TABLE 2.
Effects of metal ions and inhibitors on activity of the protease of strain 1A02591.
| Metal ion (2 mM) | Relative activitya (%) | Metal ion (2 mM) | Relative activitya (%) | Inhibitorsb (2 mM) | Residual activityc (%) |
| Control | 100.00 | Mn2+ | 120.22 ± 7.59 | Control | 100.00 |
| Ca2+ | 99.11 ± 5.18 | Ba2+ | 98.55 ± 0.17 | PMSF | 54.54 ± 2.55 |
| Li+ | 104.86 ± 7.21 | Fe2+ | 76.79 ± 3.41 | EDTA | 51.42 ± 3.59 |
| K+ | 97.80 ± 2.05 | Zn2+ | 83.20 ± 3.52 | EGTA | ND |
| Mg2+ | 96.02 ± 1.90 | Sr2+ | 102.17 ± 1.70 | o-P | 31.99 ± 2.67 |
| Cu2+ | 72.32 ± 6.46 | Co2+ | 85.87 ± 4.31 | ||
| Ni2+ | 57.14 ± 3.21 | Sn2+ | 101.87 ± 1.79 |
a The protease activity was measured at 70°C and pH 7.5 with casein as the substrate. The activity (298.25 ± 18.33 U/mL) of the protease without any metal ion was used as a control (100%). b PMSF, phenylmethylsulfonyl fluoride; EDTA, ethylene diamine tetraacetic acid; EGTA, ethylene glycol tetraacetic acid; o-P, o-phenanthroline. c The residual activity of the protease was measured at 70°C and pH 7.5 with casein as the substrate after the protease was incubated with an inhibitor at 4°C for 60 min. The activity (298.25 ± 18.33 U/mL) of the protease without any inhibitor was used as the control (100%). The data represent the mean ± SD of three experimental repeats. ND means that the enzyme activity was not detectable.