Table 1.
Substrate specificity of Op5Man5.
| Substrate | Specific activity (U⋅mg−1)a | Relative activity (%)b |
|---|---|---|
| Aryl glycosidesc,d | ||
| pNP-βMan | 92 ± 10.4 | 100 |
| pNP-αMan | ND | ND |
| pNPβ-Xyl | ND | ND |
| pNP-βFuc | ND | ND |
| pNP-αFuc | ND | ND |
| pNP-βGal | ND | ND |
| pNP-βGlc | ND | ND |
| pNP-βCel | ND | ND |
| Mannooligosaccharidesc,d | ||
| M2 | 1.3 ± 0.2 | 50 |
| M3 | 1.4 ± 0.2 | 53 |
| M4 | 1.7 ± 0.3 | 67 |
| M5 | 2.2 ± 0.1 | 85 |
| M6 | 2.6 ± 0.2 | 100 |
| Polysaccharidesc,d | ||
| Ivory nut mannan | 0.29 ± 0.07 | 100 |
| Konjac glucomannan | 0.18 ± 0.02 | 63 |
| Galactomannan | ND | ND |
| LGB | ND | ND |
| Xylan | ND | ND |
| Barley β-glucans | ND | ND |
| CMC | ND | ND |
a
The specific activity on aryl glycosides is expressed as the amount of enzyme (in mg) releasing 1 μmol⋅min−1 pNP. The specific activity on mannooligo- and polysaccharides was measured using the GOD-POD assay and is expressed as the amount of enzyme (in mg) releasing 1 μmol⋅min−1 glucose.
b
The relative activity was calculated from the specific activity of each substrate with the most preferred substrate set to 100%.
c
Errors of experimental data are represented as mean ± standard deviation from triplicate experiments.
d
ND, not detected