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. 2015 Oct 22;26(2):193–202. doi: 10.1093/glycob/cwv092

Table II.

WXyn43 kinetic constants in comparison with reported data on β-xylosidases from XynB2 (Michlmayr et al. 2013) and LbX (Jordan et al. 2013), both from strains of L. brevis

β-Xylosidase Substrate Kinetic constant
kcat (s−1) KM (mM) kcat/KM (s−1 mM−1)
WXyn43
p-Nitrophenyl-β-d-xylopyranoside 258 ± 11 7.4 ± 1.1 34.9 ± 5.4
(1 → 4)-β-d-Xylobiose 961 ± 25 7.2 ± 0.5 133.5 ± 9.9
(1 → 4)-β-d-Xylotriose 900 ± 13 6.5 ± 0.3 138.5 ± 6.7
(1 → 4)-β-d-Xylotetraose 770 ± 7 17 ± 0.3 45.3 ± 0.9
XynB2a
p-Nitrophenyl-β-d-xylopyranoside 46 11 ± 1 4.1
(1 → 4)-β-d-Xylobiose 233 4.8 ± 0.4 48
LbXb
p-Nitrophenyl-β-d-xylopyranoside 73.4 ± 1.5 6.93 ± 0.26 10.6 ± 0.2
(1 → 4)-β-d-Xylobiose 407 ± 9 2.96 ± 0.24 138 ± 9
(1 → 4)-β-d-Xylotriose 235 ± 4 2.91 ± 0.15 80.8 ± 3.0
(1 → 4)-β-d-Xylotetraose 146 ± 4 2.40 ± 0.08 32.6 ± 1.2

aReactions performed at 37°C and pH 5.5 and b25°C and pH 6.0.