Development of an orthogonal fatty acid biosynthesis system in E. coli for oleochemical production |
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| Institution: | 1. Joint BioEnergy Institute, 5885 Hollis Street, 4th Floor, Emeryville, CA 94608, United States;2. Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, United States;3. Joint Genome Institute, Walnut Creek, CA 94598, United States;4. QB3 Institute, University of California-Berkeley, 5885 Hollis Street, 4th Floor, Emeryville, CA 94608, United States;5. Synthetic Biology Engineering Research Center, University of California, Berkeley, CA 94720, United States;6. Department of Chemical & Biomolecular Engineering, Department of Bioengineering, University of California, Berkeley, CA 94720, United States;1. Bredesen Center for Interdisciplinary Research and Graduate Education, The University of Tennessee, Knoxville and Oak Ridge National Laboratory, Oak Ridge, TN, USA;2. BioEnergy Science Center, Oak Ridge National Laboratory, Oak Ridge, TN, USA;3. Department of Chemical and Biomolecular Engineering, The University of Tennessee, Knoxville, TN, USA;4. Biosciecnes Division, Oak Ridge National Laboratory, Oak Ridge, TN, USA;5. Thayer School of Engineering, Dartmouth College, Hanover, NH, USA;1. Department of Chemical and Biomolecular Engineering, United States;2. UTK-ORNL Joint Institute of Biological Science, United States;3. Bredesen Center for Interdisciplinary Research and Graduate Education, United States;4. Institute of Biomedical Engineering, The University of Tennessee, Knoxville, TN, United States;5. BioEnergy Science Center, Oak Ridge National Laboratory, Oak Ridge, TN, USA;1. Department of Genetic Engineering, College of Biotechnology and Bioengineering, Sungkyunkwan University, Suwon 440-746, Republic of Korea;2. School of Interdisciplinary Bioscience and Bioengineering, Pohang University of Science and Technology, Pohang 790-784, Republic of Korea;3. Department of Chemical Engineering, Pohang University of Science and Technology, Pohang 790-784, Republic of Korea;4. Department of Agricultural Biotechnology and Center for Agricultural Biomaterials, Seoul National University, Seoul 151-921, Republic of Korea;5. Bio R&D Center, Samsung Advanced Institute of Technology, Yongin 446-712, Republic of Korea;6. Department of Food Science and Engineering, Ewha Womans University, Seoul 120-750, Republic of Korea;7. Department of Bioengineering and Technology, College of Engineering, Kangwon National University, Chuncheon 220-701, Republic of Korea;1. Department of Chemical and Biological Engineering, University of Wisconsin-Madison, Madison, WI, 53706, United States;2. Microbiology Doctoral Training Program, University of Wisconsin-Madison, Madison, WI, 53706, United States;3. DOE Great Lakes Bioenergy Research Center, University of Wisconsin–Madison, Madison, WI, 53706, USA;1. Synthetic Biology and Biofuels Group, International Centre for Genetic Engineering and Biotechnology, New Delhi, India;2. DBT-ICGEB Centre for Advanced Bioenergy Research, International Centre for Genetic Engineering and Biotechnology, New Delhi, India |
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| Abstract: | Here we report recombinant expression and activity of several type I fatty acid synthases that can function in parallel with the native Escherichia coli fatty acid synthase. Corynebacterium glutamicum FAS1A was the most active in E. coli and this fatty acid synthase was leveraged to produce oleochemicals including fatty alcohols and methyl ketones. Coexpression of FAS1A with the ACP/CoA-reductase Maqu2220 from Marinobacter aquaeolei shifted the chain length distribution of fatty alcohols produced. Coexpression of FAS1A with FadM, FadB, and an acyl-CoA-oxidase from Micrococcus luteus resulted in the production of methyl ketones, although at a lower level than cells using the native FAS. This work, to our knowledge, is the first example of in vivo function of a heterologous fatty acid synthase in E. coli. Using FAS1 enzymes for oleochemical production have several potential advantages, and further optimization of this system could lead to strains with more efficient conversion to desired products. Finally, functional expression of these large enzyme complexes in E. coli will enable their study without culturing the native organisms. |
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| Keywords: | Fatty alcohols Methyl ketones Fatty acid synthase Synthetic biology |
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