Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
69716 | Journal of Molecular Catalysis B: Enzymatic | 2014 | 5 Pages |
•Solvent structure affects resolution performance of (R, S)-2-octanol by lipase.•Acyclic linear solvent resulted in efficient enantioselectivity and enzymatic activity.•Mixture of acetone and carbon tetrachloride was developed for enhancing enzymatic resolution.
In order to find a suitable reaction system for the enzymatic resolution of (R, S)-2-octanol, the effects of the molecular structure of the solvent on the enantioselectivity (E) and enzymatic activity of Yarrowia lipolytica lipase (YLL) immobilized onto magnetic nanoparticles were systematically analyzed. Both the E and enzymatic activity of the reaction in an acyclic, structurally linear solvent were higher than those in the corresponding branched chain solvent or cyclic solvent. In a mixed solvent system with acetone and carbon tetrachloride (v/v = 3:7), the immobilized YLL exhibited high enantioselectivity, activity, and reusability. The thermodynamic analysis showed that the enantiomer discrimination was enthalpy-driven at all temperatures tested. These results present new opportunities and challenges for understanding and intensifying the enzymatic resolution process of (R, S)-2-octanol by designing suitable solvent system.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slide