Enzymatic Resolution and Separation of Secondary Alcohols Based on Fatty Esters as Acylating Agents

The enzymatic resolution of rac-1-phenylethanol using ethyl myristate as acylating agent and solvent and Candida antarctica lipase B (CAL-B) as biocatalyst was demonstrated with catalyst and medium reuse. Both enantiomers of 1-phenylethanol were isolated by sequential enzymatic reactions and product distillations. From the first enzymatic reaction, (S)-1-phenylethanol was isolated with a 41% yield and 80% enantiomeric excess, and from the second enzymatic reaction, (R)-1-phenylethanol was isolated with a 56% yield and 63% enantiomeric excess.