Lipase-catalysed resolution of 3-(aryloxy)-1,2-propanediol derivatives - Towards an improved active site model of Pseudomonas cepacia lipase (Amano PS)

Article abstract of DOI:10.1016/0957-4166(95)00166-M

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.