Tertiary Structure and Characterization of a Glycoside Hydrolase Family 44 Endoglucanase from Clostridium acetobutylicum
Appl. Environ. Microbiol. Warner et al. 76: 338
Supplemental material
Files in this Data Supplement:
- Supplemental file 1 - Supplemental figure legends.
MS Word document, 42K. - Supplemental file 2 - Multiple sequence alignment of GH44 enzymes (Fig. S1).
JPEG Image file, 2.24 MB. - Supplemental file 3 - Enzyme activity in 0.1 M NaOAc buffer, pH 5.0, at 25°C on varying concentrations of CMC (Fig. S2a).
JPEG Image file, 434K. - Supplemental file 4 - Enzyme activity in 0.1 M NaOAc buffer, pH 5.0, at 25°C on varying concentrations of birch wood xylan (Fig. S2b).
JPEG Image file, 469K. - Supplemental file 5 - Enzyme activity in 0.1 M NaOAc buffer, pH 5.0, at 25°C on varying concentrations of larch wood xylan (Fig. S2c).
JPEG Image file, 456K. - Supplemental file 6 - Effect of temperature on enzyme activity in 2% (wt/vol) CMC and 0.1 M NaOAc buffer, pH 5.0 (Fig. S3).
JPEG Image file, 504K. - Supplemental file 7 - Effect of pH on enzyme activity at 25°C in 2% (wt/vol) CMC and 0.1 M NaOAc buffer (Fig. S4).
JPEG Image file, 413K. - Supplemental file 8 - Effect of temperature on enzyme thermostability in 10 mM HEPES buffer (Fig. S5).
JPEG Image file, 453K.
