Fig. 2

Domain structure of GH5_5A and enzymatic activity of its recombinant catalytic domain. A Predicted domain structure of the GH5_5A protein with boundaries of relevant domains (amino acid numbers from the start). B Degradation of chromogenic carboxymethyl cellulose (Azo-CM-Cellulose) by OaGH5_5E results in a blue supernatant after centrifugation. C Relative activity of two recombinant GH5_5 domains over a temperature range (mean and standard deviation; n = 6). D Relative activity of two recombinant GH5_5 domains over a pH range (mean and standard deviation; n = 6). E Michaelis-Menten kinetics of OaGH5_5P with CMC-Na as substrate (mean and standard deviation; n = 6). F Activity of the recombinant protein OaGH5_5E on 23 chromogenic carbohydrates as determined by absorbance measurements after the GlycoSpot assay. Two replicates and boiled enzyme (as negative control) have been used