Enzymatic Resolution of Ethyl α-Hydroxyphosphinates in a Modified Reaction Environment

The enzymatic resolutions of two racemic ethyl hydroxyalkane(P-phenyl)phosphinates were performed by both esterification and hydrolysis approaches. The first reaction was performed in anhydrous diisopropyl ether with triethylamine or pyridine as additives by using lipases from three different source...

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Bibliographic Details
Published in:Phosphorus, sulfur, and silicon and the related elements sulfur, and silicon and the related elements, 2010-08, Vol.185 (9), p.1915-1920
Main Authors: Majewska, Paulina, Lejczak, Barbara, Kafarski, Paweł
Format: Article
Language:English
Subjects:
Biocatalysis
enantioselectivity
hydroxyphosphinates
hydroxyphosphonates
lipases
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Summary:The enzymatic resolutions of two racemic ethyl hydroxyalkane(P-phenyl)phosphinates were performed by both esterification and hydrolysis approaches. The first reaction was performed in anhydrous diisopropyl ether with triethylamine or pyridine as additives by using lipases from three different sources (Candida cylindracea, Aspergillus niger, and Mucor javanicus). The increase in enantioselectivity was observed when NEt 3 was applied. The second reaction-lipase-catalysed hydrolysis of ethyl butyryloxyalkane(P-phenyl)phosphinates-was carried out by Candida cylindracea lipase in diisopropyl ether saturated with water or in aqueous solutions containing MgCl 2 , LiCl, or Triton X-100. The usefulness of biphasic systems consisting of diisopropyl ether and water or aqueous solution of MgCl 2 , LiCl, or Triton X-100 also were tested. The use of biphasic system in the presence of Triton X-100 resulted in the higher conversion of the substrates.
ISSN:1042-6507
1563-5325
DOI:10.1080/10426500903365595