Biocatalytic kinetic resolution of β-perfluoroalkyl alcohols catalysed by Candida antarctica lipase A

Primary objective was to evaluate the influence of various factors, including the choice of biocatalyst, solvent, and acylating agent, as well as the impact of substrate structure on reaction conversion and enantioselectivity. Of all the commercial lipases screened, only Candida antarctica lipase A (CalA) demonstrated significant catalytic activity under the mild reaction conditions. Subsequent optimisation revealed that hydrophobic solvents and, notably, vinyl acetate as a dual-role reagent, enhanced reaction efficiency and enantioselectivity. The study further established a structure-activity relationship, showing that the presence and position of aromatic ring substituents and the length of the perfluoroalkyl chain subtly but positively influenced enantioselectivity. While the enantiomeric ratios obtained were moderate (E-values up to 30), the findings lay a crucial foundation for future research.