TABLE 3.
Purification of recombinant alcohol dehydrogenase from E. coli JM109(pUCalrA)a
| Purification step | Total activity (U) | Sp act (U · mg−1) | Total protein (mg) | Purification (fold) | Yield (%) |
|---|---|---|---|---|---|
| Cell extract | 250,000 | 190 | 1,400 | 1 | 100 |
| Ultracentrifugation supernatant | 270,000 | 170 | 1,600 | 0.91 | 110 |
| Butyl-Toyopearl | 97,000 | 410 | 230 | 2.2 | 39 |
| Heat precipitation | 47,000 | 1,700 | 30 | 9.1 | 19 |
a
Heat precipitation was perfomed at 65°C for 15 min, and the enzyme was recovered from the centrifugation supernatant. Other purification procedures and the enzyme activity assay were the same as those used for the original strain.