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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 NaCl on the activity and stability of the mutants of H8. (A) Effect of NaCl on the activity of WT H8 and its mutants. The activities of H8 and its mutants were determined at different NaCl concentrations at their respective optimum temperatures. The activities of WT H8 (70.9 U/mg), R195E (65.6 U/mg), R203E (7.5 U/mg), R216E (82.6 U/mg), R236E (53.0 U/mg), and R263E (62.0 U/mg) in 0 M NaCl were taken as 100%, respectively. (B) Effect of NaCl on the stability of WT H8 and its mutants. The enzymes were incubated in buffers containing different NaCl concentrations at 0°C for 1 h, and the residual activity was measured at their optimum temperatures, respectively. The activities of WT H8 (68.6 U/mg), R195E (64.5 U/mg), R203E (6.7 U/mg), R216E (72.8 U/mg), R236E (48.8 U/mg), and R263E (61.0 U/mg) in 0 M NaCl were taken as 100%, respectively. The graphs show data from triplicate experiments (mean ± SD).