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.