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Table 2 Kinetic parameters of Xyl2

From: Structural and functional characterization of a highly stable endo-β-1,4-xylanase from Fusarium oxysporum and its development as an efficient immobilized biocatalyst

Activity Endo-β-(1,4)-xylanase β-d-xylosidase
Substrate RBB-xylan pNP-β-Xyl
SA (µmol min−1 mg−1)a Opt. pH K M (mM) Vmax (µM min−1) k cat (min−1) k cat/K M (mM−1 min−1) SA (µmol min−1 mg−1)b Opt. pH k cat/K M (mM−1 min−1)c
Xyl2 27.2 7.0 − 8.0 40 ± 13 2.9 ± 0.6 16.0 ± 1.6 (400 ± 2) × 10−3 0.19 6.0 (61 ± 3) × 10−3
  1. aSA, specific xylanase activity, calculated as μmol Remazol Brilliant Blue R liberated per mg of enzyme per minute at pH 8.0 and 40 °C
  2. b SA specific β-d-xylosidase activity, calculated as μmol pNP liberated per mg of enzyme per minute at pH 6.0 and 40 °C
  3. cThe k cat/K M ratio for the β-d-xylosidase activity was calculated directly from a progress curve