Introducing a salt bridge into the lipase of Stenotrophomonas maltophilia results in a very large increase in thermal stability

@article{Wu2014IntroducingAS,
  title={Introducing a salt bridge into the lipase of Stenotrophomonas maltophilia results in a very large increase in thermal stability},
  author={Jianping Wu and Mu Li and Yong Zhou and Li-rong Yang and Gang Xu},
  journal={Biotechnology Letters},
  year={2014},
  volume={37},
  pages={403-407}
}
High thermostability of enzymes is a prerequisite for their biotechnological applications. An organic solvent-tolerant and cold-active lipase, from the Stenotrophomonas maltophilia, was unstable above 40 °C in previous studies. To increase the enzyme stability, possible hydrogen-bond networks were simulated by the introduction of a salt bridge in a highly flexible region of the protein. Compared with the wild-type lipase, a mutant lipase (G165D and F73R) showed a >900-fold improvement in half… CONTINUE READING
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Rational stabilization of enzymes by computational redesign of surface charge-charge interactions.

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