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The Relationship Between Enhanced Enzyme Activity and Structural Dynamics in Ionic Liquids: a Combined Computational and Experimental Study
학술지 Physical Chemistry Chemical Physics, 16, 2944-2953 (2014)
저자명 Ho Shin Kim, Sung Ho Ha, Latsavongsakda Sethaphong, Yoon-Mo Koo and Yaroslava G. Yingling
Candida antarctica lipase B (CALB) is an efficient biocatalyst for hydrolysis, esterification, and polymerization
reactions. In order to understand how to control enzyme activity and stability we performed a combined
experimental and molecular dynamics simulation study of CALB in organic solvents and ionic liquids (ILs).
Our results demonstrate that the conformational changes of the active site cavity are directly related to
enzyme activity and decrease in the following order: [Bmim][TfO] > tert-butanol > [Bmim][Cl]. The entrance
to the cavity is modulated by two isoleucines, ILE-189 and ILE-285, one of which is located on the
a-10 helix. The a-10 helix can substantially change its conformation due to specific interactions with
solvent molecules. This change is acutely evident in [Bmim][Cl] where interactions of LYS-290 with
chlorine anions caused a conformational switch between a-helix and turn. Disruption of the a-10 helix
structure results in a narrow cavity entrance and, thus, reduced the activity of CALB in [Bmim][Cl].
Finally, our results show that the electrostatic energy between solvents in this study and CALB is
correlated with the structural changes leading to differences in enzyme activity.
이전글 Quantitative Analysis of the Three Main Genera in Effective Microorganisms Using qPCR
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