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Covalently Immobilized Lipases are Efficient Stereoselective Catalysts for the Kinetic Resolution of rac ‐(5‐Phenylfuran‐2‐yl)‐β‐alanine Ethyl Ester Hydrochlorides
Author(s) -
Nagy Botond,
Galla Zsolt,
Bencze László Csaba,
Toșa Monica Ioana,
Paizs Csaba,
Forró Enikő,
Fülöp Ferenc
Publication year - 2017
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.201700174
Subject(s) - chemistry , kinetic resolution , lipase , hydrolysis , catalysis , pseudomonas fluorescens , organic chemistry , hydrochloride , substrate (aquarium) , covalent bond , candida antarctica , enzyme , enantioselective synthesis , oceanography , biology , geology , bacteria , genetics
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 NH 4 OAc buffer (20 m m , 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.