Research Article

Protease from Aspergillus oryzae: Biochemical Characterization and Application as a Potential Biocatalyst for Production of Protein Hydrolysates with Antioxidant Activities

Table 4

The effects of various salts and compounds on the protease activity.

Ions and inhibitorsResidual activity (%)
0.05 mM0.5 mM5.0 mM
Control100.00 ± 4.57

ZnSO496.59 ± 7.6355.41 ± 3.8223.88 ± 2.44
MgSO497.10 ± 4.1397.77 ± 4.1097.21 ± 2.12
FeSO490.45 ± 5.0942.96 ± 3.44Undetected
MnSO4105.99 ± 4.6389.56 ± 4.6780.87 ± 5.89
CaCl295.03 ± 5.1192.73 ± 5.3193.96 ± 1.56
CuSO482.68 ± 2.8322.19 ± 0.6113.98 ± 3.53
NaCl99.39 ± 2.22103.13 ± 2.01100.29 ± 4.49
CoCl288.71 ± 0.6772.72 ± 4.51Undetected
(NH4)2SO4100.66 ± 4.0898.52 ± 3.3495.73 ± 3.00
Glutathione97.95 ± 3.9797.29 ± 3.22101.97 ± 3.36
Cysteine98.26 ± 3.9687.23 ± 2.7646.80 ± 2.29
KCl96.55 ± 4.9391.62 ± 4.4630.65 ± 4.77
Mg(NO3)298.01 ± 0.4697.38 ± 3.1694.31 ± 1.72
MnCl2101.74 ± 3.9392.17 ± 8.8073.83 ± 7.17
CaCO3101.65 ± 3.4196.99 ± 1.3652.01 ± 2.75
EDTA101.52 ± 2.02100.13 ± 3.4799.25 ± 3.56
Iodoacetamide79.98 ± 3.8763.79 ± 2.5133.20 ± 3.10
p-Chloromercuribenzoate98.89 ± 4.5597.52 ± 2.8694.66 ± 2.47
Sodium azide96.03 ± 0.2697.20 ± 1.5597.38 ± 5.20
N-Bromosuccinimide78.56 ± 3.7610.56 ± 2.125.10 ± 1.40
Urea96.73 ± 2.9994.70 ± 3.4392.58 ± 3.20

Results are presented as the mean () ± SD (standard deviation).