Skip to main content

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