Chemoselective enzymatic preparation of N-hydroxyalkylacrylamides, monomers for hydrophilic polymer matrices
A lipase-catalyzed procedure is described for the preparation of N-hydroxyalkylacrylamides useful among a number of electrophoretical applications such as capillary and gel electrophoresis. The N-hydroxyalkylacrylamides were prepared through an aminolysis reaction of alkanolamines on ethyl acrylate....
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ftunibueairesbd:todo:paper_13811177_v39_n1-4_p50_Rustoy 2023-10-29T02:31:11+01:00 Chemoselective enzymatic preparation of N-hydroxyalkylacrylamides, monomers for hydrophilic polymer matrices Rustoy, E.M. Baldessari, A. https://hdl.handle.net/20.500.12110/paper_13811177_v39_n1-4_p50_Rustoy unknown http://hdl.handle.net/20.500.12110/paper_13811177_v39_n1-4_p50_Rustoy info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar Chemoselectivity Electrophoresis Lipase Substituted acrylamides Enzyme kinetics Enzymes Hydrophilicity Monomers Reaction kinetics Chemoselective enzymatic preparation N-hydroxyalkylacrylamides Nitrogen compounds acrylamide derivative polymer triacylglycerol lipase aminolysis article Candida antarctica catalysis chemical reaction enzyme degradation gel electrophoresis purification room temperature JOUR ftunibueairesbd https://doi.org/20.500.12110/paper_13811177_v39_n1-4_p50_Rustoy 2023-10-05T01:41:14Z A lipase-catalyzed procedure is described for the preparation of N-hydroxyalkylacrylamides useful among a number of electrophoretical applications such as capillary and gel electrophoresis. The N-hydroxyalkylacrylamides were prepared through an aminolysis reaction of alkanolamines on ethyl acrylate. The reaction was catalyzed by Candida antarctica lipase. The addition of radical inhibitors improved chemoselectivity and amides were obtained in high yield and purity at room temperature. © 2006 Elsevier B.V. All rights reserved. Journal/Newspaper Antarc* Antarctica Biblioteca Digital FCEN-UBA (Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires) |
institution |
Open Polar |
collection |
Biblioteca Digital FCEN-UBA (Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires) |
op_collection_id |
ftunibueairesbd |
language |
unknown |
topic |
Chemoselectivity Electrophoresis Lipase Substituted acrylamides Enzyme kinetics Enzymes Hydrophilicity Monomers Reaction kinetics Chemoselective enzymatic preparation N-hydroxyalkylacrylamides Nitrogen compounds acrylamide derivative polymer triacylglycerol lipase aminolysis article Candida antarctica catalysis chemical reaction enzyme degradation gel electrophoresis purification room temperature |
spellingShingle |
Chemoselectivity Electrophoresis Lipase Substituted acrylamides Enzyme kinetics Enzymes Hydrophilicity Monomers Reaction kinetics Chemoselective enzymatic preparation N-hydroxyalkylacrylamides Nitrogen compounds acrylamide derivative polymer triacylglycerol lipase aminolysis article Candida antarctica catalysis chemical reaction enzyme degradation gel electrophoresis purification room temperature Rustoy, E.M. Baldessari, A. Chemoselective enzymatic preparation of N-hydroxyalkylacrylamides, monomers for hydrophilic polymer matrices |
topic_facet |
Chemoselectivity Electrophoresis Lipase Substituted acrylamides Enzyme kinetics Enzymes Hydrophilicity Monomers Reaction kinetics Chemoselective enzymatic preparation N-hydroxyalkylacrylamides Nitrogen compounds acrylamide derivative polymer triacylglycerol lipase aminolysis article Candida antarctica catalysis chemical reaction enzyme degradation gel electrophoresis purification room temperature |
description |
A lipase-catalyzed procedure is described for the preparation of N-hydroxyalkylacrylamides useful among a number of electrophoretical applications such as capillary and gel electrophoresis. The N-hydroxyalkylacrylamides were prepared through an aminolysis reaction of alkanolamines on ethyl acrylate. The reaction was catalyzed by Candida antarctica lipase. The addition of radical inhibitors improved chemoselectivity and amides were obtained in high yield and purity at room temperature. © 2006 Elsevier B.V. All rights reserved. |
format |
Journal/Newspaper |
author |
Rustoy, E.M. Baldessari, A. |
author_facet |
Rustoy, E.M. Baldessari, A. |
author_sort |
Rustoy, E.M. |
title |
Chemoselective enzymatic preparation of N-hydroxyalkylacrylamides, monomers for hydrophilic polymer matrices |
title_short |
Chemoselective enzymatic preparation of N-hydroxyalkylacrylamides, monomers for hydrophilic polymer matrices |
title_full |
Chemoselective enzymatic preparation of N-hydroxyalkylacrylamides, monomers for hydrophilic polymer matrices |
title_fullStr |
Chemoselective enzymatic preparation of N-hydroxyalkylacrylamides, monomers for hydrophilic polymer matrices |
title_full_unstemmed |
Chemoselective enzymatic preparation of N-hydroxyalkylacrylamides, monomers for hydrophilic polymer matrices |
title_sort |
chemoselective enzymatic preparation of n-hydroxyalkylacrylamides, monomers for hydrophilic polymer matrices |
url |
https://hdl.handle.net/20.500.12110/paper_13811177_v39_n1-4_p50_Rustoy |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
http://hdl.handle.net/20.500.12110/paper_13811177_v39_n1-4_p50_Rustoy |
op_rights |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar |
op_doi |
https://doi.org/20.500.12110/paper_13811177_v39_n1-4_p50_Rustoy |
_version_ |
1781067027373359104 |