Lipase-catalyzed synthesis and characterization of a novel linear polyamidoamine oligomer

A linear polyamidoamine oligomer was obtained by polymerization of ethyl acrylate and N-methyl-1,3-diaminopropane, catalyzed by the Candida antarctica lipase. Depending on the reaction conditions such as substrates concentration, solvent and enzyme:substrate ratio, the enzyme catalyzes the polymeriz...

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Autores principales:	Monsalve, Leandro Nicolás, Erra Balsells, Rosa, Baldessari, Alicia
Publicado:	2010
Materias:	Lipase-catalyzed Michael addition Polyamidoamine oligomer Addition reactions Environmental impact Enzymes Functional polymers Medical applications Oligomers Polymerization Substrates Biomedical applications Candida antarctica lipase Lipase-catalyzed synthesis Michael additions Polyamidoamine oligomers Polymerization reaction Substrates concentration Catalysis biomedical use catalyst chemical reaction environmental impact oligomer polymerization substrate
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00323861_v51_n14_p2998_Monsalve http://hdl.handle.net/20.500.12110/paper_00323861_v51_n14_p2998_Monsalve
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_00323861_v51_n14_p2998_Monsalve
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spelling	paper:paper_00323861_v51_n14_p2998_Monsalve2025-07-30T17:41:01Z Lipase-catalyzed synthesis and characterization of a novel linear polyamidoamine oligomer Monsalve, Leandro Nicolás Erra Balsells, Rosa Baldessari, Alicia Lipase-catalyzed Michael addition Polyamidoamine oligomer Addition reactions Environmental impact Enzymes Functional polymers Medical applications Oligomers Polymerization Substrates Biomedical applications Candida antarctica lipase Lipase-catalyzed Lipase-catalyzed synthesis Michael additions Polyamidoamine oligomers Polymerization reaction Substrates concentration Catalysis biomedical use catalyst chemical reaction environmental impact oligomer polymerization substrate A linear polyamidoamine oligomer was obtained by polymerization of ethyl acrylate and N-methyl-1,3-diaminopropane, catalyzed by the Candida antarctica lipase. Depending on the reaction conditions such as substrates concentration, solvent and enzyme:substrate ratio, the enzyme catalyzes the polymerization reaction or Michael adducts formation. The polymeric material, characterized by FTIR, 1H and 13C NMR and UV-MALDI-TOF-MS, shows low molecular weight and high monodispersity. The activity showed by C. antarctica lipase in the polymerization reaction is highly selective and allows to obtain a product with potential biomedical applications in mild condition reactions and low environmental impact. © 2010 Elsevier Ltd. Fil:Monsalve, L.N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Erra-Balsells, R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Baldessari, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2010 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00323861_v51_n14_p2998_Monsalve http://hdl.handle.net/20.500.12110/paper_00323861_v51_n14_p2998_Monsalve
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Lipase-catalyzed Michael addition Polyamidoamine oligomer Addition reactions Environmental impact Enzymes Functional polymers Medical applications Oligomers Polymerization Substrates Biomedical applications Candida antarctica lipase Lipase-catalyzed Lipase-catalyzed synthesis Michael additions Polyamidoamine oligomers Polymerization reaction Substrates concentration Catalysis biomedical use catalyst chemical reaction environmental impact oligomer polymerization substrate
spellingShingle	Lipase-catalyzed Michael addition Polyamidoamine oligomer Addition reactions Environmental impact Enzymes Functional polymers Medical applications Oligomers Polymerization Substrates Biomedical applications Candida antarctica lipase Lipase-catalyzed Lipase-catalyzed synthesis Michael additions Polyamidoamine oligomers Polymerization reaction Substrates concentration Catalysis biomedical use catalyst chemical reaction environmental impact oligomer polymerization substrate Monsalve, Leandro Nicolás Erra Balsells, Rosa Baldessari, Alicia Lipase-catalyzed synthesis and characterization of a novel linear polyamidoamine oligomer
topic_facet	Lipase-catalyzed Michael addition Polyamidoamine oligomer Addition reactions Environmental impact Enzymes Functional polymers Medical applications Oligomers Polymerization Substrates Biomedical applications Candida antarctica lipase Lipase-catalyzed Lipase-catalyzed synthesis Michael additions Polyamidoamine oligomers Polymerization reaction Substrates concentration Catalysis biomedical use catalyst chemical reaction environmental impact oligomer polymerization substrate
description	A linear polyamidoamine oligomer was obtained by polymerization of ethyl acrylate and N-methyl-1,3-diaminopropane, catalyzed by the Candida antarctica lipase. Depending on the reaction conditions such as substrates concentration, solvent and enzyme:substrate ratio, the enzyme catalyzes the polymerization reaction or Michael adducts formation. The polymeric material, characterized by FTIR, 1H and 13C NMR and UV-MALDI-TOF-MS, shows low molecular weight and high monodispersity. The activity showed by C. antarctica lipase in the polymerization reaction is highly selective and allows to obtain a product with potential biomedical applications in mild condition reactions and low environmental impact. © 2010 Elsevier Ltd.
author	Monsalve, Leandro Nicolás Erra Balsells, Rosa Baldessari, Alicia
author_facet	Monsalve, Leandro Nicolás Erra Balsells, Rosa Baldessari, Alicia
author_sort	Monsalve, Leandro Nicolás
title	Lipase-catalyzed synthesis and characterization of a novel linear polyamidoamine oligomer
title_short	Lipase-catalyzed synthesis and characterization of a novel linear polyamidoamine oligomer
title_full	Lipase-catalyzed synthesis and characterization of a novel linear polyamidoamine oligomer
title_fullStr	Lipase-catalyzed synthesis and characterization of a novel linear polyamidoamine oligomer
title_full_unstemmed	Lipase-catalyzed synthesis and characterization of a novel linear polyamidoamine oligomer
title_sort	lipase-catalyzed synthesis and characterization of a novel linear polyamidoamine oligomer
publishDate	2010
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00323861_v51_n14_p2998_Monsalve http://hdl.handle.net/20.500.12110/paper_00323861_v51_n14_p2998_Monsalve
work_keys_str_mv	AT monsalveleandronicolas lipasecatalyzedsynthesisandcharacterizationofanovellinearpolyamidoamineoligomer AT errabalsellsrosa lipasecatalyzedsynthesisandcharacterizationofanovellinearpolyamidoamineoligomer AT baldessarialicia lipasecatalyzedsynthesisandcharacterizationofanovellinearpolyamidoamineoligomer
_version_	1840326658831155200

Lipase-catalyzed synthesis and characterization of a novel linear polyamidoamine oligomer

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