Promiscuous behavior of Rhizomucor miehei lipase in the synthesis of N-substituted β-amino esters

A mild and efficient procedure for the aza-Michael addition of amines to acrylates by using lipases as catalysts is reported. Various lipases, mono- and bifunctional amines, alkyl acrylates, and reaction parameters were studied. Under the optimal conditions, Rhizomucor miehei lipase showed high sele...

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Autores principales: Monsalve, Leandro Nicolás, Baldessari, Alicia
Publicado: 2012
Materias:
Amino esters
Enzyme catalysis
Michael addition
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1434193X_v_n6_p1164_Monsalve
http://hdl.handle.net/20.500.12110/paper_1434193X_v_n6_p1164_Monsalve
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_1434193X_v_n6_p1164_Monsalve
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spelling paper:paper_1434193X_v_n6_p1164_Monsalve2023-06-08T16:14:26Z Promiscuous behavior of Rhizomucor miehei lipase in the synthesis of N-substituted β-amino esters Monsalve, Leandro Nicolás Baldessari, Alicia Amino esters Enzyme catalysis Michael addition A mild and efficient procedure for the aza-Michael addition of amines to acrylates by using lipases as catalysts is reported. Various lipases, mono- and bifunctional amines, alkyl acrylates, and reaction parameters were studied. Under the optimal conditions, Rhizomucor miehei lipase showed high selectivity. It catalyzed the formation of the Michael monoadduct as the only product in high yield and purity. Moreover, when diamines were used as nucleophiles, the lipase catalyzed the addition of only one of the two amino groups, showing in this case high substrate specificity. This promiscuous and highly selective behavior displayed by Rhizomucor miehei lipase allowed us to obtain 22 N-substituted β-amino esters, 15 of them being new products. A mild and efficient enzymatic method for the aza-Michael addition of mono- and bifunctional amines to acrylates was developed. The high substrate specificity showed by Rhizomucor miehei lipase as the catalyst for this reaction was a key feature for obtaining various N-substituted β-amino esters in high yield and purity. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. Fil:Monsalve, L.N. 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. 2012 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1434193X_v_n6_p1164_Monsalve http://hdl.handle.net/20.500.12110/paper_1434193X_v_n6_p1164_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 Amino esters
Enzyme catalysis
Michael addition
spellingShingle Amino esters
Enzyme catalysis
Michael addition
Monsalve, Leandro Nicolás
Baldessari, Alicia
Promiscuous behavior of Rhizomucor miehei lipase in the synthesis of N-substituted β-amino esters
topic_facet Amino esters
Enzyme catalysis
Michael addition
description A mild and efficient procedure for the aza-Michael addition of amines to acrylates by using lipases as catalysts is reported. Various lipases, mono- and bifunctional amines, alkyl acrylates, and reaction parameters were studied. Under the optimal conditions, Rhizomucor miehei lipase showed high selectivity. It catalyzed the formation of the Michael monoadduct as the only product in high yield and purity. Moreover, when diamines were used as nucleophiles, the lipase catalyzed the addition of only one of the two amino groups, showing in this case high substrate specificity. This promiscuous and highly selective behavior displayed by Rhizomucor miehei lipase allowed us to obtain 22 N-substituted β-amino esters, 15 of them being new products. A mild and efficient enzymatic method for the aza-Michael addition of mono- and bifunctional amines to acrylates was developed. The high substrate specificity showed by Rhizomucor miehei lipase as the catalyst for this reaction was a key feature for obtaining various N-substituted β-amino esters in high yield and purity. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
author Monsalve, Leandro Nicolás
Baldessari, Alicia
author_facet Monsalve, Leandro Nicolás
Baldessari, Alicia
author_sort Monsalve, Leandro Nicolás
title Promiscuous behavior of Rhizomucor miehei lipase in the synthesis of N-substituted β-amino esters
title_short Promiscuous behavior of Rhizomucor miehei lipase in the synthesis of N-substituted β-amino esters
title_full Promiscuous behavior of Rhizomucor miehei lipase in the synthesis of N-substituted β-amino esters
title_fullStr Promiscuous behavior of Rhizomucor miehei lipase in the synthesis of N-substituted β-amino esters
title_full_unstemmed Promiscuous behavior of Rhizomucor miehei lipase in the synthesis of N-substituted β-amino esters
title_sort promiscuous behavior of rhizomucor miehei lipase in the synthesis of n-substituted β-amino esters
publishDate 2012
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1434193X_v_n6_p1164_Monsalve
http://hdl.handle.net/20.500.12110/paper_1434193X_v_n6_p1164_Monsalve
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AT baldessarialicia promiscuousbehaviorofrhizomucormieheilipaseinthesynthesisofnsubstitutedbaminoesters
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