147220-41-5Relevant articles and documents
Lipase-catalysed resolution of 3-(aryloxy)-1,2-propanediol derivatives - Towards an improved active site model of Pseudomonas cepacia lipase (Amano PS)
Theil,Lemke,Ballschuh,Kunath,Schick
, p. 1323 - 1344 (2007/10/02)
A variety of 3-(aryloxy)-1,2-propanediol derivatives with different substituents on the aromatic ring or at the primary hydroxy group were used as substrates in a kinetic resolution by transesterification with vinyl acetate catalysed by lipase from Pseudomonas cepacia (Amano PS). Derivatives with substituents in the para-position of the aromatic ring were accepted as substrates and resolved with high enantioselectivity. The corresponding derivatives with substituents in the ortho-position were much worse substrates for lipase PS or even non-substrates if the substituent was sufficiently space-filling as found for the tert-butyl, phenyl, benzyl or benzoyl residue. Otherwise, if the primary hydroxy group was substituted by unbranched long-chain acyl residues very good substrates were resulting. In contrast, derivatives with sterically crowded residues at the primary hydroxy group such as the pivaloyl, tert-butyldimethylsilyl, methansulfonyl, para-toluenesulfonyl or trityl groups were non-substrates for lipase PS.
Kinetic resolution of aliphatic 1,2-diols by a lipase-catalyzed sequential acetylation
Theil, Fritz,Weidner, Judith,Ballschuh, Sibylle,Kunath, Annamarie,Schick, Hans
, p. 305 - 306 (2007/10/02)
The kinetic resolution of 13 racemic aliphatic 1,2-diols (rac-1a-m) by means of a lipase-catalyzed sequential acetylation was investigated. The enantioselectivity of the 3-aryloxy-propane-1,2-diols rac-1a-k depends on the substitution pattern at the aryl ring.
