title: Porcine pancreatic lipase-catalized enantioselective hydrolysis of N-protected amino acid methyl-esters.
abstract: A preparative-scale enantioselective hydrolysis of racemic methyl esters of several N-protected amino acid has been carried out by using crude porcine pancreatic lipase (Triacylglycerol lipase, EC 3.1.1.3) PPL as a hydrolytic enzyme. In all cases 50% of the racemic methyl ester was hydrolysed to the N-protected L-amino acid with high yield and high optical purity.Hydrolysis rates were very close related not only to the amino acid structure but also to the steric and/or electronic nature of the ester and N-protecting groups. Thus, the very convenient ester methyl group can be enantioselectively hydrolysed with PPL when N-protecting group is a carbonyl derivative, as it is the usual benzoyl group.
authors.affiliation: Department of Organic Chemistry, Córdoba University, Cordoba, Spain.
authors.forename: F M
authors.initials: FM
authors.lastname: Bautista
authors.forename: J M
authors.initials: JM
authors.lastname: Campelo
authors.forename: A
authors.initials: A
authors.lastname: García
authors.forename: D
authors.initials: D
authors.lastname: Luna
authors.forename: J M
authors.initials: JM
authors.lastname: Marinas