Abstract
Methyl N-acetyl phenylserinates (1, 2), methyl N-acetyl nitrophenylserinates (3, 4), and methyl N-benzoyl threoninates (5, 6) were resolved conveniently into the enantiomers with high optical purities by enzymatic hydrolysis in the presence of α-chymotrypsin, subtilisin, or bromelain. The threo and erythro forms were treated separately and the latter form was usually more reactive. Chymotrypsin and subtilisin are highly specific for the enantiomer having the same configuration on carbon-2 (S) as the natural standard amino acids. In contrast, bromelain shows the reverse specificity on phenylserine derivatives. This is a notable exception to the usual S-stereospecificity pattern of proteases. Keywords: enzymatic hydrolysis, resolution of amino acids.
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