Abstract
The enzymatic optical resolution of racemic N-benzyl-3-pyrrolidinol (2) was investigated. It was found that only (R)-2 was acetylated by the lipase Amano P in yields of 50% and 100%e.e. Remaining (S)-alcohol 2 could be chemically inverted to (R)-acetate 3. A continuous reaction in a column reactor could be also applied to this optical resolution. After concentrating the eluted solution, the residue was subjected to the inversion reaction to provide (R)-acetate 3 in an 83% yield and 91%e.e. from the racemate.
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