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Table 2 Effect of metal ions (10 mM) on the relative activities of the purified recombinant xylanases

From: Cooperation of hydrolysis modes among xylanases reveals the mechanism of hemicellulose hydrolysis by Penicillium chrysogenum P33

Metal ions

Relative activity (%)

Xyl1

Xyl2

Xyl3

Control

100.0 ± 0.9

100.0 ± 1.2

100.0 ± 0.5

Ca2+

94.3 ± 1.1

80.4 ± 4.8

89.2 ± 0.4

K+

109.4 ± 0.6

105.0 ± 1.1

105.3 ± 0.5

Ag+

17.5 ± 0.4

8.7 ± 1.0

5.0 ± 0.2

Pb2+

78.9 ± 0.3

43.8 ± 0.3

53.5 ± 0.7

Ni2+

100.1 ± 0.1

81.6 ± 0.3

98.2 ± 3.0

Mg2+

97.2 ± 0.7

84.0 ± 0.1

93.4 ± 1.1

Cu2+

54.7 ± 0.7

11.4 ± 0.4

14.2 ± 0.6

Co2+

103.6 ± 0.4

82.7 ± 0.6

86.4 ± 0.2

Na+

108.9 ± 0.8

102.6 ± 0.3

102.8 ± 1.1

Fe3+

95.7 ± 0.3

42.2 ± 0.3

67.2 ± 0.4

Zn2+

109.8 ± 0.2

81.7 ± 0.7

96.6 ± 0.2

Al3+

108.3 ± 0.2

61.9 ± 2.1

97.4 ± 0.1

  1. Experiments were carried out in the presence of 10 mM metal ions at optimal conditions (35 °C and pH 6.0 for Xyl1; 50 °C and pH 5.0 for Xyl2; 55 °C and pH 6.0 for Xyl3), using 1.0% beechwood xylan as substrate. The relative enzyme activity was calculated using the activity of the enzyme without any added metal ions as 100%
  2. The experiments were performed in duplicate, and the data are presented as the means ± standard deviations