Therefore, we have turned our attention to an alternative approach to the kinetic resolution of chromanols 1d-q, namely, enzymatic hydrolysis of racemic acetates 3d-q. These derivatives were obtained via standard acetylation of alcohols 1dq using Ac2Opy and were purified by column chromatography before further enzymatic reactions, with yields of 81-98% (Scheme 4). Preliminary experiments with acetate 3d showed that porcine liver esterase (PLE) allowed achieving 50% conversion faster than all other enzymes studied (Table ; note the relatively high catalyst loading used). With these results in hands, we have applied the PLE-catalyzed hydrolysis protocol to all acetates 3d-q (Table ). As was anticipated, the reaction time increased with increasing the substituent size (see, for example, Entries 1-4 or 9-11). Notably, the presence of heteroatoms in the substituent(s) at the C-2 position decreased the reaction rate considerably (see Entries 5-7 and 12-14). Also, spirocyclic and (hetera)cycloalkyl-substituted substrates 3d-q of similar substituent nature had comparable hydrolysis rates (see Entries 2/9, 3/10, 4/11, 5/12, or 6/13).