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From cotyledons of Raphanus sativus (red radish) an esterase activity which catalyzes the hy­drolysis of sinapine into sinapic acid and choline has been isolated. The enzyme, which has a near absolute specificity, is not analogous with any esterase described in the literature. The reaction has a pH optimum of 8.5 and the apparent K m  is 1.95 × 10 -5  m. The enzyme is relatively insensi­tive to both physostigmine (eserine) {K i  = 1.73 × 10 -4  m) and neostigmine (K i  = 2 .1 3 × 10 -4  ᴍ). Diisopropyl fluorophosphate (DFP) showed no inhibition and diethyl p-nitrophenylphosphate (E 600) only a slight inhibitory effect at 10 -5  ᴍ, respectively. Choline (10 -2  ᴍ) was inhibitory but acetylcholine (10 -2  ᴍ) stimulated the enzyme activity.

Sinapine Esterase I. Characterization of Sinapine Esterase from Cotyledons of Raphanus sativus