| 초록 |
Organophosphorus hydrolase (OPH) from Pseudomonas diminuta or Flavobacterium sp. is a homodimeric organophosphotriesterase that can degrade a broad spectrum of toxic organophosphates. The application of OPH for bioremediation is of great interest because of its high turnover rate. Recombinant Escherichia coli expressing OPH can degrade a variety of organophosphates. The ability of E. coli to grow into much higher cell densities than P. diminuta and Flavobacterium enables the development of large-scale detoxification processes. However, the whole cell biocatalyst expressing intracellular OPH has has a low production yield of OPH due to its very low solubility and mass transport limitations of substrates and products because the cell membrane acts as a diffusion barrier. Therefore, several strategies have been attempted to enhance OPH production yield or bioconversion efficiency such as insertion of multiple gene fusions, fusion with a soluble partner to increase solubility, and display on cell surface. In this research, we tried to direct OPH into Escherichia coli periplasmic space using the pelB signal sequence well known for potential periplasmic localization. |
