Table 3.
Purification table of Acinetobacter sp. AU07 lipase.
| Step | Total protein (mg) | Total activity (U) | Specific activity (U/mg) | Yield (%) | Purification (fold) |
|---|---|---|---|---|---|
| Supernatant | 8.57 | 331.16 | 38.64 | 100 | 1 |
| Ammonium sulphate | 4.30 | 232.09 | 53.96 | 70.10 | 1.4 |
| Ion-exchange chromatography | 1.43 | 119.36 | 83.47 | 36.04 | 2.2 |
A two-step purification of the lipase by ammonium sulfate (60% saturation) and ion exchange chromatography (0.1–1 M NaCl elution). The assay was performed by incubating the enzyme at 30 °C for 10 min with 1 mM 4-NP as the substrate. The protein concentration was estimated by the standard Bradford assay procedure. Each value is the average of three replicates.