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Table 4 Enzyme kinetic parameters for cel12B, cel8C, and peh28a

From: Molecular and biochemical characterization of recombinant cel12B, cel8C, and peh28 overexpressed in Escherichia coli and their potential in biofuel production

Enzyme Substrate V bmax (µmol/ml/min) K cm (mg/ml) k dcat (s−1) k cat/K em (ml/mg/s)
cel12B CMC 2.4 ± 0.2 19 ± 3 2.7 ± 0.2 0.14 ± 0.03
cel8C CMC 39 ± 4 35 ± 6 85 ± 9 2.5 ± 0.7
peh28 Polygalacturonic acid 2.0 ± 0.5 0.87 ± 0.29 4.2 ± 1.0 4.9 ± 2.8
  1. aThe parameters were determined at 40 °C and pH 5.0 for peh28 using 0.05–0.55 mg/ml polygalacturonic acid and at 45 °C and pH 5.0 for cel12B and cel8C using 1–40 mg/ml CMC. Parameters are given as a mean of triplicates ± SE
  2. bMaximum velocity (at substrate saturation)
  3. cMichaelis–Menten constant (half-saturation constant)
  4. dTurnover number (enzyme concentration-independent specific rate at saturation)
  5. eCatalytic efficiency (specificity constant)