Novel carboxyl esterase preparations for the resolution of linalyl acetate

Biocatalytic resolution of the tertiary terpene alcohol (+/-)-linalool was accomplished via hydrolysis of its corresponding acetate ester using two hi ghly enantiospecific enzymes (E > 100). The latter were identified in a cru de cell-free extract of Rhodococcus ruber DSM 43338 and could be separated by (partial) protein purification. Since they showed opposite enantioprefer ence, they were termed (R)- and (S)-linalyl acetate hydrolase (LAH). The ac tivity and selectivity of the enzyme preparations was markedly dependent on the fermentation conditions.