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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.