Escherichia coli.
Auteurs : Su Hyun Sung [Corée du Sud] ; Bong-Gyu Kim ; Joong-Hoon AhnSource :
- Journal of microbiology and biotechnology [ 1738-8872 ] ; 2011.
Descripteurs français
- KwdFr :
- Biotransformation (MeSH), Clonage moléculaire (MeSH), Escherichia coli (génétique), Escherichia coli (métabolisme), Génie génétique (méthodes), Methyltransferases (génétique), Methyltransferases (métabolisme), Microbiologie industrielle (MeSH), Protéines Escherichia coli (génétique), Protéines Escherichia coli (métabolisme), Quercétine (analogues et dérivés), Quercétine (génétique), Quercétine (métabolisme).
- MESH :
- analogues et dérivés : Quercétine.
- génétique : Escherichia coli, Methyltransferases, Protéines Escherichia coli, Quercétine.
- métabolisme : Escherichia coli, Methyltransferases, Protéines Escherichia coli, Quercétine.
- méthodes : Génie génétique.
- Biotransformation, Clonage moléculaire, Microbiologie industrielle.
English descriptors
- KwdEn :
- Biotransformation (MeSH), Cloning, Molecular (MeSH), Escherichia coli (genetics), Escherichia coli (metabolism), Escherichia coli Proteins (genetics), Escherichia coli Proteins (metabolism), Genetic Engineering (methods), Industrial Microbiology (MeSH), Methyltransferases (genetics), Methyltransferases (metabolism), Quercetin (analogs & derivatives), Quercetin (genetics), Quercetin (metabolism).
- MESH :
- chemical , analogs & derivatives : Quercetin.
- chemical , genetics : Escherichia coli Proteins, Methyltransferases, Quercetin.
- genetics : Escherichia coli.
- metabolism : Escherichia coli, Escherichia coli Proteins, Methyltransferases, Quercetin.
- methods : Genetic Engineering.
- Biotransformation, Cloning, Molecular, Industrial Microbiology.
Abstract
POMT7, which is an O-methyltransferase from poplar, transfers a methyl group to several flavonoids that contain a 7-hydroxyl group. POMT7 has been shown to have a higher affinity toward quercetin, and the reaction product rhamnetin has been shown to inhibit the formation of beta-amyloid. Thus, rhamnetin holds great promise for use in therapeutic applications; however, methods for mass production of this compound are not currently available. In this study, quercetin was biotransformed into rhamnetin using Escherichia coli expressing POMT7, with the goal of developing an approach for mass production of rhamnetin. In order to maximize the production of rhamnetin, POMT7 was subcloned into four different E. coli expression vectors, each of which was maintained in E. coli with a different copy number, and the best expression vector was selected. In addition, the S-adenosylmethionine biosynthesis pathway was engineered for optimal cofactor production. Through the combination of optimized POMT7 expression and cofactor production, the production of rhamnetin was increased up to 111 mg/l, which is approximately 2-fold higher compared with the E. coli strain containing only POMT7.
DOI: 10.4014/jmb.1104.04048
PubMed: 21876376
Affiliations:
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University, Seoul 143-701, Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>Bio/Molecular Informatics Center, Department of Bioscience and Biotechnology, Konkuk University, Seoul 143-701</wicri:regionArea><placeName><settlement type="city">Séoul</settlement><region type="capital">Région capitale de Séoul</region></placeName></affiliation></author><author><name sortKey="Kim, Bong Gyu" sort="Kim, Bong Gyu" uniqKey="Kim B" first="Bong-Gyu" last="Kim">Bong-Gyu Kim</name></author><author><name sortKey="Ahn, Joong Hoon" sort="Ahn, Joong Hoon" uniqKey="Ahn J" first="Joong-Hoon" last="Ahn">Joong-Hoon Ahn</name></author></analytic><series><title level="j">Journal of microbiology and biotechnology</title><idno type="eISSN">1738-8872</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biotransformation (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>Escherichia coli (genetics)</term><term>Escherichia coli (metabolism)</term><term>Escherichia coli Proteins (genetics)</term><term>Escherichia coli Proteins (metabolism)</term><term>Genetic Engineering (methods)</term><term>Industrial Microbiology (MeSH)</term><term>Methyltransferases (genetics)</term><term>Methyltransferases (metabolism)</term><term>Quercetin (analogs & derivatives)</term><term>Quercetin (genetics)</term><term>Quercetin (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Biotransformation (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Escherichia coli (génétique)</term><term>Escherichia coli (métabolisme)</term><term>Génie génétique (méthodes)</term><term>Methyltransferases (génétique)</term><term>Methyltransferases (métabolisme)</term><term>Microbiologie industrielle (MeSH)</term><term>Protéines Escherichia coli (génétique)</term><term>Protéines Escherichia coli (métabolisme)</term><term>Quercétine (analogues et dérivés)</term><term>Quercétine (génétique)</term><term>Quercétine (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Quercetin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Escherichia coli Proteins</term><term>Methyltransferases</term><term>Quercetin</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Quercétine</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term><term>Methyltransferases</term><term>Protéines Escherichia coli</term><term>Quercétine</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term><term>Escherichia coli Proteins</term><term>Methyltransferases</term><term>Quercetin</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Genetic Engineering</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Escherichia coli</term><term>Methyltransferases</term><term>Protéines Escherichia coli</term><term>Quercétine</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Génie génétique</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biotransformation</term><term>Cloning, Molecular</term><term>Industrial Microbiology</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biotransformation</term><term>Clonage moléculaire</term><term>Microbiologie industrielle</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">POMT7, which is an O-methyltransferase from poplar, transfers a methyl group to several flavonoids that contain a 7-hydroxyl group. POMT7 has been shown to have a higher affinity toward quercetin, and the reaction product rhamnetin has been shown to inhibit the formation of beta-amyloid. Thus, rhamnetin holds great promise for use in therapeutic applications; however, methods for mass production of this compound are not currently available. In this study, quercetin was biotransformed into rhamnetin using Escherichia coli expressing POMT7, with the goal of developing an approach for mass production of rhamnetin. In order to maximize the production of rhamnetin, POMT7 was subcloned into four different E. coli expression vectors, each of which was maintained in E. coli with a different copy number, and the best expression vector was selected. In addition, the S-adenosylmethionine biosynthesis pathway was engineered for optimal cofactor production. Through the combination of optimized POMT7 expression and cofactor production, the production of rhamnetin was increased up to 111 mg/l, which is approximately 2-fold higher compared with the E. coli strain containing only POMT7.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21876376</PMID><DateCompleted><Year>2011</Year><Month>12</Month><Day>05</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1738-8872</ISSN><JournalIssue CitedMedium="Internet"><Volume>21</Volume><Issue>8</Issue><PubDate><Year>2011</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Journal of microbiology and biotechnology</Title><ISOAbbreviation>J Microbiol Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Optimization of rhamnetin production in Escherichia coli.</ArticleTitle><Pagination><MedlinePgn>854-7</MedlinePgn></Pagination><Abstract><AbstractText>POMT7, which is an O-methyltransferase from poplar, transfers a methyl group to several flavonoids that contain a 7-hydroxyl group. POMT7 has been shown to have a higher affinity toward quercetin, and the reaction product rhamnetin has been shown to inhibit the formation of beta-amyloid. Thus, rhamnetin holds great promise for use in therapeutic applications; however, methods for mass production of this compound are not currently available. In this study, quercetin was biotransformed into rhamnetin using Escherichia coli expressing POMT7, with the goal of developing an approach for mass production of rhamnetin. In order to maximize the production of rhamnetin, POMT7 was subcloned into four different E. coli expression vectors, each of which was maintained in E. coli with a different copy number, and the best expression vector was selected. In addition, the S-adenosylmethionine biosynthesis pathway was engineered for optimal cofactor production. 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