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Table 1 Kinetic parameters of single domain variants of BoCE6–CE1 and FjCE6–CE1, where activity could be detected

From: Multimodular fused acetyl–feruloyl esterases from soil and gut Bacteroidetes improve xylanase depolymerization of recalcitrant biomass

EnzymeSubstrateKM (mM)kcat (s−1)kcat/KM (s−1 mM−1)
FjCE6pNP-Ac6.9 ± 2.557 ± 128.3 ± 3.5
4-MU-Ac0.15 ± 0.026.7 ± 0.243.4 ± 4.4
FjCE1pNP-Ac0.95 ± 0.145.6 ± 0.35.9 ± 0.9
4-MU-Ac0.07 ± 0.010.61 ± 0.038.7 ± 1.7
MFA0.11 ± 0.022.5 ± 0.223.1 ± 4.5
MSA0.14 ± 0.021.8 ± 0.113.0 ± 2.2
MCA0.34 ± 0.100.83 ± 0.142.7 ± 1.0
MpCA0.39 ± 0.121.5 ± 0.33.9 ± 1.4
BoCE6pNP-Ac1.8 ± 0.236.0 ± 2.220.1 ± 2.7
4-MU-Ac0.027 ± 0.0061.2 ± 0.142.8 ± 10.0
BoCE1pNP-Ac1.4 ± 0.10.70 ± 0.020.50 ± 0.04
4-MU-Ac0.04 ± 0.010.28 ± 0.017.1 ± 1.6
MFANot saturable up to 0.3 mM0.011 ± 3 × 10−4
MSANot saturable up to 0.3 mM0.043 ± 0.017
  1. All constructs were assayed on the full range of acetyl- and feruloyl esterase substrates (pNP-Ac, 4-MU-Ac, MFA, MSA, MCA and MpCA). Results are presented as the average of three experiments with standard errors. Data were fitted to the Michaelis–Menten equation using OriginPro software. For reactions that could not be saturated with substrate, kcat/Km was determined using linear regression