TY - JOUR
T1 - Research on the pig liver esterase (PLE)-catalyzed kinetic resolution of half-esters derived from prochiral diesters
AU - Noguchi, Naoyoshi
AU - Tsuna, Kazuhiro
AU - Nakada, Masahisa
N1 - Copyright:
Copyright 2013 Elsevier B.V., All rights reserved.
PY - 2013/4/15
Y1 - 2013/4/15
N2 - The pig liver esterase (PLE)-catalyzed kinetic resolution of half-esters derived from prochiral diesters is described. Generally, the PLE-catalyzed enantioselective hydrolysis of prochiral diesters affords the corresponding half-esters in high yield, because further hydrolysis of the half-esters does not typically occur. However, we found that some half-esters undergo PLE-catalyzed hydrolysis when they are gradually added to a PLE suspension in a potassium phosphate buffer at pH 8.0 via a syringe pump, leading to the kinetic resolution of the half-esters.
AB - The pig liver esterase (PLE)-catalyzed kinetic resolution of half-esters derived from prochiral diesters is described. Generally, the PLE-catalyzed enantioselective hydrolysis of prochiral diesters affords the corresponding half-esters in high yield, because further hydrolysis of the half-esters does not typically occur. However, we found that some half-esters undergo PLE-catalyzed hydrolysis when they are gradually added to a PLE suspension in a potassium phosphate buffer at pH 8.0 via a syringe pump, leading to the kinetic resolution of the half-esters.
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U2 - 10.1016/j.tetasy.2013.01.019
DO - 10.1016/j.tetasy.2013.01.019
M3 - Article
AN - SCOPUS:84876014548
SN - 0957-4166
VL - 24
SP - 357
EP - 361
JO - Tetrahedron Asymmetry
JF - Tetrahedron Asymmetry
IS - 7
ER -