Porcine pancreatic lipase-catalized enantioselective hydrolysis of N-protected amino acid methyl-esters

F M Bautista; J M Campelo; A García; D Luna; J M Marinas

doi:10.1007/BF00806078

Porcine pancreatic lipase-catalized enantioselective hydrolysis of N-protected amino acid methyl-esters

Amino Acids. 1992 Feb;2(1-2):87-95. doi: 10.1007/BF00806078.

Authors

F M Bautista¹, J M Campelo, A García, D Luna, J M Marinas

Affiliation

¹ Department of Organic Chemistry, Córdoba University, Cordoba, Spain.

PMID: 24194275
DOI: 10.1007/BF00806078

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.