Structural and Mechanistic Insights into the Improvement of the Halotolerance of a Marine Microbial Esterase by Increasing Intra- and Interdomain Hydrophobic Interactions.

@article{Li2017StructuralAM,
  title={Structural and Mechanistic Insights into the Improvement of the Halotolerance of a Marine Microbial Esterase by Increasing Intra- and Interdomain Hydrophobic Interactions.},
  author={Ping-Yi Li and Yi Zhang and Bin-Bin Xie and Yan-qi Zhang and Jie Hao and Yue Wang and Peng Wang and Chun-yang Li and Q Qin and Xi-ying Zhang and H Su and Mei Shi and Yu-Zhong Zhang and Xiu-lan Chen},
  journal={Applied and environmental microbiology},
  year={2017},
  volume={83 18}
}
Halotolerant enzymes are beneficial for industrial processes requiring high salt concentrations and low water activity. Most halophilic proteins are evolved to have reduced hydrophobic interactions on the surface and in the hydrophobic cores for their haloadaptation. However, in this study, we improved the halotolerance of a thermolabile esterase, E40, by increasing intraprotein hydrophobic interactions. E40 was quite unstable in buffers containing more than 0.3 M NaCl, and its kcat and… CONTINUE READING