| 초록 |
The recombinant proteins have been synthesized inside the prokaryotic cells like Escherichia coli and extracted by breaking the cells. However, constructing a system which can secrete the recombinant proteins is far more efficient than breaking the cells. Pseudomonas fluorescens is an efficient platform for the secretory production of recombinant proteins. P. fluorescens has an ABC transporter secreting endogenous thermostable lipase (TliA) and protease, which can be exploited to transport recombinant proteins across the cell membrane. Various proteins have been tested for their secretion. The criteria of well-secreted and non-secreted proteins were protein isoelectric point (pI) value with negative charged proteins preferred for secretion. The ABC transporter system will provide greater convenience for the secretory production and purification of recombinant proteins in Gram-negative bacteria, such as E. coli and Pseudomonas species. |
