| 초록 |
Twin arginine translocation (Tat) pathway has advantage of secreting protein in periplasm after it is folded in cytoplasm. When organophosphorus hydrolase (OPH) is expressed with Tat signal sequence in Escherichia coli, inclusion body in cytoplasm is a dominant form. Therefore, whole cell activity is relatively low. In the present work, we investigated a strategy for overcoming this problem in a whole cell system by enforcing periplasmic secretion of OPH through chaperone co-expression. We co-expressed molecular chaperone including GroEL/ES with OPH. We found significant increase of OPH in a soluble form compared to that without chaperone and this might be due to increased protein folding. Furthermore, whole cell OPH activity of chaperone co-expressing cells was about 20 times greater than that of non-expressing cells. Chaperone may successfully assist in enhancement of whole cell OPH activity. |
