Title: Introducing a salt bridge into the lipase of Stenotrophomonas maltophilia results in a very large increase in thermal stability Wu JP, Li M, Zhou Y, Yang LR, Xu G Ref: Biotechnol Lett, 37:403, 2015 : PubMed
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 degrees 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-life at 50 degrees C, with the optimal activity-temperature increasing from 35 to 90 degrees C. Therefore, the hydrogen-bond strategy is a powerful approach for improving enzyme stability through the introduction of a salt bridge.
        
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Wu JP, Li M, Zhou Y, Yang LR, Xu G (2015) Introducing a salt bridge into the lipase of Stenotrophomonas maltophilia results in a very large increase in thermal stability Biotechnol Lett37: 403-7
Wu JP, Li M, Zhou Y, Yang LR, Xu G (2015) Biotechnol Lett37: 403-7