TABLE 2.
Purification of veratryl alcohol-oxidizing peroxidases from Coprinus radians DSMZ 888a
| Purification step | Total activity | Total amt of protein (mg) | Sp act (U mg−1) | Yield (%) | Purification (fold) |
|---|---|---|---|---|---|
| Culture liquid | 627 | 752.4 | 0.83 | 100 | 1.0 |
| First ultrafiltration step (10 kDa) | 613 | 691.5 | 0.89 | 97.8 | 1.1 |
| Second ultrafiltration step (10 kDa) | 547 | 316.2 | 1.73 | 87.2 | 2.1 |
| Q Sepharose FF fraction I | 143 | 25.0 | 5.7 | 22.8 | 6.9 |
| Q Sepharose FF fraction II | 341 | 18.2 | 18.7 | 54.4 | 22.5 |
| Mono Q CrP I | 40 | 1.6 | 25.1 | 6.4 | 30.1 |
| Mono Q CrP II | 150 | 7.2 | 20.6 | 23.9 | 24.8 |
| Mono Q CrP III | 100 | 3.3 | 30.5 | 15.9 | 36.6 |
| SEC CrP I | 27 | 0.9 | 31.5 | 4.3 | 37.8 |
| SEC CrP II | 60 | 2.0 | 30.6 | 9.6 | 36.7 |
| SEC CrP III | 21 | 0.55 | 38.5 | 3.3 | 46.2 |
a
Enzyme activities are based on the oxidation of veratryl alcohol to veratraldehyde at pH 7 (according to the method described in reference 41).