Development of a mixed solvent system for the efficient resolution of (R, S)-2-octanol catalyzed by magnetite-immobilized lipase

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.