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Bioresources and Bioprocessing

Table 1 Effects of metal ions on the enzymatic activity of the recombinant AcCR

From: Enzymatic characterization of a recombinant carbonyl reductase from Acetobacter sp. CCTCC M209061

Reagent

Concentration (mM)

Relative activity (%)

Control

 

100.0 ± 0.8

Mn2+

2

122.3 ± 0.4

5

119.9 ± 0.7

K+

2

110.6 ± 1.2

5

103.4 ± 0.8

Fe2+

2

106.7 ± 1.0

5

106.0 ± 2.9

Zn2+

2

94.8 ± 1.2

5

85.8 ± 1.3

Mg2+

2

115.7 ± 0.7

5

123.5 ± 2.4

Ba2+

2

100.8 ± 0.5

5

97.9 ± 1.7

Ca2+

2

116.7 ± 0.6

5

113.9 ± 1.0

Cu2+

2

43.0 ± 0.7

5

24.9 ± 0.7

Co2+

2

99.6 ± 2.1

5

113.8 ± 0.2

Hg2+

2

Nd

5

Nd

Ag+

2

Nd

5

Nd

  1. Reaction conditions: 0.5 mM NADH, 2 mL 50 mM citrate–phosphate buffer (pH 6.5) with different metal ions, and 5 mM 4′-chloroacetophenone were incubated for 10 min at 35 °C before adding 20 μL purified recombinant AcCR (about 0.008 mg of the purified enzyme), and recorded the changes of absorbance for 3 min
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