Production of d-glucuronic acid from myo-inositol using Escherichia coli whole-cell biocatalyst overexpressing a novel myo-inositol oxygenase from Thermothelomyces thermophile.
Identifieur interne : 000404 ( Main/Exploration ); précédent : 000403; suivant : 000405Production of d-glucuronic acid from myo-inositol using Escherichia coli whole-cell biocatalyst overexpressing a novel myo-inositol oxygenase from Thermothelomyces thermophile.
Auteurs : Fei Teng [République populaire de Chine] ; Ran You [République populaire de Chine] ; Meirong Hu [République populaire de Chine] ; Weifeng Liu [République populaire de Chine] ; Lei Wang [République populaire de Chine] ; Yong Tao [République populaire de Chine]Source :
- Enzyme and microbial technology [ 1879-0909 ] ; 2019.
Descripteurs français
- KwdFr :
- Acide glucuronique (métabolisme), Animaux (MeSH), Arabidopsis (enzymologie), Arabidopsis (génétique), Biotransformation (MeSH), Chaetomium (enzymologie), Chaetomium (génétique), Cryptococcus neoformans (enzymologie), Cryptococcus neoformans (génétique), Escherichia coli (génétique), Escherichia coli (métabolisme), Expression des gènes (MeSH), Inositol (métabolisme), Inositol oxygenase (génétique), Inositol oxygenase (métabolisme), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Sordariales (enzymologie), Sordariales (génétique), Souris (MeSH).
- MESH :
- enzymologie : Arabidopsis, Chaetomium, Cryptococcus neoformans, Sordariales.
- génétique : Arabidopsis, Chaetomium, Cryptococcus neoformans, Escherichia coli, Inositol oxygenase, Protéines recombinantes, Sordariales.
- métabolisme : Acide glucuronique, Escherichia coli, Inositol, Inositol oxygenase, Protéines recombinantes.
- Animaux, Biotransformation, Expression des gènes, Souris.
English descriptors
- KwdEn :
- Animals (MeSH), Arabidopsis (enzymology), Arabidopsis (genetics), Biotransformation (MeSH), Chaetomium (enzymology), Chaetomium (genetics), Cryptococcus neoformans (enzymology), Cryptococcus neoformans (genetics), Escherichia coli (genetics), Escherichia coli (metabolism), Gene Expression (MeSH), Glucuronic Acid (metabolism), Inositol (metabolism), Inositol Oxygenase (genetics), Inositol Oxygenase (metabolism), Mice (MeSH), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Sordariales (enzymology), Sordariales (genetics).
- MESH :
- chemical , genetics : Inositol Oxygenase, Recombinant Proteins.
- chemical , metabolism : Glucuronic Acid, Inositol, Inositol Oxygenase, Recombinant Proteins.
- enzymology : Arabidopsis, Chaetomium, Cryptococcus neoformans, Sordariales.
- genetics : Arabidopsis, Chaetomium, Cryptococcus neoformans, Escherichia coli, Sordariales.
- metabolism : Escherichia coli.
- Animals, Biotransformation, Gene Expression, Mice.
Abstract
D-glucuronic acid (GlcUA) is an important intermediate with numerous applications in the food, cosmetics, and pharmaceutical industries. Its biological production routes which employ myo-inositol oxygenase (MIOX) as the key enzyme are attractive. In this study, five diverse MIOX-encoding genes, from Cryptococcus neoformans, Chaetomium thermophilum, Arabidopsis thaliana, Thermothelomyces thermophila, and Mus musculus were overexpressed in Escherichia coli, respectively. A novel MIOX from Thermothelomyces thermophila (TtMIOX) exhibited high specific activity, and efficiently converted myo-inositol to GlcUA. Meanwhile, the degradation of GlcUA was inhibited by inactivation of uxaC from the Escherichia coli genome. Finally, the BWΔuxaC whole-cell biocatalyst harboring TtMIOX resulted in the production of 106 g/L GlcUA within 12 h in a 1-L bioreactor, corresponding to a conversion of 91% and productivity of 8.83 g/L/h. This study provides a feasible method for the industrial production of GlcUA.
DOI: 10.1016/j.enzmictec.2019.04.013
PubMed: 31088620
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Electronic address: wl8893@163.com.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Institute of Microbiology, Chinese Academy of Sciences, CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Beijing</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author><author><name sortKey="Tao, Yong" sort="Tao, Yong" uniqKey="Tao Y" first="Yong" last="Tao">Yong Tao</name><affiliation wicri:level="3"><nlm:affiliation>College of Life Science, University of Chinese Academy of Sciences, Beijing, China. Electronic address: taoyong@im.ac.cn.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Life Science, University of Chinese Academy of Sciences, Beijing</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author></analytic><series><title level="j">Enzyme and microbial technology</title><idno type="eISSN">1879-0909</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Arabidopsis (enzymology)</term><term>Arabidopsis (genetics)</term><term>Biotransformation (MeSH)</term><term>Chaetomium (enzymology)</term><term>Chaetomium (genetics)</term><term>Cryptococcus neoformans (enzymology)</term><term>Cryptococcus neoformans (genetics)</term><term>Escherichia coli (genetics)</term><term>Escherichia coli (metabolism)</term><term>Gene Expression (MeSH)</term><term>Glucuronic Acid (metabolism)</term><term>Inositol (metabolism)</term><term>Inositol Oxygenase (genetics)</term><term>Inositol Oxygenase (metabolism)</term><term>Mice (MeSH)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Sordariales (enzymology)</term><term>Sordariales (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide glucuronique (métabolisme)</term><term>Animaux (MeSH)</term><term>Arabidopsis (enzymologie)</term><term>Arabidopsis (génétique)</term><term>Biotransformation (MeSH)</term><term>Chaetomium (enzymologie)</term><term>Chaetomium (génétique)</term><term>Cryptococcus neoformans (enzymologie)</term><term>Cryptococcus neoformans (génétique)</term><term>Escherichia coli (génétique)</term><term>Escherichia coli (métabolisme)</term><term>Expression des gènes (MeSH)</term><term>Inositol (métabolisme)</term><term>Inositol oxygenase (génétique)</term><term>Inositol oxygenase (métabolisme)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Sordariales (enzymologie)</term><term>Sordariales (génétique)</term><term>Souris (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Inositol Oxygenase</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glucuronic Acid</term><term>Inositol</term><term>Inositol Oxygenase</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Arabidopsis</term><term>Chaetomium</term><term>Cryptococcus neoformans</term><term>Sordariales</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Arabidopsis</term><term>Chaetomium</term><term>Cryptococcus neoformans</term><term>Sordariales</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Arabidopsis</term><term>Chaetomium</term><term>Cryptococcus neoformans</term><term>Escherichia coli</term><term>Sordariales</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Arabidopsis</term><term>Chaetomium</term><term>Cryptococcus neoformans</term><term>Escherichia coli</term><term>Inositol oxygenase</term><term>Protéines recombinantes</term><term>Sordariales</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acide glucuronique</term><term>Escherichia coli</term><term>Inositol</term><term>Inositol oxygenase</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Biotransformation</term><term>Gene Expression</term><term>Mice</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Biotransformation</term><term>Expression des gènes</term><term>Souris</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">D-glucuronic acid (GlcUA) is an important intermediate with numerous applications in the food, cosmetics, and pharmaceutical industries. Its biological production routes which employ myo-inositol oxygenase (MIOX) as the key enzyme are attractive. In this study, five diverse MIOX-encoding genes, from Cryptococcus neoformans, Chaetomium thermophilum, Arabidopsis thaliana, Thermothelomyces thermophila, and Mus musculus were overexpressed in Escherichia coli, respectively. A novel MIOX from Thermothelomyces thermophila (TtMIOX) exhibited high specific activity, and efficiently converted myo-inositol to GlcUA. Meanwhile, the degradation of GlcUA was inhibited by inactivation of uxaC from the Escherichia coli genome. Finally, the BWΔuxaC whole-cell biocatalyst harboring TtMIOX resulted in the production of 106 g/L GlcUA within 12 h in a 1-L bioreactor, corresponding to a conversion of 91% and productivity of 8.83 g/L/h. This study provides a feasible method for the industrial production of GlcUA.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31088620</PMID><DateCompleted><Year>2019</Year><Month>08</Month><Day>22</Day></DateCompleted><DateRevised><Year>2019</Year><Month>08</Month><Day>22</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0909</ISSN><JournalIssue CitedMedium="Internet"><Volume>127</Volume><PubDate><Year>2019</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Enzyme and microbial technology</Title><ISOAbbreviation>Enzyme Microb Technol</ISOAbbreviation></Journal><ArticleTitle>Production of d-glucuronic acid from myo-inositol using Escherichia coli whole-cell biocatalyst overexpressing a novel myo-inositol oxygenase from Thermothelomyces thermophile.</ArticleTitle><Pagination><MedlinePgn>70-74</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0141-0229(19)30063-8</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.enzmictec.2019.04.013</ELocationID><Abstract><AbstractText>D-glucuronic acid (GlcUA) is an important intermediate with numerous applications in the food, cosmetics, and pharmaceutical industries. Its biological production routes which employ myo-inositol oxygenase (MIOX) as the key enzyme are attractive. In this study, five diverse MIOX-encoding genes, from Cryptococcus neoformans, Chaetomium thermophilum, Arabidopsis thaliana, Thermothelomyces thermophila, and Mus musculus were overexpressed in Escherichia coli, respectively. A novel MIOX from Thermothelomyces thermophila (TtMIOX) exhibited high specific activity, and efficiently converted myo-inositol to GlcUA. Meanwhile, the degradation of GlcUA was inhibited by inactivation of uxaC from the Escherichia coli genome. Finally, the BWΔuxaC whole-cell biocatalyst harboring TtMIOX resulted in the production of 106 g/L GlcUA within 12 h in a 1-L bioreactor, corresponding to a conversion of 91% and productivity of 8.83 g/L/h. This study provides a feasible method for the industrial production of GlcUA.</AbstractText><CopyrightInformation>Copyright © 2019 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Teng</LastName><ForeName>Fei</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Institute of Microbiology, Chinese Academy of Sciences, CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Beijing, China; College of Life Science, University of Chinese Academy of Sciences, Beijing, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>You</LastName><ForeName>Ran</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Institute of Microbiology, Chinese Academy of Sciences, CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Beijing, China; University of Science and Technology of China, Anhui, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hu</LastName><ForeName>Meirong</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Institute of Microbiology, Chinese Academy of Sciences, CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Beijing, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Weifeng</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>Institute of Microbiology, Chinese Academy of Sciences, CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Beijing, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Lei</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Institute of Microbiology, Chinese Academy of Sciences, CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Beijing, China. Electronic address: wl8893@163.com.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tao</LastName><ForeName>Yong</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>College of Life Science, University of Chinese Academy of Sciences, Beijing, China. Electronic address: taoyong@im.ac.cn.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>04</Month><Day>24</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="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>4L6452S749</RegistryNumber><NameOfSubstance UI="D007294">Inositol</NameOfSubstance></Chemical><Chemical><RegistryNumber>8A5D83Q4RW</RegistryNumber><NameOfSubstance UI="D020723">Glucuronic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.13.99.1</RegistryNumber><NameOfSubstance UI="D050562">Inositol Oxygenase</NameOfSubstance></Chemical></ChemicalList><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001711" MajorTopicYN="N">Biotransformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002597" MajorTopicYN="N">Chaetomium</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003455" MajorTopicYN="N">Cryptococcus neoformans</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="Y">Gene Expression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020723" MajorTopicYN="N">Glucuronic Acid</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007294" MajorTopicYN="N">Inositol</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D050562" MajorTopicYN="N">Inositol Oxygenase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020037" MajorTopicYN="N">Sordariales</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">D-glucuronic acid</Keyword><Keyword MajorTopicYN="N">Myo-inositol oxygenase</Keyword><Keyword MajorTopicYN="N">Thermothelomyces thermophile</Keyword><Keyword MajorTopicYN="N">Whole-cell biocatalyst</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>03</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2019</Year><Month>04</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>04</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>5</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>5</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>8</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31088620</ArticleId><ArticleId IdType="pii">S0141-0229(19)30063-8</ArticleId><ArticleId IdType="doi">10.1016/j.enzmictec.2019.04.013</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="Teng, Fei" sort="Teng, Fei" uniqKey="Teng F" first="Fei" last="Teng">Fei Teng</name></noRegion><name sortKey="Hu, Meirong" sort="Hu, Meirong" uniqKey="Hu M" first="Meirong" last="Hu">Meirong Hu</name><name sortKey="Liu, Weifeng" sort="Liu, Weifeng" uniqKey="Liu W" first="Weifeng" last="Liu">Weifeng Liu</name><name sortKey="Tao, Yong" sort="Tao, Yong" uniqKey="Tao Y" first="Yong" last="Tao">Yong Tao</name><name sortKey="Wang, Lei" sort="Wang, Lei" uniqKey="Wang L" first="Lei" last="Wang">Lei Wang</name><name sortKey="You, Ran" sort="You, Ran" uniqKey="You R" first="Ran" last="You">Ran You</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|texte= Production of d-glucuronic acid from myo-inositol using Escherichia coli whole-cell biocatalyst overexpressing a novel myo-inositol oxygenase from Thermothelomyces thermophile.
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