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%).
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
