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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)