Fatty aldehydes in cyanobacteria are a metabolically flexible precursor for a diversity of biofuel products
We describe how pathway engineering can be used to convert a single intermediate derived from lipid biosynthesis, fatty aldehydes, into a variety of biofuel precursors including alkanes, free fatty acids and wax esters. In cyanobacteria, long-chain acyl-ACPs can be reduced to fatty aldehydes, and th...
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| Veröffentlicht in: | PloS one 2013-03, Vol.8 (3), p.e58307-e58307 |
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| creator | Kaiser, Brett K Carleton, Michael Hickman, Jason W Miller, Cameron Lawson, David Budde, Mark Warrener, Paul Paredes, Angel Mullapudi, Srinivas Navarro, Patricia Cross, Fred Roberts, James M |
| description | We describe how pathway engineering can be used to convert a single intermediate derived from lipid biosynthesis, fatty aldehydes, into a variety of biofuel precursors including alkanes, free fatty acids and wax esters. In cyanobacteria, long-chain acyl-ACPs can be reduced to fatty aldehydes, and then decarbonylated to alkanes. We discovered a cyanobacteria class-3 aldehyde-dehydrogenase, AldE, that was necessary and sufficient to instead oxidize fatty aldehyde precursors into fatty acids. Overexpression of enzymes in this pathway resulted in production of 50 to 100 fold more fatty acids than alkanes, and the fatty acids were secreted from the cell. Co-expression of acyl-ACP reductase, an alcohol-dehydrogenase and a wax-ester-synthase resulted in a third fate for fatty aldehydes: conversion to wax esters, which accumulated as intracellular lipid bodies. Conversion of acyl-ACP to fatty acids using endogenous cyanobacterial enzymes may allow biofuel production without transgenesis. |
| doi_str_mv | 10.1371/journal.pone.0058307 |
| format | Article |
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In cyanobacteria, long-chain acyl-ACPs can be reduced to fatty aldehydes, and then decarbonylated to alkanes. We discovered a cyanobacteria class-3 aldehyde-dehydrogenase, AldE, that was necessary and sufficient to instead oxidize fatty aldehyde precursors into fatty acids. Overexpression of enzymes in this pathway resulted in production of 50 to 100 fold more fatty acids than alkanes, and the fatty acids were secreted from the cell. Co-expression of acyl-ACP reductase, an alcohol-dehydrogenase and a wax-ester-synthase resulted in a third fate for fatty aldehydes: conversion to wax esters, which accumulated as intracellular lipid bodies. Conversion of acyl-ACP to fatty acids using endogenous cyanobacterial enzymes may allow biofuel production without transgenesis.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0058307</identifier><identifier>PMID: 23505484</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Alcohol ; Alcohols ; Aldehyde Dehydrogenase - metabolism ; Aldehydes ; Aldehydes - metabolism ; Alkanes ; Arabidopsis thaliana ; Biodiesel fuels ; Biofuels ; Biology ; Biomass ; Biomass energy ; Biosynthesis ; Chromatography ; Conversion ; Cyanobacteria ; Cyanobacteria - genetics ; Cyanobacteria - metabolism ; Dehydrogenase ; Dehydrogenases ; E coli ; Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific) - genetics ; Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific) - metabolism ; Enzymes ; Esters ; Fatty acids ; Fatty Acids - biosynthesis ; Fatty Acids - metabolism ; Fuels ; Gene Expression ; Genes ; Genetic engineering ; Kinetics ; Laboratories ; Lipid bodies ; Lipid peroxidation ; Lipids ; Pathology ; Physiological aspects ; Precursors ; Reductase ; Synechococcus elongatus ; Synechocystis ; Waxes - metabolism</subject><ispartof>PloS one, 2013-03, Vol.8 (3), p.e58307-e58307</ispartof><rights>COPYRIGHT 2013 Public Library of Science</rights><rights>2013 Kaiser et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2013 Kaiser et al 2013 Kaiser et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c758t-a88fed83fc5fc940435ac4feeb552c504e7dd9b35f619d52b38f53a02e739c183</citedby><cites>FETCH-LOGICAL-c758t-a88fed83fc5fc940435ac4feeb552c504e7dd9b35f619d52b38f53a02e739c183</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3594298/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3594298/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79343,79344</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23505484$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kaiser, Brett K</creatorcontrib><creatorcontrib>Carleton, Michael</creatorcontrib><creatorcontrib>Hickman, Jason W</creatorcontrib><creatorcontrib>Miller, Cameron</creatorcontrib><creatorcontrib>Lawson, David</creatorcontrib><creatorcontrib>Budde, Mark</creatorcontrib><creatorcontrib>Warrener, Paul</creatorcontrib><creatorcontrib>Paredes, Angel</creatorcontrib><creatorcontrib>Mullapudi, Srinivas</creatorcontrib><creatorcontrib>Navarro, Patricia</creatorcontrib><creatorcontrib>Cross, Fred</creatorcontrib><creatorcontrib>Roberts, James M</creatorcontrib><title>Fatty aldehydes in cyanobacteria are a metabolically flexible precursor for a diversity of biofuel products</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>We describe how pathway engineering can be used to convert a single intermediate derived from lipid biosynthesis, fatty aldehydes, into a variety of biofuel precursors including alkanes, free fatty acids and wax esters. 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Conversion of acyl-ACP to fatty acids using endogenous cyanobacterial enzymes may allow biofuel production without transgenesis.</description><subject>Alcohol</subject><subject>Alcohols</subject><subject>Aldehyde Dehydrogenase - metabolism</subject><subject>Aldehydes</subject><subject>Aldehydes - metabolism</subject><subject>Alkanes</subject><subject>Arabidopsis thaliana</subject><subject>Biodiesel fuels</subject><subject>Biofuels</subject><subject>Biology</subject><subject>Biomass</subject><subject>Biomass energy</subject><subject>Biosynthesis</subject><subject>Chromatography</subject><subject>Conversion</subject><subject>Cyanobacteria</subject><subject>Cyanobacteria - genetics</subject><subject>Cyanobacteria - metabolism</subject><subject>Dehydrogenase</subject><subject>Dehydrogenases</subject><subject>E coli</subject><subject>Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific) - genetics</subject><subject>Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific) - metabolism</subject><subject>Enzymes</subject><subject>Esters</subject><subject>Fatty acids</subject><subject>Fatty Acids - biosynthesis</subject><subject>Fatty Acids - metabolism</subject><subject>Fuels</subject><subject>Gene Expression</subject><subject>Genes</subject><subject>Genetic engineering</subject><subject>Kinetics</subject><subject>Laboratories</subject><subject>Lipid bodies</subject><subject>Lipid peroxidation</subject><subject>Lipids</subject><subject>Pathology</subject><subject>Physiological aspects</subject><subject>Precursors</subject><subject>Reductase</subject><subject>Synechococcus elongatus</subject><subject>Synechocystis</subject><subject>Waxes - metabolism</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><sourceid>DOA</sourceid><recordid>eNqNk99r2zAQx83YWLtu_8HYDIOxPSSTLSuWXwalrFugUNivV3GWTok6xUoluTT__eTGLfHowxBC4vS5751Ouix7XZB5Qevi05XrfQd2vnUdzglhnJL6SXZcNLScLUpCnx7sj7IXIVwliPLF4nl2VFJGWMWr4-zPOcS4y8EqXO8Uhtx0udxB51qQEb2BHDzmkG8wQuuskWDtLtcWb01rMd96lL0Pzuc6TciVuUEfTFJ0Om-N0z3aBDnVyxheZs802ICvxvUk-3X-5efZt9nF5dfl2enFTNaMxxlwrlFxqiXTsqlIRRnISiO2jJWSkQprpZqWMr0oGsXKlnLNKJASa9rIgtOT7O1ed2tdEGOdgigoJbxh1R2x3BPKwZXYerMBvxMOjLgzOL8S4KORFoWiyCqtaoJNW9WguYayRV0DS4M2ddL6PEbr2w0qiV30YCei05POrMXK3QjKmqpshmQ-jALeXfcYotiYINFa6ND1Q95FzVlDWZHQd_-gj99upFaQLmA67VJcOYiK06rmtGQ1GfKeP0KloXBjZPpU2iT7xOHjxCExEW_jCvoQxPLH9_9nL39P2fcH7BrBxnVwto_GdWEKVntQeheCR_1Q5IKIoSfuqyGGnhBjTyS3N4cP9OB03wT0L0DFCPs</recordid><startdate>20130311</startdate><enddate>20130311</enddate><creator>Kaiser, Brett K</creator><creator>Carleton, Michael</creator><creator>Hickman, Jason W</creator><creator>Miller, Cameron</creator><creator>Lawson, David</creator><creator>Budde, Mark</creator><creator>Warrener, Paul</creator><creator>Paredes, Angel</creator><creator>Mullapudi, Srinivas</creator><creator>Navarro, Patricia</creator><creator>Cross, Fred</creator><creator>Roberts, James M</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20130311</creationdate><title>Fatty aldehydes in cyanobacteria are a metabolically flexible precursor for a diversity of biofuel products</title><author>Kaiser, Brett K ; Carleton, Michael ; Hickman, Jason W ; Miller, Cameron ; Lawson, David ; Budde, Mark ; Warrener, Paul ; Paredes, Angel ; Mullapudi, Srinivas ; Navarro, Patricia ; Cross, Fred ; Roberts, James M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c758t-a88fed83fc5fc940435ac4feeb552c504e7dd9b35f619d52b38f53a02e739c183</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Alcohol</topic><topic>Alcohols</topic><topic>Aldehyde Dehydrogenase - 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In cyanobacteria, long-chain acyl-ACPs can be reduced to fatty aldehydes, and then decarbonylated to alkanes. We discovered a cyanobacteria class-3 aldehyde-dehydrogenase, AldE, that was necessary and sufficient to instead oxidize fatty aldehyde precursors into fatty acids. Overexpression of enzymes in this pathway resulted in production of 50 to 100 fold more fatty acids than alkanes, and the fatty acids were secreted from the cell. Co-expression of acyl-ACP reductase, an alcohol-dehydrogenase and a wax-ester-synthase resulted in a third fate for fatty aldehydes: conversion to wax esters, which accumulated as intracellular lipid bodies. Conversion of acyl-ACP to fatty acids using endogenous cyanobacterial enzymes may allow biofuel production without transgenesis.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>23505484</pmid><doi>10.1371/journal.pone.0058307</doi><tpages>e58307</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Alcohol Alcohols Aldehyde Dehydrogenase - metabolism Aldehydes Aldehydes - metabolism Alkanes Arabidopsis thaliana Biodiesel fuels Biofuels Biology Biomass Biomass energy Biosynthesis Chromatography Conversion Cyanobacteria Cyanobacteria - genetics Cyanobacteria - metabolism Dehydrogenase Dehydrogenases E coli Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific) - genetics Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific) - metabolism Enzymes Esters Fatty acids Fatty Acids - biosynthesis Fatty Acids - metabolism Fuels Gene Expression Genes Genetic engineering Kinetics Laboratories Lipid bodies Lipid peroxidation Lipids Pathology Physiological aspects Precursors Reductase Synechococcus elongatus Synechocystis Waxes - metabolism |
| title | Fatty aldehydes in cyanobacteria are a metabolically flexible precursor for a diversity of biofuel products |
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