Enhancing photosynthetic production of glycogen-rich biomass for use as a fermentation feedstock.

Autor: Comer AD; Department of Chemical and Biological Engineering, University of Wisconsin-Madison, Madison, WI 53706, United States., Abraham JP; Department of Chemical and Biological Engineering, University of Wisconsin-Madison, Madison, WI 53706, United States., Steiner AJ; Department of Chemical and Biological Engineering, University of Wisconsin-Madison, Madison, WI 53706, United States., Korosh TC; Department of Chemical and Biological Engineering, University of Wisconsin-Madison, Madison, WI 53706, United States., Markley AL; Department of Chemical and Biological Engineering, University of Wisconsin-Madison, Madison, WI 53706, United States., Pfleger BF; Department of Chemical and Biological Engineering, University of Wisconsin-Madison, Madison, WI 53706, United States.; Microbiology Doctoral Training Program, University of Wisconsin-Madison, Madison, WI 53706, United States.
Jazyk: angličtina
Zdroj: Frontiers in energy research [Front Energy Res] 2020 May; Vol. 8. Date of Electronic Publication: 2020 May 29.
DOI: 10.3389/fenrg.2020.00093
Abstrakt: Current sources of fermentation feedstocks, i.e. corn, sugar cane, or plant biomass, fall short of demand for liquid transportation fuels and commodity chemicals in the United States. Aquatic phototrophs including cyanobacteria have the potential to supplement the supply of current fermentable feedstocks. In this strategy, cells are engineered to accumulate storage molecules including glycogen, cellulose, and/or lipid oils that can be extracted from harvested biomass and fed to heterotrophic organisms engineered to produce desired chemical products. In this manuscript, we examine the production of glycogen in the model cyanobacteria, Synechococcus sp . strain PCC 7002, and subsequent conversion of cyanobacterial biomass by an engineered Escherichia coli to octanoic acid as a model product. In effort to maximize glycogen production, we explored the deletion of catabolic enzymes and overexpression of GlgC, an enzyme that catalyzes the first committed step towards glycogen synthesis. We found that deletion of glgP increased final glycogen titers when cells were grown in diurnal light. Overexpression of GlgC led to a temporal increase in glycogen content but not in an overall increase in final titer or content. The best strains were grown, harvested, and used to formulate media for growth of E. coli . The cyanobacterial media was able to support the growth of an engineered E. coli and produce octanoic acid at the same titer as common laboratory media.
Databáze: MEDLINE