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. Author manuscript; available in PMC: 2015 Sep 21.
Published in final edited form as: J Mol Biol. 2015 Jan 12;427(6 0 0):1451–1463. doi: 10.1016/j.jmb.2015.01.003

Table 2.

Extent of reaction on insoluble substrates

Enzyme Avicel1,2 BMCC1,3
− β-glucosidase + β-glucosidase4 − β-glucosidase + β-glucosidase4
 FgCel5A 0.0222 ± 0.0017 0.0258 ± 0.0010 0.0288 ± 0.0009 0.0394 ± 0.0016
 FgC5A.3 0.0227 ± 0.0015 0.0277 ± 0.0014 0.0256 ± 0.0039 0.0437 ± 0.0029
1

Extents of reaction were measured using purified enzymes at 50°C according to the IUPAC standard protocol for β-1,4-endoglucanase on insoluble substrates. Reducing sugars formed were detected using standard DNS protocol and the extent of reaction was calculated based on the theoretical maximum of reducing ends based on substrate loading. Error represents the standard deviation from a minimum of three replicate experiments.

2

340 nmol enzyme per gram Avicel substrate.

3

2,500 nmol enzyme per gram BMCC substrate.

4

30 CBU per gram substrate.