1993 Volume 57 Issue 8 Pages 1334-1337
We screened microorganisms for those that resolved a stereoisomer from rac-1-phenoxy-2-propyl acetate (PPAc). Several species of Nocardia and Rhodococcus hydrolyzed rac-PPAc to rac-1-phenoxy-2-propanol (PPol), and then selectively decomposed an isomer of PPol, leading to an accumulation of (R)-PPol. Several yeasts and bacteria hydrolyzed PPAc asymmetrically, affording (R)-PPol and the ester of (S)-PPol. An enzyme that catalyzed the asymmetric hydrolysis of PPAc was partially purified from Corynebacterium glutamicum ATCC 13059 and characterized. The enzymatic hydrolysis was highly specific for (R)-PPAc.
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