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

Lipase-catalyzed enzymatic resolution of several new, exotic and variously substituted rac-(5-phenylfuran-2-yl)-beta-alanine ethyl esters was investigated. Given the structural instability of unsubstituted rac-(5-phenylfuran-2-yl)-beta-alanine ethyl ester, we used the stable hydrochloride salt of th...

Teljes leírás

Elmentve itt :
Bibliográfiai részletek
Szerzők: Nagy Botond
Galla Zsolt
Bencze László Csaba
Tosa Monica Ioana
Paizs Csaba
Forró Enikő
Fülöp Ferenc
Dokumentumtípus: Cikk
Megjelent: Wiley-VCH 2017
Sorozat:EUROPEAN JOURNAL OF ORGANIC CHEMISTRY
doi:10.1002/ejoc.201700174

mtmt:3266871
Online Access:http://publicatio.bibl.u-szeged.hu/12514
Leíró adatok
Tartalmi kivonat:Lipase-catalyzed enzymatic resolution of several new, exotic and variously substituted rac-(5-phenylfuran-2-yl)-beta-alanine ethyl esters was investigated. Given the structural instability of unsubstituted rac-(5-phenylfuran-2-yl)-beta-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 beta-amino ester hydrochlorides in NH4OAc buffer (20 mM, pH 5.8) at 30 degrees 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.
Terjedelem/Fizikai jellemzők:2878-2882
ISSN:1434-193X