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Table 2 Steady-state kinetic parameters of CauloGA at 30°C, pH 5.0

From: Glucoamylase of Caulobacter crescentus CB15: cloning and expression in Escherichia coli and functional identification

Substrates

kcata(s-1)

Kma(mM)

kcat/Km(s-1mM-1)

Kib(mM)

Maltose

38.2 ± 0.94

0.87 ± 0.08

43.9

38.2 ± 1.11

Maltotriose

150 ± 4.37

0.16 ± 0.02

938

4.49 ± 0.31

Maltotetraose

155 ± 0.66

0.14 ± 0.004

1110

1.10 ± 0.06

Maltopentaose

122 ± 4.21

0.03 ± 0.008

4070

0.92 ± 0.04

Maltohexaose

125 ± 1.91

0.05 ± 0.004

2500

1.05 ± 0.08

Maltoheptaose

114 ± 4.57

0.04 ± 0.003

2850

1.25 ± 0.25

  1. akcat and Km values (means ± standard deviation) were obtained based on the results with maltose (0–4.5 mM), maltotriose (0–0.9 mM) and maltotetraose to maltoheptaose (0–0.36 mM) as the substrates. Experiments were performed in triplicate.
  2. bKi values (means ± standard deviation) were obtained based on the results with maltose to maltotetraose (0–18 mM) and with maltopentaose to maltoheptaose (0–9 mM) as the substrates. Experiments were carried out in triplicate.