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. 2017 Jun 2;10:142. doi: 10.1186/s13068-017-0808-y

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© The Author(s) 2017

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. 3 — Characterization of four selected candidate GHases: Enzyme activities measured against pNP-substrates under different temperatures with constant pH and different pH with optimum temperature. Protein 1 with pNP-β-D-galactopyranoside a. Tm 50°C; pH 7.5; 68.6 U/mg and b. Tm 50°C; pH 8.0; 58.74 U/mg; Protein 2 with pNP-β-D-xylopyranoside c. Tm 50°C; pH 7.5; 117.8 U/mg and d. Tm 50°C; pH 9.0; 122.11 U/mg; Protein 2 with pNP-α-L-arabinopyranoside e. Tm 40°C; pH 7.5; 16.8 U/mg and f. Tm 40°C; pH 6.0; 16.62 U/mg; Protein 5 with pNP-α-D-glucopyranoside g. Tm 50°C; pH 7.5; 30.6 U/mg and h. Tm 50°C; pH 10.0; 102.54 U/mg; Protein 6 with pNP-α Dglucopyranoside i. Tm 40°C; pH 7.5; 6.97 U/mg and j. Tm 40°C; pH 10.0; 107.63 U/mg