| 초록 |
The use of enzymes in organic solvents offers possibilities for new industrial application. However, the direct contact of organic solvent with enzyme can result in conformational change, which finally lead to deactivation and destabilization. For this reason, there have been numerous researches for the enhancement of enzyme activity and/or stability in organic solvents. Using the methods of directed evolution and site-directed mutagenesis, several successful results were reported. However, these methods are kinds of trial-and-error and hard to succeed. Therefore, a predictive method based on theoretical study is required. In present study, the difference between structure of the organo-philic enzymes (which are active and/or stable in the organic solvents) and the counterpart enzymes (the common enzyme) were analyzed using molecular simulation. The solvation free energy was employed as a key parameter for the comparative analysis and for the development of a new predictive simulation method. |
