Abstract
Enzymatic resolution and dynamic kinetic resolution of γ-hydroxy acid derivatives 1 have been investigated. Efficient kinetic resolution was obtained using Pseudomonas cepacia lipase in toluene ( E value ∼400). The combination of enzymatic kinetic resolution with a ruthenium-catalyzed racemization resulted in an efficient dynamic kinetic resolution. The use of a hydrogen source to depress ketone formation in the dynamic kinetic resolution yields the corresponding acetates in good yield (up to 93%) and enantioselectivity (up to 99%).
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