TABLE 1.
Purification of laccase 1 activity from M. quercophilus
| Step | Vol (ml) | Protein (mg) | Total activity (U) | Sp act (U/mg) | Yield (%) | Purification (fold) |
|---|---|---|---|---|---|---|
| Supernatant | 2,000 | 144.0 | 800 | 5.6 | 100 | |
| Ultrafiltration | 50 | 106.2 | 718 | 6.9 | 90 | 1.2 |
| Q-Sepharosea | 26 | 39.0 | 401 | 10.3 | 50 | 1.9 |
| Sephacryl S-200 | 20 | 26.0 | 289 | 11.1 | 36 | 2.0 |
| Chelating Sepharose (Cu)b | 20 | 18.8 | 245 | 13.0 | 31 | 2.4 |
a
About 60% of the laccase activity eluted as a single peak early in the gradient (within 20 min at 170 mM NaCl), while 10% eluted as two peaks late in the gradient (350 mM NaCl). The fractions corresponding to the first peak were pooled and further purified.
b
Laccase 1 eluted as a single peak in the fractions corresponding to 0.4 to 0.6 M ammonium sulfate.