Artículo
Effects of Organic Solvents on Immobilized Lipase in Pectin Microspheres
Fecha de publicación:
12/2008
Editorial:
Humana Press
Revista:
Applied Biochemistry And Biotechnology
ISSN:
0273-2289
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
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.
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Licencia
Identificadores
Colecciones
Articulos(PROIMI)
Articulos de PLANTA PILOTO DE PROC.IND.MICROBIOLOGICOS (I)
Articulos de PLANTA PILOTO DE PROC.IND.MICROBIOLOGICOS (I)
Citación
Costas, Luciana; Bosio, Valeria Elizabeth; Pandey, A.; Castro, Guillermo Raul; Effects of Organic Solvents on Immobilized Lipase in Pectin Microspheres; Humana Press; Applied Biochemistry And Biotechnology; 151; 2-3; 12-2008; 578-586
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