Covalently Immobilized Lipases are Efficient Stereoselective Catalysts for the Kinetic Resolution of rac-(5-Phenylfuran-2-yl)-β-alanine Ethyl Ester Hydrochlorides

Botond Nagy, Zsolt Galla, László Csaba Bencze, Monica Ioana Toșa, Csaba Paizs, E. Forró, F. Fülöp

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Lipase-catalyzed enzymatic resolution of several new, exotic and variously substituted rac-(5-phenylfuran-2-yl)-β-alanine ethyl esters was investigated. Given the structural instability of unsubstituted rac-(5-phenylfuran-2-yl)-β-alanine ethyl ester, we used the stable hydrochloride salt of this rac-heteroaryl-3-aminopropanoic acid ethyl ester as potential substrate to increase the scope of the reaction. Optimization experiments revealed an efficient procedure for both analytical- and preparative-scale (S)-selective hydrolysis of several racemic β-amino ester hydrochlorides in NH4OAc buffer (20 mm, pH 5.8) at 30 °C. Enzymatic resolutions were performed with covalently bound lipase AK from Pseudomonas fluorescens and lipase PS from Burkholderia cepacia on Immobead T2-150 as catalyst. Seven out of eight new resolution products were successfully isolated and appropriately characterized.

Original languageEnglish
Pages (from-to)2878-2882
Number of pages5
JournalEuropean Journal of Organic Chemistry
Volume2017
Issue number20
DOIs
Publication statusPublished - Jan 1 2017

Keywords

  • Enzyme catalysis
  • Hydrolases
  • Hydrolysis
  • Kinetic resolution
  • β-Amino acid

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Organic Chemistry

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