Chen, C.-S., Fujimoto, Y., Girdaukas, G. and Sih, C.J. (1982) Quantitative Analyses of Biochemical Kinetic Resolutions of Enantiomers. Journal of the American Chemical Society, 104, 7294-7299.
https://doi.org/10.1021/ja00389a064

has been cited by the following article:

• TITLE: Enzyme-Mediated Enantioselective Hydrolysis of Aliphatic Dicarboxylic Acid Diesters

  AUTHORS: Yuta Igawa, Hironobu Ise, Sakina Ichinoseki, Fumie Maeda, Ai Kobayashi, Kazutsugu Matsumoto

  KEYWORDS: Adipate, Enzymatic Hydrolysis, Glutarate, Lipase, Optically Active Alcohols

  JOURNAL NAME: Journal of Biomaterials and Nanobiotechnology, Vol.8 No.1, January 12, 2017

  ABSTRACT: The enzyme-mediated highly enantioselective hydrolysis of aliphatic dicarboxylic acid diesters has been developed. The racemic diesters were easily prepared by the coupling of racemic alcohols with dicarboxylic anhydrides followed by esterification or with dicarboxylic acids. In the cases of bis(1-phenylethyl) glutarate and bis(1-phenylethyl) adipate, the diesters which contained the dl- and meso-form diastereomers, were enantioselectively hydrolyzed by lipase from Candida antarctica (Novozym 435) in buffer at 30°C to afford the almost optically pure (R)-1-phenylethanol. On the other hand, the following chemical hydrolysis of the remaining (S, S)-diesters and (S)-monoesters gave the (S)-alcohol. Finally, both enantiomers were stoichiometrically obtained in about 100% isolated yield based on the racemic diesters. The enzymatic reaction was also applicable for the preparation of several optically active alcohols. In some cases, both the reactivities and enantioselectivities were quite different from those in the case of the corresponding simple acetates.