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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Publicado: 2006
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Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13811177_v39_n1-4_p50_Rustoy
http://hdl.handle.net/20.500.12110/paper_13811177_v39_n1-4_p50_Rustoy
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spelling paper:paper_13811177_v39_n1-4_p50_Rustoy2023-06-08T16:12:20Z Chemoselective enzymatic preparation of N-hydroxyalkylacrylamides, monomers for hydrophilic polymer matrices 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. 2006 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13811177_v39_n1-4_p50_Rustoy 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
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.
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
publishDate 2006
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13811177_v39_n1-4_p50_Rustoy
http://hdl.handle.net/20.500.12110/paper_13811177_v39_n1-4_p50_Rustoy
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