Abstract
As a result of screening several lipases, esterases and proteases for the ability to resolve ester derivatives of the racemic title compound rac -2, a lipase-catalyzed enantioselective hydrolysis of methyl ester rac -4 was developed on a 200 g scale. Exposure of the readily available racemic bicyclo[2.2.1]heptane derivative rac -4 to thermostable lipase SP 526 from Candida antarctica in buffered solution affords the desired (+)-enantiomer as (remaining) ester 4 with ≥ 99% enantiomeric excess in 82% yield.
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