Lipase-promoted kinetic resolution of racemic, P-chiral hydroxymethylphosphonates and phosphinates
摘要:
Lipase-mediated acetylation of racemic P-chiral hydroxymethylphosphonates and phosphinates, and hydrolysis of their O-acetyl derivatives have been conducted under kinetic resolution conditions to give the enantiomerically enriched title products with up to 92% ee. Their absolute configuration has been determined by means of chemical correlation and CD measurements. (C) 1998 Elsevier Science Ltd. All rights reserved.
Enzymatic reactions in ionic liquids: lipase-catalysed kinetic resolution of racemic, P -chiral hydroxymethanephosphinates and hydroxymethylphosphine oxides
Lipase-mediated acetylation of racemic P-chiral hydroxymethanephosphinates and hydroxymethylphosphine oxides was performed in ionic liquids under kinetic resolution conditions. Lipase AK (Amano) and lipase from Pseudomonas fluorescens (Fluka) were up to six times more enantioselective in BMIM-PF6, solutions than in common organic solvents. On the contrary, the analogous reactions performed in BMIM-BF4, were practically non-stereoselective. (C) 2002 Published by Elsevier Science Ltd.