EC Number   |
Reference |
|---|
   1.10.3.2 | incubation of apo-CueO with excess CuSO4 (10 equiv) in Mops buffer (pH 7) in the presence of GSH (1 mM) at 4°C leads to incorporation of copper ions |
763183 |
| 1.10.3.2 | purification and recovery of immobilized and extractable transgenic enzyme, treatment with copper for activation of apoenzyme and as purification step |
654306 |
| 1.10.3.2 | reconstitution of Cu-depleted enzyme |
396348, 396376, 396381 |
| 1.10.3.2 | the enzyme is denatured in the presence of a number of denaturing agents (EDTA, DTT and GdnHCl) and refolded back to functional state with copper. In the folding experiments under alkaline conditions, zinc can replace copper in restoring 100% of laccase activity |
685393 |
| 1.10.3.2 | the isolated enzyme does not exhibit any enzymatic activity and lacks the blue colour typical of multicopper oxidase. Supplementation of purified CueO with CuSO4 activates the enzyme and renders it blue |
763449 |
| 1.10.3.2 | unfolding of the purified laccase, chemical reagents like 1-100 mM EDTA, 50-200 mM DTT and 1-6 M guanidinium hydrochloride, 100% activity is regained with 1 mM copper at pH 8.0 or by 1 mM Zn2+ at pH 5.5 |
685393 |
