Effects of organic solvents on immobilized lipase in pectin microspheres

Lipase from Brevibacillus agri 52 was found stable up to 90% diethylenglycol (DEG), glycerol (GLY), and 1,2 propanediol (1,2 PRO) at 37 °C for 1 h and the stability was reduced only approximately 20% after 12 h incubation, but in 40% dimethylsulfoxide (DMSO), lipase activity was stable only for 1 h....

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Detalles Bibliográficos
Autores principales: Costas, L., Bosio, Valeria Elizabeth, Pandey, A., Castro, Guillermo Raúl
Formato: Articulo
Lenguaje:Inglés
Publicado: 2008
Materias:
Bioquímica
Non-aqueous biocatalysis
Lipases
Enzyme stability
Solvent mixtures
Pectin gels
Gel microspheres
Enzyme encapsulation
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/152992
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-152992
record_format dspace
spelling I19-R120-10915-1529922023-05-16T04:06:37Z http://sedici.unlp.edu.ar/handle/10915/152992 issn:1559-0291 issn:0273-2289 Effects of organic solvents on immobilized lipase in pectin microspheres Costas, L. Bosio, Valeria Elizabeth Pandey, A. Castro, Guillermo Raúl 2008 2023-05-15T15:07:56Z en Bioquímica Non-aqueous biocatalysis Lipases Enzyme stability Solvent mixtures Pectin gels Gel microspheres Enzyme encapsulation Lipase from Brevibacillus agri 52 was found stable up to 90% diethylenglycol (DEG), glycerol (GLY), and 1,2 propanediol (1,2 PRO) at 37 °C for 1 h and the stability was reduced only approximately 20% after 12 h incubation, but in 40% dimethylsulfoxide (DMSO), lipase activity was stable only for 1 h. Inhibition of the biocatalysts with dimethylformamide (DMF) was detected at 20% solvent concentration. In water immiscible systems, the stability of lipase in n-hexane, n-tetradecane and n-heptane resembles the water activity, but in the presence of isobutanol, 1-hexanol, and butylbutirate, the stability was significantly reduced. Lipase 52 precipitates in the presence of 50% acetone or ethanol/ water mixtures, but enzymatic activity was partially recovered by adding 20% GLY, DEG, 1,2 PRO, or DMSO to the reaction mixture. Furthermore, by increasing DEG in 70% DMF/ DEG mixtures, the lipase activity was protected. Encapsulation of lipase in pectin gels cross-linked with calcium ions brings three to four times more enzymatic activity in 70% water miscible organic solvents compared to aqueous systems. Centro de Investigación y Desarrollo en Fermentaciones Industriales Articulo Articulo http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) application/pdf 578–586
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Bioquímica
Non-aqueous biocatalysis
Lipases
Enzyme stability
Solvent mixtures
Pectin gels
Gel microspheres
Enzyme encapsulation
spellingShingle Bioquímica
Non-aqueous biocatalysis
Lipases
Enzyme stability
Solvent mixtures
Pectin gels
Gel microspheres
Enzyme encapsulation
Costas, L.
Bosio, Valeria Elizabeth
Pandey, A.
Castro, Guillermo Raúl
Effects of organic solvents on immobilized lipase in pectin microspheres
topic_facet Bioquímica
Non-aqueous biocatalysis
Lipases
Enzyme stability
Solvent mixtures
Pectin gels
Gel microspheres
Enzyme encapsulation
description Lipase from Brevibacillus agri 52 was found stable up to 90% diethylenglycol (DEG), glycerol (GLY), and 1,2 propanediol (1,2 PRO) at 37 °C for 1 h and the stability was reduced only approximately 20% after 12 h incubation, but in 40% dimethylsulfoxide (DMSO), lipase activity was stable only for 1 h. Inhibition of the biocatalysts with dimethylformamide (DMF) was detected at 20% solvent concentration. In water immiscible systems, the stability of lipase in n-hexane, n-tetradecane and n-heptane resembles the water activity, but in the presence of isobutanol, 1-hexanol, and butylbutirate, the stability was significantly reduced. Lipase 52 precipitates in the presence of 50% acetone or ethanol/ water mixtures, but enzymatic activity was partially recovered by adding 20% GLY, DEG, 1,2 PRO, or DMSO to the reaction mixture. Furthermore, by increasing DEG in 70% DMF/ DEG mixtures, the lipase activity was protected. Encapsulation of lipase in pectin gels cross-linked with calcium ions brings three to four times more enzymatic activity in 70% water miscible organic solvents compared to aqueous systems.
format Articulo
Articulo
author Costas, L.
Bosio, Valeria Elizabeth
Pandey, A.
Castro, Guillermo Raúl
author_facet Costas, L.
Bosio, Valeria Elizabeth
Pandey, A.
Castro, Guillermo Raúl
author_sort Costas, L.
title Effects of organic solvents on immobilized lipase in pectin microspheres
title_short Effects of organic solvents on immobilized lipase in pectin microspheres
title_full Effects of organic solvents on immobilized lipase in pectin microspheres
title_fullStr Effects of organic solvents on immobilized lipase in pectin microspheres
title_full_unstemmed Effects of organic solvents on immobilized lipase in pectin microspheres
title_sort effects of organic solvents on immobilized lipase in pectin microspheres
publishDate 2008
url http://sedici.unlp.edu.ar/handle/10915/152992
work_keys_str_mv AT costasl effectsoforganicsolventsonimmobilizedlipaseinpectinmicrospheres
AT bosiovaleriaelizabeth effectsoforganicsolventsonimmobilizedlipaseinpectinmicrospheres
AT pandeya effectsoforganicsolventsonimmobilizedlipaseinpectinmicrospheres
AT castroguillermoraul effectsoforganicsolventsonimmobilizedlipaseinpectinmicrospheres
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