Table 2.
Effect of metal ions, reducing agents, and ionic and nonionic surfactants on XynAMG1 xylanase activity.
| Agent | 2 mM | 10 mM |
|---|---|---|
| None | 100 ± 0.2 | 100 ± 0.2 |
| Mg2+ | 96.8 ± 0.9 | 92.4 ± 0.7 |
| Ca2+ | 91.4 ± 3.1 | 77.3 ± 2.9 |
| Mn2+ | 99.9 ± 2.5 | 97.3 ± 3.7 |
| Co2+ | 98.5 ± 2.9 | 94.2 ± 2.2 |
| Cu2+ | 86.3 ± 2.2 | 41.4 ± 1.9 |
| Zn2+ | 98.8 ± 0.9 | 95.5 ± 1.4 |
| β-Mercaptoethanol | 95.3 ± 1.0 | 93.6 ± 1.1 |
| DTT | 95.0 ± 1.6 | 94.7 ± 2.0 |
| EDTA | 91.6 ± 3.1 | 87.3 ± 3.1 |
| SDS | 22.1 ± 1.5 | 14.7 ± 1.3 |
| Triton X-100 | 96.2 ± 2.2 | 103.9 ± 1.2 |
| Tween- 80 | 97.9 ± 2.8 | 108.8 ± 2.6 |
The purified XynAMG1 was assayed in the standard assay condition in the presence of 2 mM or 10 mM test agents. The xylanase activity measured in the absence of the test agent was set as 100%. All the values are means of three replications.