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...
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| Dokumentumtípus: | Cikk |
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Wiley-VCH
2017
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| Sorozat: | EUROPEAN JOURNAL OF ORGANIC CHEMISTRY
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| doi: | 10.1002/ejoc.201700174 |
| mtmt: | 3266871 |
| Online Access: | http://publicatio.bibl.u-szeged.hu/12514 |
| LEADER | 01954nab a2200277 i 4500 | ||
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| 001 | publ12514 | ||
| 005 | 20200310161653.0 | ||
| 008 | 171220s2017 hu o 0|| zxx d | ||
| 022 | |a 1434-193X | ||
| 024 | 7 | |a 10.1002/ejoc.201700174 |2 doi | |
| 024 | 7 | |a 3266871 |2 mtmt | |
| 040 | |a SZTE Publicatio Repozitórium |b hun | ||
| 041 | |a zxx | ||
| 100 | 1 | |a Nagy Botond | |
| 245 | 1 | 0 | |a Covalently Immobilized Lipases are Efficient Stereoselective Catalysts for the Kinetic Resolution of rac-(5-Phenylfuran-2-yl)-beta-alanine Ethyl Ester Hydrochlorides |h [elektronikus dokumentum] / |c Nagy Botond |
| 260 | |a Wiley-VCH |c 2017 | ||
| 300 | |a 2878-2882 | ||
| 490 | 0 | |a EUROPEAN JOURNAL OF ORGANIC CHEMISTRY | |
| 520 | 3 | |a 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. | |
| 700 | 0 | 1 | |a Galla Zsolt |e aut |
| 700 | 0 | 1 | |a Bencze László Csaba |e aut |
| 700 | 0 | 1 | |a Tosa Monica Ioana |e aut |
| 700 | 0 | 1 | |a Paizs Csaba |e aut |
| 700 | 0 | 1 | |a Forró Enikő |e aut |
| 700 | 0 | 1 | |a Fülöp Ferenc |e aut |
| 856 | 4 | 0 | |u http://publicatio.bibl.u-szeged.hu/12514/1/Nagy_et_al_2017_European_Journal_of_Organic_Chemistry_u.pdf |z Dokumentum-elérés |