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. 2016 Jul 20;9:147. doi: 10.1186/s13068-016-0560-8

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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. 2 — Enzymatic properties of the purified recombinant Bgl3A produced in P. pastoris using pNPG as the substrate. a Effect of pH on enzyme activities. b pH stability of Bgl3A after 1 h incubation at 37 °C. c Effect of temperature on enzyme activities. d Thermostability of Bgl3A at pH 4.5 and different temperatures up to 60 min. Each value in the panel represents the mean ± SD (n = 3)