Immobilization of Thermomyces lanuginosus lipase by different techniques on Immobead 150 support: characterization and applications.
Appl Biochem Biotechnol
; 172(5): 2507-20, 2014 Mar.
Article
en En
| MEDLINE
| ID: mdl-24398921
Thermomyces lanuginosus lipase (TLL) was immobilized on native and modified Immobead 150, with epoxy groups removed by hydrolysis and oxidized to add aldehyde on its surface. Immobilizations on both supports were performed by adsorption, adsorption and cross-linking, covalent attachment, multipoint covalent attachment, and, for the modified support, multipoint covalent attachment using ethylenediamine. Biocatalysts were evaluated for thermal and solvent stabilities, and the best biocatalyst was also tested after incubation in ionic liquids and used in the synthesis of butyl butyrate and isoamyl butyrate. Multipoint covalent immobilized TLL on the native Immobead 150 (Emulti) showed a half-life of 5.32 h at 70 °C, being approximately 30 times more stable than its soluble form; it showed high stability in acetone, hexane, and isooctane. Its enzymatic activity was up to 40% when incubated in ionic liquids. Ester synthesis produced yields of esterification above 60% in 24 h. Of all immobilization protocols, the Emulti performed best concerning the thermal, solvent, and ionic liquids stabilities. Emulti was successfully applied to the synthesis of butyl butyrate and isoamyl butyrate, which are very important products for the food and beverage industries.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas Fúngicas
/
Enzimas Inmovilizadas
/
Lipasa
Idioma:
En
Revista:
Appl Biochem Biotechnol
Año:
2014
Tipo del documento:
Article
País de afiliación:
Brasil
Pais de publicación:
Estados Unidos