TABLE 1.
Substrate saturation kinetic parameters of CsBGlu12
The parameters were studied in reaction mixture containing different concentrations of the substrates (1.95–500 μm). Kcat was calculated assuming the molecular mass of the recombinant CsBGlu12 subunit was 57 kDa. All values are the means ± S.D. of three separate preparations of the recombinant enzyme. No detectable activity was observed for coumarin, phenyethanoid, and apocarotenoid glucosides.
| Substrate | Km | Kcat | Kcat/Km |
|---|---|---|---|
| μm | s−1 | s−1mm−1 | |
| Cellobiose | 46.44 ± 4.60 | 0.83 ± 0.02 | 17.90 ± 0.3 |
| Cellotriose | 61.42 ± 3.30 | 0.80 ± 0.03 | 13.02 ± 0.3 |
| Cellotetraose | 62.25 ± 1.78 | 0.78 ± 0.02 | 12.53 ± 0.2 |
| Cellopentose | 74.81 ± 3.81 | 0.78 ± 0.03 | 10.42 ± 0.3 |
| Kaempferol 3-O-β-glucoside | 39.22 ± 3.27 | 0.71 ± 0.02 | 18.10 ± 0.2 |
| Quercetin 3-O-β-glucoside | 54.16 ± 4.21 | 0.92 ± 0.02 | 17.00 ± 0.2 |
| Naringenin 7-O-β-glucoside | 60.21 ± 3.26 | 1.05 ± 0.06 | 17.40 ± 1.6 |
| Iridin | 72.80 ± 4.97 | 1.29 ± 0.05 | 7.70 ± 0.3 |
| 1-O-Sinopyl-β-d-glucose | 132.4 ± 3.60 | 1.46 ± 0.04 | 2.56 ± 0.1 |