TABLE 1.
Purification of oxygenase variantsa
Enzyme | Purification step | Total protein (mg) | Total activity (U) | Sp act (U/mg) | Yield (%) |
---|---|---|---|---|---|
BphAELB400 | Crude extract | 1,069 | 32 | 0.03 (0.01) | 100 |
Source Q | 72 | 7 | 0.10 (0.02) | 22 | |
Phenyl-Sepharose | 15 | 3 | 0.22 (0.03) | 9 | |
BphAEB356 | Crude extract | 1,200 | 600 | 0.5 (0.1) | 100 |
Source Q | 153 | 230 | 1.5 (0.5) | 38 | |
Phenyl-Sepharose | 41 | 164 | 4.0 (0.3) | 27 | |
BphAEII9 | Crude extract | 2,196 | 198 | 0.09 (0.03) | 100 |
Source Q | 105 | 32 | 0.3 (0.1) | 16 | |
Phenyl-Sepharose | 41 | 25 | 0.6 (0.1) | 13 | |
BphAEII10 | Crude extract | 1,314 | 40 | 0.03 (0.02) | 100 |
Source Q | 174 | 17 | 0.12 (0.03) | 43 | |
Phenyl-Sepharose | 28 | 8 | 0.30 (0.02) | 20 |
One unit of enzyme activity is defined as the amount of enzyme required to consume 1 μmol of O2/min. Standard deviations (n = 4) are indicated in parentheses.