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Table 1 Effect on metal ions and chelating agent EDTA on hydrolytic activity. The enzyme purified without divalent cations added served as the control. The divalent metal salts or EDTA were added to this sample. The highest activity was observed when 1 mM ZnCl2 was added in all purification buffers and was set to 100%

From: Chaperone assisted recombinant expression of a mycobacterial aminoacylase in Vibrio natriegens and Escherichia coli capable of N-lauroyl-L-amino acid synthesis

Metal ion or chelating agent

Relative activity [%]

Specific activity [U/mg]

Control

51

65.2 (± 0.6)

1 mM EDTA

36

45.7 (± 3.6)

Purified with 1 mM ZnCl2

100

127.2 (± 0.6)

Purified with 1 mM ZnCl2, 1 mM EDTA added

96

122.7 (± 1.6)

1 mM ZnCl2

84

106.8 (± 8.6)

0.5 mM ZnCl2

81

103.5 (± 6.6)

0.1 mM ZnCl2

84

107.3 (± 5.8)

0.05 mM ZnCl2

85

107.9 (± 6.2)

0.01 mM ZnCl2

86

109.7 (± 4.0)

0.001 mM ZnCl2

65

82.3 (± 7.0)

1 mM MgSO4

47

60.3 (± 4.2)

1 mM MnCl2

48

60.9 (± 4.4)

1 mM CaCl2

50

63.8 (± 2.1)

1 mM CoCl2

52

66.0 (± 8.7)

1 mM NiSO4

43

54.4 (± 5.5)

1 mM FeSO4

42

52.9 (± 1.1)

1 mM CuSO4

40

51.2 (± 0.1)