TABLE 3.
Simplified in vitro refolding of denatured mature lipase
| Chaperone | U/mg of lipasea:
|
|
|---|---|---|
| Native chaperone | Denatured | |
| Δ70HpHis | 4,850 | 4,660 |
| Δ34HpHis | 670 | 2,280 |
| ompAΔ70HpHis | 1,040 | 4,170 |
| ompAΔ34HpHis/ompAΔ34HpHisb | 1,730 | 3,580 |
| ompAΔ34HpHisc | ND | 0 |
a
Specific activity is given as units per milligram of lipase used for refolding. ND, not determined. The inactive lipase was purified from 2 g of wet cells. The amount of the crude chaperone added to the refolding mixture was five to six times higher than that of the crude lipase.
b
Cell extract from E. coli pT-ompAΔ34HpHis in which 50% of the expressed ompAΔ34HpHis is not processed and is insoluble. Hence, only ompAΔ34HpHis is present in the cell extract after sonification (native chaperone).
c
Isolated from inclusion bodies produced by E. coli pT-ompAΔ34HpHis.