From the University of Minnesota:
MINNEAPOLIS / ST. PAUL (03/23/2011) —University of Minnesota researchers are a key step closer to making renewable petroleum fuels using bacteria, sunlight and carbon dioxide, a goal funded by a $2.2 million United States Department of Energy grant.
Graduate student Janice Frias, who earned her doctorate in January, made the critical step by figuring out how to use a protein to transform fatty acids produced by the bacteria into ketones, which can be cracked to make hydrocarbon fuels. The university is filing patents on the process.
The research is published in the April 1 issue of the Journal of Biological Chemistry. Frias, whose advisor was Larry Wackett, Distinguished McKnight Professor of Biochemistry, is lead author. Other team members include organic chemist Jack Richman, a researcher in the College of Biological Sciences’ Department of Biochemistry, Molecular Biology and Biophysics, and undergraduate Jasmine Erickson, a junior in the College of Biological Sciences. Wackett, who is senior author, is a faculty member in the College of Biological Sciences and the university’s BioTechnology Institute.
“Janice Frias is a very capable and hard-working young scientist,” Wackett says. “She exemplifies the valuable role graduate students play at a public research university.”
Aditya Bhan and Lanny Schmidt, chemical engineering professors in the College of Science and Engineering, are turning the ketones into diesel fuel using catalytic technology they have developed. The ability to produce ketones opens the door to making petroleum-like hydrocarbon fuels using only bacteria, sunlight and carbon dioxide.
“There is enormous interest in using carbon dioxide to make hydrocarbon fuels,” Wackett says. “CO2 is the major greenhouse gas mediating global climate change, so removing it from the atmosphere is good for the environment. It’s also free. And we can use the same infrastructure to process and transport this new hydrocarbon fuel that we use for fossil fuels.”
The research is funded by a $2.2 million grant from the U.S. Department of Energy’s Advanced Research Projects Agency-energy (ARPA-e) program, created to stimulate American leadership in renewable energy technology.
The U of M proposal was one of only 37 selected from 3,700 and one of only three featured in the New York Times when the grants were announced in October 2009. The University of Minnesota’s Initiative for Renewable Energy and the Environment (IREE) and the College of Biological Sciences also provided funding.
Wackett is principal investigator for the ARPA-e grant. His team of co-investigators includes Jeffrey Gralnick, assistant professor of microbiology and Marc von Keitz, chief technical officer of BioCee, as well as Bhan and Schmidt. They are the only group using a photosynthetic bacterium and a hydrocarbon-producing bacterium together to make hydrocarbons from carbon dioxide.
The U of M team is using Synechococcus, a bacterium that fixes carbon dioxide in sunlight and converts CO2 to sugars. Next, they feed the sugars to Shewanella, a bacterium that produces hydrocarbons. This turns CO2, a greenhouse gas produced by combustion of fossil fuel petroleum, into hydrocarbons.
Hydrocarbons (made from carbon and hydrogen) are the main component of fossil fuels. It took hundreds of millions of years of heat and compression to produce fossil fuels, which experts expect to be largely depleted within 50 years.
In press at the Journal of Biological Chemistry
Purification and Characterization of OleA from Xanthomonas campestris and Demonstration of a Non-decarboxylative Claisen Condensation Reaction*
+ Author Affiliations
From the Department of Biochemistry, Molecular Biology, and Biophysics and BioTechnology Institute, University of Minnesota, St. Paul, Minnesota 55108
OleA catalyzes the condensation of fatty acyl groups in the first step of bacterial long-chain olefin biosynthesis, but the mechanism of the condensation reaction is controversial. In this study, OleA from Xanthomonas campestris was expressed in Escherichia coli and purified to homogeneity. The purified protein was shown to be active with fatty acyl-CoA substrates that ranged from C8 to C16 in length. With limiting myristoyl-CoA (C14), 1 mol of the free coenzyme A was released/mol of myristoyl-CoA consumed. Using [14C]myristoyl-CoA, the other products were identified as myristic acid, 2-myristoylmyristic acid, and 14-heptacosanone. 2-Myristoylmyristic acid was indicated to be the physiologically relevant product of OleA in several ways. First, 2-myristoylmyristic acid was the major condensed product in short incubations, but over time, it decreased with the concomitant increase of 14-heptacosanone. Second, synthetic 2-myristoylmyristic acid showed similar decarboxylation kinetics in the absence of OleA. Third, 2-myristoylmyristic acid was shown to be reactive with purified OleC and OleD to generate the olefin 14-heptacosene, a product seen in previous in vivo studies. The decarboxylation product, 14-heptacosanone, did not react with OleC and OleD to produce any demonstrable product. Substantial hydrolysis of fatty acyl-CoA substrates to the corresponding fatty acids was observed, but it is currently unclear if this occurs in vivo. In total, these data are consistent with OleA catalyzing a non-decarboxylative Claisen condensation reaction in the first step of the olefin biosynthetic pathway previously found to be present in at least 70 different bacterial strains.
h/t to WUWT reader JPE for the starting point link to Science Daily in Tips and Notes