| Title : Introducing a salt bridge into the lipase of Stenotrophomonas maltophilia results in a very large increase in thermal stability - Wu_2015_Biotechnol.Lett_37_403 |
| Author(s) : Wu JP , Li M , Zhou Y , Yang LR , Xu G |
| Ref : Biotechnol Lett , 37 :403 , 2015 |
|
Abstract :
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. |
| PubMedSearch : Wu_2015_Biotechnol.Lett_37_403 |
| PubMedID: 25257598 |
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 Lett
37 :403
Wu JP, Li M, Zhou Y, Yang LR, Xu G (2015)
Biotechnol Lett
37 :403