Porcine pancreatic lipase-catalized enantioselective hydrolysis of N-protected amino acid methyl-esters
Bautista, F.M.; Campelo, J.M.; García, A.; Luna, D.; Marinas, J.M.
Amino Acids 2(1-2): 87-95
ISSN/ISBN: 0939-4451 PMID: 24194275 DOI: 10.1007/bf00806078
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 18.104.22.168) 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.