text: As with synthetic kinetic resolution procedures, enzymatic acylation kinetic resolutions have seen the broadest application in a synthetic context. Especially important has been the use of enzymatic kinetic resolution to efficiently and cheaply prepare amino acids. On a commercial scale, Degussa's methodology employing acylases is capable of resolving numerous natural and unnatural amino acids. The racemic mixtures can be prepared via Strecker synthesis, and the use of either porcine kidney acylase (for straight chain substrates) or an enzyme from the mold Aspergillus oryzae (for branched side chain substrates) can effectively yield enantioenriched amino acids in high (85-90%) yields. The unreacted starting material can be racemized in situ, thus making this a dynamic kinetic resolution.
  In addition, lipases are used extensively for kinetic resolution in both academic and industrial settings.
  Lipases have been used to resolve primary alcohols, secondary alcohols, a limited number of tertiary alcohols, carboxylic acids, diols, and even chiral allenes. Lipase from Pseudomonas cepacia (PSL) is the most widely used in the resolution of primary alcohols and has been used with vinyl acetate as an acylating agent to kinetically resolve the primary alcohols shown below.
  For the resolution of secondary alcohols, pseudomonas cepecia lipase (PSL-C) has been employed effectively to generate excellent ees of the (R')-enantiomer of the alcohol. The use of isopropenyl acetate as the acylating agent results in acetone as the byproduct, which is effectively removed from the reaction using molecular sieves.