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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