| 초록 |
Hexanoic acid and its derivatives can be utilized in various industrial applications such as perfumes and food additives. Production of hexanoic acid often relies on petroleum, but the increase and instability of its price have made the production through bioprocesses more attractive. Although several natural bacteria, such as Clostridium sp. or Megasphaera sp., are known to produce it, limited cellular information and genetic engineering tools make it difficult to re-design those biological systems. In this study, Escherichia coli was engineered to optimize the hexanoic acid production by precise flux rebalancing between acetyl-CoA and butyryl-CoA. First, E. coli native thioesterase (TesB) was replaced with acetyl-CoA transferase (ACT) from Megasphaera sp. MH, and the titer was increased by 1.47-fold. Next, flux rebalancing was carried out by tuning E. coli acetyl-CoA acetyltransferase (AtoB), and the titer in the strain with optimal atoB expression level was increased by 8.7-fold compared to parental strain. Our results demonstrate that ACT from Megasphaera sp. MH is proper enzyme for hexanoic acid synthesis, and atoB should be fine-tuned to increase hexanoic acid production. |
