Acylation of β‐Amino Esters and Hydrolysis of β‐Amido Esters: Candida antarctica Lipase A as a Chemoselective Deprotection Catalyst

Abstract N‐Acylation by lipase A 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 1.0–2.0 m scale. With the N...

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Bibliographic Details
Published in:ChemCatChem
Main Authors: Mäenpää, Harri, Kanerva, Liisa T., Liljeblad, Arto
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 2016
Subjects:
Antarc*
Antarctica
Online Access:http://dx.doi.org/10.1002/cctc.201501381
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fcctc.201501381
https://onlinelibrary.wiley.com/doi/full/10.1002/cctc.201501381
Description
Summary:Abstract N‐Acylation by lipase A 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 1.0–2.0 m 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.

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