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Table 3 Effects of different metal ions on the activity of CscA

From: Systematic unravelling of the inulin hydrolase from Bacillus amyloliquefaciens for efficient conversion of inulin to poly-(γ-glutamic acid)

Metal ions Relative activity (%)
1 mM 10 mM
Nonea 100 ± 1 100 ± 2
EDTAb 99 ± 1 97 ± 1
ZnCl2 83 ± 1 76 ± 1
MnCl2 125 ± 1 131 ± 2
CaCl2 114 ± 1 117 ± 1
CoCl2 92 ± 1 84 ± 1
KCl 109 ± 2 115 ± 2
CuCl2 43 ± 2
AlCl3 102 ± 1 97 ± 2
NaCl 97 ± 1 92 ± 1
  1. The inulinase activity of EDTA-treated CscA was assayed in PBS buffer (1/15 M, pH 7.5) at 55 °C for 20 min after incubating of 1 mM or 10 mM various metal ions. Each value represents the mean of triplicate measurements and varied from the mean by not more than 10%
  2. aThe activity of purified CscA enzyme without EDTA treatment and metal ions addition was set as 100%
  3. bThe activity of purified CscA enzyme after EDTA treatment but without metal ions addition