Characterization of an aldo–keto reductase from Thermotoga maritima with high thermostability and a broad substrate spectrum
A novel aldo–keto reductase gene, Tm1743, from Thermotoga maritima was overexpressed in Escherichia coli. The enzyme displayed the highest activity at 90 °C and at pH 9. It retained 63 % of its activity after 15 h at 85 °C. The enzyme also could tolerate (up to 10 % v/v) acetonitrile, ethanol and 2-...
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| Veröffentlicht in: | Biotechnology letters 2013-05, Vol.35 (5), p.757-762 |
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| container_title | Biotechnology letters |
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| creator | Ma, Yuan-Hui Lv, Dan-Qing Zhou, Shuo Lai, Dun-Yue Chen, Zhen-Ming |
| description | A novel aldo–keto reductase gene, Tm1743, from Thermotoga maritima was overexpressed in Escherichia coli. The enzyme displayed the highest activity at 90 °C and at pH 9. It retained 63 % of its activity after 15 h at 85 °C. The enzyme also could tolerate (up to 10 % v/v) acetonitrile, ethanol and 2-propanol with slightly increased activities. Methanol, DMSO and acetone decreased activity slightly. Furthermore, Tm1743 exhibited broad substrate specificity towards various keto esters, ketones and aldehydes, with relative activities ranging from 2 to 460 % compared to the control. Its optimum substrate, 2,2,2-trifluoroacetophenone, was asymmetrically reduced in a coupled NADPH-regeneration system with an enantioselectivity of 99.8 % and a conversion of 98 %. |
| doi_str_mv | 10.1007/s10529-013-1141-6 |
| format | Article |
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The enzyme displayed the highest activity at 90 °C and at pH 9. It retained 63 % of its activity after 15 h at 85 °C. The enzyme also could tolerate (up to 10 % v/v) acetonitrile, ethanol and 2-propanol with slightly increased activities. Methanol, DMSO and acetone decreased activity slightly. Furthermore, Tm1743 exhibited broad substrate specificity towards various keto esters, ketones and aldehydes, with relative activities ranging from 2 to 460 % compared to the control. Its optimum substrate, 2,2,2-trifluoroacetophenone, was asymmetrically reduced in a coupled NADPH-regeneration system with an enantioselectivity of 99.8 % and a conversion of 98 %.</description><identifier>ISSN: 0141-5492</identifier><identifier>EISSN: 1573-6776</identifier><identifier>DOI: 10.1007/s10529-013-1141-6</identifier><identifier>PMID: 23338701</identifier><language>eng</language><publisher>Dordrecht: Springer-Verlag</publisher><subject>acetone ; Alcohol Oxidoreductases - chemistry ; Alcohol Oxidoreductases - metabolism ; Aldehyde Reductase ; Aldehydes ; Aldo-Keto Reductases ; Applied Microbiology ; Asymmetry ; Biochemistry ; Biomedical and Life Sciences ; Biotechnology ; dimethyl sulfoxide ; enantiomers ; Enzyme Stability ; Enzymes ; Escherichia coli ; Esters ; Ethanol ; Ethyl alcohol ; gene overexpression ; genes ; isopropyl alcohol ; Kinetics ; Life Sciences ; methanol ; Methyl alcohol ; Microbiology ; Original Research Paper ; Reductases ; Stereoisomerism ; Substrate Specificity ; Temperature ; thermal stability ; Thermotoga maritima ; Thermotoga maritima - enzymology</subject><ispartof>Biotechnology letters, 2013-05, Vol.35 (5), p.757-762</ispartof><rights>Springer Science+Business Media Dordrecht 2013</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c458t-190663db1112f091e4bdd665635a09c4f99980ad91de78ae96f77b6239cd0fb93</citedby><cites>FETCH-LOGICAL-c458t-190663db1112f091e4bdd665635a09c4f99980ad91de78ae96f77b6239cd0fb93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10529-013-1141-6$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10529-013-1141-6$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23338701$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ma, Yuan-Hui</creatorcontrib><creatorcontrib>Lv, Dan-Qing</creatorcontrib><creatorcontrib>Zhou, Shuo</creatorcontrib><creatorcontrib>Lai, Dun-Yue</creatorcontrib><creatorcontrib>Chen, Zhen-Ming</creatorcontrib><title>Characterization of an aldo–keto reductase from Thermotoga maritima with high thermostability and a broad substrate spectrum</title><title>Biotechnology letters</title><addtitle>Biotechnol Lett</addtitle><addtitle>Biotechnol Lett</addtitle><description>A novel aldo–keto reductase gene, Tm1743, from Thermotoga maritima was overexpressed in Escherichia coli. The enzyme displayed the highest activity at 90 °C and at pH 9. It retained 63 % of its activity after 15 h at 85 °C. The enzyme also could tolerate (up to 10 % v/v) acetonitrile, ethanol and 2-propanol with slightly increased activities. Methanol, DMSO and acetone decreased activity slightly. Furthermore, Tm1743 exhibited broad substrate specificity towards various keto esters, ketones and aldehydes, with relative activities ranging from 2 to 460 % compared to the control. Its optimum substrate, 2,2,2-trifluoroacetophenone, was asymmetrically reduced in a coupled NADPH-regeneration system with an enantioselectivity of 99.8 % and a conversion of 98 %.</description><subject>acetone</subject><subject>Alcohol Oxidoreductases - chemistry</subject><subject>Alcohol Oxidoreductases - metabolism</subject><subject>Aldehyde Reductase</subject><subject>Aldehydes</subject><subject>Aldo-Keto Reductases</subject><subject>Applied Microbiology</subject><subject>Asymmetry</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>dimethyl sulfoxide</subject><subject>enantiomers</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Esters</subject><subject>Ethanol</subject><subject>Ethyl alcohol</subject><subject>gene overexpression</subject><subject>genes</subject><subject>isopropyl alcohol</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>methanol</subject><subject>Methyl alcohol</subject><subject>Microbiology</subject><subject>Original Research Paper</subject><subject>Reductases</subject><subject>Stereoisomerism</subject><subject>Substrate Specificity</subject><subject>Temperature</subject><subject>thermal stability</subject><subject>Thermotoga maritima</subject><subject>Thermotoga maritima - enzymology</subject><issn>0141-5492</issn><issn>1573-6776</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNks1u1DAUhS0EokPhAdiAl90EfP0bL9GIP6kSC9q15cTOxCUZD7ajqixQ34E35EnwkMKysLrSvd85i3MuQs-BvAJC1OsMRFDdEGANAIdGPkAbEIo1Uin5EG3IcSm4pifoSc5XhBCtiHqMTihjrFUENuj7drTJ9sWn8M2WEPc4DtjusZ1c_Hn744svESfvlr7Y7PGQ4owvRp_mWOLO4tmmUMJs8XUoIx7DbsTl9zUX24UplJvq5bDFXYrW4bx0uSRbPM4H35e0zE_Ro8FO2T-7m6fo8t3bi-2H5vzT-4_bN-dNz0VbGtBESuY6AKAD0eB555yUQjJhie75oLVuiXUanFet9VoOSnWSMt07MnSanaKz1feQ4tfF52LmkHs_TXbv45INSAVcEAbq3ygTlGrB2_9wZbzlNXIBFYUV7VPMOfnBHFINLt0YIOZYplnLNLVMcyzTyKp5cWe_dLN3fxV_2qsAXYFcT_udT-YqLmlfg7zX9eUqGmw0dpdCNpefaX2V-h5cKM7uJaiqKbFfPne-Dw</recordid><startdate>20130501</startdate><enddate>20130501</enddate><creator>Ma, Yuan-Hui</creator><creator>Lv, Dan-Qing</creator><creator>Zhou, Shuo</creator><creator>Lai, Dun-Yue</creator><creator>Chen, Zhen-Ming</creator><general>Springer-Verlag</general><general>Springer Netherlands</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7QL</scope><scope>7QO</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7TB</scope><scope>7U5</scope><scope>L7M</scope></search><sort><creationdate>20130501</creationdate><title>Characterization of an aldo–keto reductase from Thermotoga maritima with high thermostability and a broad substrate spectrum</title><author>Ma, Yuan-Hui ; Lv, Dan-Qing ; Zhou, Shuo ; Lai, Dun-Yue ; Chen, Zhen-Ming</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c458t-190663db1112f091e4bdd665635a09c4f99980ad91de78ae96f77b6239cd0fb93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>acetone</topic><topic>Alcohol Oxidoreductases - chemistry</topic><topic>Alcohol Oxidoreductases - metabolism</topic><topic>Aldehyde Reductase</topic><topic>Aldehydes</topic><topic>Aldo-Keto Reductases</topic><topic>Applied Microbiology</topic><topic>Asymmetry</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>dimethyl sulfoxide</topic><topic>enantiomers</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Esters</topic><topic>Ethanol</topic><topic>Ethyl alcohol</topic><topic>gene overexpression</topic><topic>genes</topic><topic>isopropyl alcohol</topic><topic>Kinetics</topic><topic>Life Sciences</topic><topic>methanol</topic><topic>Methyl alcohol</topic><topic>Microbiology</topic><topic>Original Research Paper</topic><topic>Reductases</topic><topic>Stereoisomerism</topic><topic>Substrate Specificity</topic><topic>Temperature</topic><topic>thermal stability</topic><topic>Thermotoga maritima</topic><topic>Thermotoga maritima - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ma, Yuan-Hui</creatorcontrib><creatorcontrib>Lv, Dan-Qing</creatorcontrib><creatorcontrib>Zhou, Shuo</creatorcontrib><creatorcontrib>Lai, Dun-Yue</creatorcontrib><creatorcontrib>Chen, Zhen-Ming</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Biotechnology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ma, Yuan-Hui</au><au>Lv, Dan-Qing</au><au>Zhou, Shuo</au><au>Lai, Dun-Yue</au><au>Chen, Zhen-Ming</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of an aldo–keto reductase from Thermotoga maritima with high thermostability and a broad substrate spectrum</atitle><jtitle>Biotechnology letters</jtitle><stitle>Biotechnol Lett</stitle><addtitle>Biotechnol Lett</addtitle><date>2013-05-01</date><risdate>2013</risdate><volume>35</volume><issue>5</issue><spage>757</spage><epage>762</epage><pages>757-762</pages><issn>0141-5492</issn><eissn>1573-6776</eissn><abstract>A novel aldo–keto reductase gene, Tm1743, from Thermotoga maritima was overexpressed in Escherichia coli. The enzyme displayed the highest activity at 90 °C and at pH 9. It retained 63 % of its activity after 15 h at 85 °C. The enzyme also could tolerate (up to 10 % v/v) acetonitrile, ethanol and 2-propanol with slightly increased activities. Methanol, DMSO and acetone decreased activity slightly. Furthermore, Tm1743 exhibited broad substrate specificity towards various keto esters, ketones and aldehydes, with relative activities ranging from 2 to 460 % compared to the control. Its optimum substrate, 2,2,2-trifluoroacetophenone, was asymmetrically reduced in a coupled NADPH-regeneration system with an enantioselectivity of 99.8 % and a conversion of 98 %.</abstract><cop>Dordrecht</cop><pub>Springer-Verlag</pub><pmid>23338701</pmid><doi>10.1007/s10529-013-1141-6</doi><tpages>6</tpages></addata></record> |
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| ispartof | Biotechnology letters, 2013-05, Vol.35 (5), p.757-762 |
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| subjects | acetone Alcohol Oxidoreductases - chemistry Alcohol Oxidoreductases - metabolism Aldehyde Reductase Aldehydes Aldo-Keto Reductases Applied Microbiology Asymmetry Biochemistry Biomedical and Life Sciences Biotechnology dimethyl sulfoxide enantiomers Enzyme Stability Enzymes Escherichia coli Esters Ethanol Ethyl alcohol gene overexpression genes isopropyl alcohol Kinetics Life Sciences methanol Methyl alcohol Microbiology Original Research Paper Reductases Stereoisomerism Substrate Specificity Temperature thermal stability Thermotoga maritima Thermotoga maritima - enzymology |
| title | Characterization of an aldo–keto reductase from Thermotoga maritima with high thermostability and a broad substrate spectrum |
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