Abstract
In this study, the stability of lipase in ethanol cosolvent was improved by computational optimization of ethanol-contacting surface residues. Preferred ethanol-contacting sites on the lipase surface were investigated by solvent mapping methods and their flexibility changes in ethanol solvent were predicted by molecular dynamics simulations. In silico saturated mutation was performed for target sites in flexible regions and mutants with fewer ethanol-contacts were selected for experimental validation. For mutants showed the improved stability in 50 % (v/v) ethanol solvent with comparable thermal stability and specific activity to the wild-type lipase. This computational strategy could be used as a practical tool to design organic solvent-stable mutants of industrial enzymes.
| Original language | English |
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| Journal | ACS National Meeting Book of Abstracts |
| State | Published - 2011 |
| Event | 241st ACS National Meeting and Exposition - Anaheim, CA, United States Duration: 27 Mar 2011 → 31 Mar 2011 |