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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