Proteases from Canavalia ensiformis: Active and Thermostable Enzymes with Potential of Application in Biotechnology

Table 4

Effects of cations on C. ensiformis extracts peptidase activity.

Residual activity (%)
Extract	Cation
	Mg^2+	Mn^2+	Zn^2+	Ca^2+
CE-A	63.4 ± 13.7	758.8 ± 2.1	854.0 ± 126.9	25.2 ± 10.4
CE-D	41.8 ± 9.3	1010.5 ± 189.6	1276.9 ± 9.4	187.98 ± 23.4
CE-P	41.3 ± 19.9	36.5 ± 32.6	275.7 ± 23.8	70.4 ± 5.6
CE-T	226.9 ± 14.4	0.0 ± 0.0	328.8 ± 40.8	274.4 ± 37.0
CE-CA	0.0 ± 0.0	0.0 ± 0.0	782.4 ± 8.3	106.3 ± 7.4
CE-RA	105.4 ± 8.3	167.7 ± 2.8	144.2 ± 26.4	121.5 ± 10.6
CE-SA	68.7 ± 8.8	0.0 ± 0.0	263.0 ± 104.8	0.0 ± 0.0

The extracts were preincubated with each cation for 30 min at room temperature. The remaining activity was assayed by incubation with 0.125 mM L-TAME. Values are the remaining activity of serine protease as percentage of the activity on L-TAME without compounds, measured as described in “Materials and Methods,” and represent the average of 3 separate experiments carried out in duplicate.