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, L.N., Kaniz Fatema, M., Nonami, H., Erra-Balsells, R., Baldessari, A.
Formato:	JOUR
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:	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	todo:paper_00323861_v51_n14_p2998_Monsalve
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spelling	todo:paper_00323861_v51_n14_p2998_Monsalve2023-10-03T14:45:14Z Lipase-catalyzed synthesis and characterization of a novel linear polyamidoamine oligomer Monsalve, L.N. Kaniz Fatema, M. Nonami, H. Erra-Balsells, R. Baldessari, A. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, L.N. Kaniz Fatema, M. Nonami, H. Erra-Balsells, R. Baldessari, A. 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.
format	JOUR
author	Monsalve, L.N. Kaniz Fatema, M. Nonami, H. Erra-Balsells, R. Baldessari, A.
author_facet	Monsalve, L.N. Kaniz Fatema, M. Nonami, H. Erra-Balsells, R. Baldessari, A.
author_sort	Monsalve, L.N.
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
url	http://hdl.handle.net/20.500.12110/paper_00323861_v51_n14_p2998_Monsalve
work_keys_str_mv	AT monsalveln lipasecatalyzedsynthesisandcharacterizationofanovellinearpolyamidoamineoligomer AT kanizfatemam lipasecatalyzedsynthesisandcharacterizationofanovellinearpolyamidoamineoligomer AT nonamih lipasecatalyzedsynthesisandcharacterizationofanovellinearpolyamidoamineoligomer AT errabalsellsr lipasecatalyzedsynthesisandcharacterizationofanovellinearpolyamidoamineoligomer AT baldessaria lipasecatalyzedsynthesisandcharacterizationofanovellinearpolyamidoamineoligomer
_version_	1807315006802362368

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

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