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Table 1 Enzymatic properties and kinetic values of purified XYL10C, XYL10C-ΔN, XylE, XynE2, and their mutants with beechwood xylan as the substrate

From: Insight into the functional roles of Glu175 in the hyperthermostable xylanase XYL10C-ΔN through structural analysis and site-saturation mutagenesis

Enzymes Optimal pH Optimal temperature (°C) Specific activity (U/mg) Km (mg/mL) kcat/Km (mL/s/mg)
XYL10C 4.5 85 3200 ± 131 0.54 ± 0.02 4900 ± 201
XYL10C-ΔN 4.0 80 8700 ± 403 0.71 ± 0.02 8800 ± 403
XYN10C-ΔN-E175Q 5.0 85 3600 ± 167 0.73 ± 0.02 4400 ± 198
XylE 5.0 70 620 ± 28 1.01 ± 0.03 490 ± 20
XylE-Q116E 5.5 70 2300 ± 108 0.81 ± 0.02 1200 ± 38
XynE2 8.0 65 870 ± 37 0.93 ± 0.03 1600 ± 39
XynE2-Q85E 7.0 65 1100 ± 49 0.72 ± 0.02 2200 ± 91
  1. Values represent mean ± SD (n = 3)