Direct photosynthetic recycling of carbon dioxide to isobutyraldehyde
Top Cited Papers
- 15 November 2009
- journal article
- research article
- Published by Springer Nature in Nature Biotechnology
- Vol. 27 (12), 1177-1180
- https://doi.org/10.1038/nbt.1586
Abstract
The feasibility of recycling CO2 to biofuels in photosynthetic organisms will depend on advances in productivity and product-purification efficiency. Atsumi et al. improve the direct conversion of CO2 by engineering Synechococcus elongatus to produce isobutyraldehyde, which can be easily recovered from the production medium. Global climate change has stimulated efforts to reduce CO2 emissions. One approach to addressing this problem is to recycle CO2 directly into fuels or chemicals using photosynthesis. Here we genetically engineered Synechococcus elongatus PCC7942 to produce isobutyraldehyde and isobutanol directly from CO2 and increased productivity by overexpression of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco). Isobutyraldehyde is a precursor for the synthesis of other chemicals, and isobutanol can be used as a gasoline substitute. The high vapor pressure of isobutyraldehyde allows in situ product recovery and reduces product toxicity. The engineered strain remained active for 8 d and produced isobutyraldehyde at a higher rate than those reported for ethanol1, hydrogen2 or lipid3 production by cyanobacteria or algae. These results underscore the promise of direct bioconversion of CO2 into fuels and chemicals, which bypasses the need for deconstruction of biomass.Keywords
This publication has 39 references indexed in Scilit:
- Engineering the isobutanol biosynthetic pathway in Escherichia coli by comparison of three aldehyde reductase/alcohol dehydrogenase genesApplied Microbiology and Biotechnology, 2009
- Biodiesel from microalgae beats bioethanolTrends in Biotechnology, 2008
- Increased Rubisco Content in Transgenic Rice Transformed with the ‘Sense’ rbcS GenePlant and Cell Physiology, 2007
- Development of the bacterial photosynthetic apparatusCurrent Opinion in Microbiology, 2006
- Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimizedProceedings of the National Academy of Sciences, 2006
- High-Throughput Screen for Poly-3-Hydroxybutyrate in Escherichia coli and Synechocystis sp. Strain PCC6803Applied and Environmental Microbiology, 2006
- Biochemical and molecular characterization of α-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids by Lactococcus lactisFEMS Microbiology Letters, 2004
- Biochemical and molecular characterization of α-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids byLactococcus lactisFEMS Microbiology Letters, 2004
- Crystal Structure of E.coli Alcohol Dehydrogenase YqhD: Evidence of a Covalently Modified NADP CoenzymeJournal of Molecular Biology, 2004
- Positive and Negative Selection of Mutant Forms of Prokaryotic (Cyanobacterial) Ribulose-1,5-bisphosphate Carboxylase/OxygenaseJournal of Molecular Biology, 2003