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. 2017 Mar 23;8:441. doi: 10.3389/fmicb.2017.00441

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Copyright © 2017 Zhang, Hao, Zhang, Chen, Xie, Shi, Zhou, Zhang and Li.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Effect of pH on the activity and stability of H8. (A) Effect of pH on the activity of H8. The activity was measured at 35°C in Britton–Robinson buffers ranging from pH 4.0 to 13.0. The highest activity at pH 10.0 (70.2 U/mg) was taken as 100%. (B) Effect of pH on the stability of H8. The enzyme was incubated in buffers ranging from pH 4.0 to 13.0 at 25°C for 1 h. The remaining activity was measured under optimal conditions. The highest activity at pH 8.0 (54.4 U/mg) was taken as 100%. The graphs show data from triplicate experiments (mean ± SD).