Biocatalytic characterization of a naturally immobilized lipase found in Araujia sericifera Brot. (Apocynaceae) latex

Lipase activity found in the insoluble fraction of Araujia sericifera Brot. (Apocynaceae) (ASL) latex, a native South American milkweed, was characterized by use of different test reactions and under different reaction conditions. In this context, hydrolytic lipase activity towards both natural and...

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Autores principales: Di Santo Meztler, Gabriela Paula, Fait, María Elisa, Foresti, M. Laura, Morcelle del Valle, Susana Raquel
Formato: Articulo
Lenguaje:Inglés
Publicado: 2014
Materias:
Ciencias Exactas
Biología
biocatálisis, lipasas, látex
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/74528
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-74528
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Exactas
Biología
biocatálisis, lipasas, látex
spellingShingle Ciencias Exactas
Biología
biocatálisis, lipasas, látex
Di Santo Meztler, Gabriela Paula
Fait, María Elisa
Foresti, M. Laura
Morcelle del Valle, Susana Raquel
Biocatalytic characterization of a naturally immobilized lipase found in Araujia sericifera Brot. (Apocynaceae) latex
topic_facet Ciencias Exactas
Biología
biocatálisis, lipasas, látex
description Lipase activity found in the insoluble fraction of Araujia sericifera Brot. (Apocynaceae) (ASL) latex, a native South American milkweed, was characterized by use of different test reactions and under different reaction conditions. In this context, hydrolytic lipase activity towards both natural and synthetic substrates and towards fatty acid esterifications was assayed at different temperatures, pH values, and biocatalyst loads. In the case of natural substrates (cottonseed oil), highest lipase activity was found at pH 8.5 and 60 °C. In the hydrolysis of synthetic substrates (p-nitrophenyl esters) the lipase showed preference for the lowest molecular-weight p-nitrophenyl ester assayed (butyrate). Results of the direct esterification of fatty acids of different chain length in organic media showed that esterification levels of up to 45% could be obtained in one hour of reaction. Activity results were compared with the activity shown by the commercial immobilized lipase Novozym 435 under defined reaction conditions. The high activity exhibited by ASL in the hydrolysis of natural substrates and particularly in the direct esterification of different fatty acids in organic medium, together with its high storage stability, suggests that this plant lipase is a promising biocatalyst for various biotechnological applications.
format Articulo
Articulo
author Di Santo Meztler, Gabriela Paula
Fait, María Elisa
Foresti, M. Laura
Morcelle del Valle, Susana Raquel
author_facet Di Santo Meztler, Gabriela Paula
Fait, María Elisa
Foresti, M. Laura
Morcelle del Valle, Susana Raquel
author_sort Di Santo Meztler, Gabriela Paula
title Biocatalytic characterization of a naturally immobilized lipase found in Araujia sericifera Brot. (Apocynaceae) latex
title_short Biocatalytic characterization of a naturally immobilized lipase found in Araujia sericifera Brot. (Apocynaceae) latex
title_full Biocatalytic characterization of a naturally immobilized lipase found in Araujia sericifera Brot. (Apocynaceae) latex
title_fullStr Biocatalytic characterization of a naturally immobilized lipase found in Araujia sericifera Brot. (Apocynaceae) latex
title_full_unstemmed Biocatalytic characterization of a naturally immobilized lipase found in Araujia sericifera Brot. (Apocynaceae) latex
title_sort biocatalytic characterization of a naturally immobilized lipase found in araujia sericifera brot. (apocynaceae) latex
publishDate 2014
url http://sedici.unlp.edu.ar/handle/10915/74528
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