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. 2016 Jul 8;9:140. doi: 10.1186/s13068-016-0550-x

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© The Author(s) 2016

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 1 — pH-dependent relative activity of THSAbf (n = 4). Enzyme activity was measured by monitoring the release of pNP or reducing sugars at different pH values. Various buffer systems were utilized: citrate (pH 3–6), phosphate (pH 6–8), and citrate–phosphate (pH 5.5–6.5). Different substrates were tested. Filled diamonds pNP-Araf; open squares pNP-Xylp; open triangles LWAX. pH profiles for pNP-Araf, pNP- Xylp, and LWAX. 100 % activity was taken as the activity at the optimal pH for a given substrate (relative activity)