Table 3 Kinetic parameters for 5 CBZ-aa-aa substrates by carboxypeptidase CapA.

From: A new carboxypeptidase from Aspergillus niger with good thermostability, pH stability and broad substrate specificity

Substrates

Vmax (μmol L−1 mg−1 s−1)

Km (mmol L−1)

kcat (s−1)

kcat/Km (mmol L−1 s−1)

CBZ-Phe-Leu

912.7 ± 93.4

0.063 ± 0.01

11.74 ± 1.02

186.35 ± 16.7

CBZ-Gly-Ala

712.3 ± 83.2

0.24 ± 0.02

1.71 ± 0.08

7.13 ± 0.48

CBZ-Ala-Lys

698.7 ± 74.4

0.18 ± 0.03

2.32 ± 0.17

12.89 ± 1.13

CBZ-Pro-Gly

162.8 ± 14.5

1.17 ± 0.21

0.47 ± 0.02

0.4 ± 0.05

CBZ-Ala-Glu

108.1 ± 11.4

1.44 ± 0.09

0.18 ± 0.01

0.13 ± 0.01

  1. Assays were carried out in 0.1 mol L−1 disodium hydrogen phosphate-citric acid buffer, at pH 6.0, 45 °C.
  2. The concentrations of CapA range from 5 to 500 μmol L−1.
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