Acylation of [beta]-Amino Esters and Hydrolysis of [beta]-Amido Esters: Candida antarctica LipaseA as a Chemoselective Deprotection Catalyst

N-Acylation by lipaseA from Candida antarctica (CAL-A) in ethyl butanoate was applied to the kinetic resolution of tert-butyl esters of 3-amino-3-phenylpropanoic acid (E>100), 3-amino-4-methylpentanoic acid (E>100) and 3-aminobutanoic acid (E=60) on 1.0-2.0m scale. With the N-acylated resoluti...

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Bibliographic Details
Published in:ChemCatChem 2016-03, Vol.8 (6), p.1226
Main Authors: Maenpaa, Harri, Kanerva, Liisa T, Liljeblad, Arto
Format: Article
Language:English
Online Access:Get full text
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Summary:N-Acylation by lipaseA from Candida antarctica (CAL-A) in ethyl butanoate was applied to the kinetic resolution of tert-butyl esters of 3-amino-3-phenylpropanoic acid (E>100), 3-amino-4-methylpentanoic acid (E>100) and 3-aminobutanoic acid (E=60) on 1.0-2.0m scale. With the N-acylated resolution products, the exceptional ability of CAL-A to hydrolyse amides and bulky tert-butyl esters was then studied. In all N-acylated tert-butyl esters, chemoselectivity favoured the amide bond cleavage. The tert-butyl ester bond was left intact with 3-amino-3-phenylpropanoate, whereas with 3-amino-4-methylpentanoate and 3-aminobutanoate the CAL-A-catalysed hydrolysis of tert-butyl ester followed the amide hydrolysis.
ISSN:1867-3880
1867-3899
DOI:10.1002/cctc.201501381