Skip to main content
. 2014 Jun 18;5:281. doi: 10.3389/fmicb.2014.00281

Table 5.

Description of the characterized β-1,4-xylanases isolated from the culture broth of a M. thermophila C1 mutant strain.

Enzyme CAZy module MW-monomer (kDa) pHopt Topt (°C) pI Gene References
Xyn10A GH10 42/31* 5.5–7.0 65–70 7.8/8.9 xyl1 Ustinov et al., 2008; van Gool et al., 2012
Xyn10B GH10 57/46* 5.5–7.0 80–85 4.4/4.3 xyl3 Ustinov et al., 2008; van Gool et al., 2012
Xyn10C GH11 40 5.0 80 4.8 xyl4 Ustinov et al., 2008
Xyn11A GH11 24 6.5 70 7.9 xyl2 Ustinov et al., 2008
Xyn11B GH11 23 6.0–6.5 65–70 8.4 xyl6 Ustinov et al., 2008
Xyn11C GH11 22 4.5 65 6.7 xyl5 Ustinov et al., 2008
Xyl7 GH11 22/30* 5.5–6.5 50–60 7.3/7.6 xyl7 van Gool et al., 2013
Xyl8 GH11 22 5.5–6.0 50–65 6.2 xyl8 van Gool et al., 2013

They display optimal activity at temperatures between 50 and 70 °C, increasing fungi's hydrolytic efficiency in various temperatures. Marked proteins

(*)

were isolated in two different forms, with (high molecular weight enzyme) or without CBM (low molecular weight enzyme).