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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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_13811177_v39_n1-4_p50_Rustoy |
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todo:paper_13811177_v39_n1-4_p50_Rustoy2023-10-03T16:11:45Z Chemoselective enzymatic preparation of N-hydroxyalkylacrylamides, monomers for hydrophilic polymer matrices Rustoy, E.M. Baldessari, A. Chemoselectivity Electrophoresis Lipase Substituted acrylamides Electrophoresis Enzyme kinetics Enzymes Hydrophilicity Monomers Reaction kinetics Chemoselective enzymatic preparation Lipase N-hydroxyalkylacrylamides Substituted acrylamides Nitrogen compounds acrylamide derivative polymer triacylglycerol lipase aminolysis article Candida antarctica catalysis chemical reaction enzyme degradation gel electrophoresis hydrophilicity purification room temperature Candida antarctica 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_13811177_v39_n1-4_p50_Rustoy |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Chemoselectivity Electrophoresis Lipase Substituted acrylamides Electrophoresis Enzyme kinetics Enzymes Hydrophilicity Monomers Reaction kinetics Chemoselective enzymatic preparation Lipase N-hydroxyalkylacrylamides Substituted acrylamides Nitrogen compounds acrylamide derivative polymer triacylglycerol lipase aminolysis article Candida antarctica catalysis chemical reaction enzyme degradation gel electrophoresis hydrophilicity purification room temperature Candida antarctica |
| spellingShingle |
Chemoselectivity Electrophoresis Lipase Substituted acrylamides Electrophoresis Enzyme kinetics Enzymes Hydrophilicity Monomers Reaction kinetics Chemoselective enzymatic preparation Lipase N-hydroxyalkylacrylamides Substituted acrylamides Nitrogen compounds acrylamide derivative polymer triacylglycerol lipase aminolysis article Candida antarctica catalysis chemical reaction enzyme degradation gel electrophoresis hydrophilicity purification room temperature Candida antarctica Rustoy, E.M. Baldessari, A. Chemoselective enzymatic preparation of N-hydroxyalkylacrylamides, monomers for hydrophilic polymer matrices |
| topic_facet |
Chemoselectivity Electrophoresis Lipase Substituted acrylamides Electrophoresis Enzyme kinetics Enzymes Hydrophilicity Monomers Reaction kinetics Chemoselective enzymatic preparation Lipase N-hydroxyalkylacrylamides Substituted acrylamides Nitrogen compounds acrylamide derivative polymer triacylglycerol lipase aminolysis article Candida antarctica catalysis chemical reaction enzyme degradation gel electrophoresis hydrophilicity purification room temperature Candida antarctica |
| 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 |
JOUR |
| 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 |
http://hdl.handle.net/20.500.12110/paper_13811177_v39_n1-4_p50_Rustoy |
| work_keys_str_mv |
AT rustoyem chemoselectiveenzymaticpreparationofnhydroxyalkylacrylamidesmonomersforhydrophilicpolymermatrices AT baldessaria chemoselectiveenzymaticpreparationofnhydroxyalkylacrylamidesmonomersforhydrophilicpolymermatrices |
| _version_ |
1782027823416868864 |